Peran jaringan ikat intramuskuler di tekstur daging

1. Takanori NISHIMURA Takanori Nishimura

Article first published online: 3 NOV 2009 Pasal pertama kali diterbitkan online: 3 NOV 2009 DOI: 10.1111/j.1740-0929.2009.00696.x DOI: 10.1111/j.1740-0929.2009.00696.x 2009 The Author. 2009 Penulis. Journal compilation 2009 Japanese Society of Animal Science Jurnal kompilasi 2009 Jepang Society of Animal Science Kata kunci: collagen; kolagen; intramuscular connective tissue; intramuskular jaringan ikat; meat; daging; proteoglycan; proteoglycan; texture tekstur

ABSTRAK
Struktur, komposisi dan jumlah jaringan ikat intramuskuler (IMCT) sangat bervariasi antara otot, spesies dan keturunan, dan tentunya memberikan kontribusi terhadap tekstur daging. With animal growth, collagen crosslinks become more stable, and the structural integrity of IMCT increases. Dengan pertumbuhan hewan, crosslinks kolagen menjadi lebih stabil, dan integritas struktural meningkat IMCT. These changes increase the mechanical properties of IMCT, contributing to the toughening of meat. Perubahan ini meningkatkan sifat mekanik IMCT, memberikan kontribusi bagi ketangguhan daging. Intramuscular fat deposits, mainly in the perimysium between muscle fiber bundles, result in marbling. Lemak intramuskular deposito, terutama di perimysium antara bundel serat otot, mengakibatkan marmer. This causes the remodeling of IMCT structures and reduces the mechanical strength of IMCT, contributing to the tenderization of beef. Hal ini menyebabkan struktur IMCT renovasi dan mengurangi kekuatan mekanik IMCT, kontribusi terhadap keempukan daging sapi. The IMCT has been thought to be rather immutable compared to myofibrils during postmortem ageing of meat. IMCT telah dianggap agak berubah dibandingkan dengan myofibrils selama umur daging postmortem. However, recent studies have shown the disintegration of IMCT during postmortem ageing of meat and its relationship to tenderization of raw meat, although its contribution to cooked meat is still controversial. Namun, studi terbaru menunjukkan disintegrasi IMCT selama penuaan postmortem daging dan hubungannya dengan keempukan daging mentah, meskipun kontribusinya terhadap daging dimasak masih kontroversial. Given the large influence of IMCT on meat texture, further elucidations of molecular mechanisms which change the structural integrity of IMCT during chronological ageing of animals and postmortem ageing of meat are needed. Mengingat pengaruh besar IMCT pada tekstur daging, penjelasannya lebih lanjut dari mekanisme molekuler yang mengubah integritas struktural IMCT selama penuaan kronologis hewan dan postmortem penuaan daging diperlukan.

PENDAHULUAN
Tekstur adalah faktor yang paling penting dalam menentukan kualitas daging dari konsumen titik pandang ( Dransfield et al. 1984 ). Meat texture depends on the structures and composition of skeletal muscle, which is mainly composed of muscle fibers and surrounding intramuscular connective tissues (IMCT). Daging tekstur tergantung pada struktur dan komposisi otot rangka, yang terutama terdiri dari serat otot dan jaringan ikat sekitarnya intramuskular (IMCT). Muscle fibers consist of myofibrils, which are made of thin (actin) and thick (myosin) filaments. serat otot terdiri dari myofibrils, yang terbuat dari tipis (aktin) dan tebal (myosin) filamen. The structural integrity of myofibrils changes during postmortem ageing of meat, which contributes to the tenderness of aged meat ( Dransfield et al. 1984 ; Takahashi 1996 ). Integritas struktural perubahan postmortem myofibrils selama umur daging, yang berkontribusi pada usia kelembutan daging ( et al Dransfield 1984. ; Takahashi 1996 ). Myofibrils form so-called 'actomyosin toughness'. Myofibrils bentuk 'ketangguhan actomyosin' disebut. On the other hand, the amount, composition and structure of IMCT vary tremendously between muscles, species, breeds, and with animal age ( Bailey & Light 1989 ). Di sisi lain, jumlah, komposisi dan struktur IMCT sangat bervariasi antara otot, spesies, bibit, dan dengan umur binatang ( Bailey & Light 1989 ). Whilst IMCT contribution to meat texture is certainly important, it has been thought to be rather immutable compared to myofibrils during postmortem ageing of meat ( Purslow 2005 ). Sementara kontribusi IMCT untuk tekstur daging tentu penting, telah dianggap agak berubah dibandingkan dengan myofibrils selama umur daging postmortem ( Purslow 2005 ). Thus it is called 'background toughness'. Oleh karena itu disebut 'latar belakang ketangguhan'. In the present article, the structural changes in IMCT during development and postmortem ageing of meat and their contributions to meat texture are reviewed. Dalam pasal ini, perubahan struktural dalam IMCT selama pengembangan dan penuaan postmortem daging dan kontribusi mereka untuk tekstur daging ditinjau.

STRUKTUR DAN KOMPOSISI IMCT

Struktur dasar dan komposisi IMCT telah ditelaah oleh beberapa penulis sebelumnya ( Borg & Caulfield 1980 ; Bailey & Light 1989 ; McCormick 1994 ; Purslow 2002 ), sehingga hanya penjelasan singkat akan diberikan di sini sebagai latar belakang. The structural integrity of muscle fibers is maintained by three layers of IMCT: (i) the endomysium that surrounds individual skeletal muscle fibers, (ii) the perimysium that bundles a group of muscle fibers, and (iii) the epimysium that ensheathes the whole muscle. Integritas struktural dari serat otot dijaga oleh tiga lapisan IMCT: (i)

endomysium yang mengelilingi serat otot rangka individu, (ii) perimysium bahwa bundel sekelompok serat otot, dan (iii) epimysium bahwa ensheathes seluruh otot . These connective tissues are composed of cells and extracellular matrix (ECM), which is composed of collagen, proteoglycans (PGs) and glycoproteins. Ini jaringan penghubung terdiri dari sel dan matriks ekstraseluler (ECM), yang terdiri dari kolagen, proteoglikan (PG) dan glikoprotein. There are various types of collagen with tissue-specific distribution and unique functional properties. Ada berbagai jenis kolagen dengan distribusi jaringan-sifat fungsional yang spesifik dan unik. Skeletal muscle contains collagen types I, III, IV, V, VI, XII and XIV ( Nishimura et al. 1997 ; Listrat et al. 1999, 2000 ). otot rangka mengandung kolagen tipe I, III, IV, V, VI, XII dan XIV ( Nishimura et al 1997. ; Listrat et al 2000. 1999, ). The major types of collagen in skeletal muscle are type I and III ( Bailey & Light 1989 ), which align into a quarter-stagger array to form fibrils in tissues. Jenis utama kolagen dalam otot rangka tipe I dan III ( Bailey & Light 1989 ), yang align menjadi terhuyung-huyung-array kuartal untuk membentuk fibril pada jaringan. The endomysium is composed of sheaths which consist of collagen fibril networks, the perimysium is composed of sheets of collagen fibers (a bundle of collagen fibrils) which show a regular wavy pattern, and the epimysium is composed of thick sheets constructed of several layers which consist of collagen fibers ( Nishimura et al. 1994 ). endomysium ini terdiri dari selubung yang terdiri dari jaringan fibril kolagen, perimysium ini terdiri dari lembaran serat kolagen (seikat fibril kolagen) yang menunjukkan pola bergelombang yang teratur, dan epimysium ini terdiri dari lembaran tebal terbuat dari beberapa lapisan yang terdiri dari serat kolagen ( Nishimura et al 1994. ). The other principal component of the ECM is PG. Komponen utama lain dari ECM PG. This macromolecule is composed of a central core protein with covalently attached glycosaminoglycan (GAG) chains. makromolekul ini terdiri dari protein inti pusat dengan glikosaminoglikan kovalen terlampir (GAG) rantai. The GAG is a polymer of disaccharide repeats that are highly sulfated and negatively charged. GAG adalah polimer mengulang disakarida yang sangat sulfat dan bermuatan negatif. Some PGs have only a single or limited number of GAGs, whereas others have up to 100 GAG chains. Beberapa PG hanya memiliki satu nomor atau terbatas GAG, sementara yang lain memiliki hingga 100 rantai GAG. Typical GAGs attached to the core protein of PGs are chondroitin sulfate, dermatan sulfate, heparan sulfate and keratan sulfate. GAG khas melekat pada protein inti dari PG adalah kondroitin sulfat, sulfat dermatan, sulfat heparan dan keratan sulfat. The core proteins are highly variable in structure and size with a molecular weight of approximately 40,000350,000 ( Iozzo & Murdoch 1996 ). Protein inti sangat bervariasi dalam struktur dan ukuran dengan berat molekul sekitar 40,000-350,000 ( Iozzo & Murdoch 1996 ). Different GAG chains can be attached to the same core protein. rantai GAG yang berbeda dapat melekat pada protein inti yang sama. Decorin, a small leucine-rich PG (SLRP), regulates collagen fibrillogenesis ( Danielson et al. 1997 ) and plays an important role in the stabilization of collagen fibrils ( Scott & Thomlinson 1998 ). Decorin, PG leusin kaya kecil (SLRP), mengatur kolagen fibrillogenesis ( Danielson et al 1997. ) dan memainkan peran penting dalam stabilisasi fibril kolagen ( Scott & Thomlinson 1998 ). Decorin is identified in IMCT ( Eggen et al. 1994 ; Nakano et al. 1997 ), and plays an important role in morphogenesis of IMCT during bovine fetal development ( Nishimura et al. 2002 ). Decorin diidentifikasi dalam IMCT ( et al Eggen 1994. ; Nakano et al 1997. ), dan memainkan peran penting dalam morfogenesis dari IMCT selama perkembangan janin bovine ( Nishimura et al 2002. ). Decorin also plays important roles in the quiescence of muscle cells ( Nishimura et al. 2008a ) and muscle cell growth by modulating growth factors ( Miura et al. 2006 ; Zhu et al. 2007 ; Kishioka et al. 2008 ). Decorin juga memainkan peran penting dalam ketenangan sel otot ( Nishimura et al 2008a. ) dan pertumbuhan sel otot dengan modulasi faktor pertumbuhan ( Miura et al 2006. ; Zhu et al 2007. ; Kishioka et al 2008. ).

PERAN IMCT TEKSTUR DALAM DAGING

Kolagen adalah komponen utama IMCT. The total collagen content in bovine muscles varies from 1% to 15% of dry weight, while elastin is a smaller component varying from 0.6% to 3.7% ( Bendall 1967 ). Kandungan kolagen total pada otot sapi bervariasi dari 1% sampai 15% dari berat kering, sedangkan elastin adalah komponen kecil bervariasi dari 0,6% menjadi 3,7% ( Bendall 1967 ). Many researchers have attempted to clarify the relationship between collagen content and toughness of meat using a combination of organoleptic evaluation and some mechanical tests, but no clear relationship has been established. Banyak peneliti telah berusaha untuk memperjelas hubungan antara konten kolagen dan ketangguhan daging menggunakan kombinasi dari evaluasi organoleptik dan beberapa uji mekanis, tetapi tidak ada hubungan yang jelas telah ditetapkan. Some researchers suggested that the eating quality of meat does not correlate to collagen content ( Herring et al. 1967 ; Hunsley et al. 1971 ), while others showed that skeletal muscle rich in collagen is tougher than that with a low content of collagen ( Dransfield 1977 ; Light et al. 1985 ; Nishiumi et al. 1995 ). Beberapa peneliti menyarankan bahwa kualitas makan daging tidak berhubungan dengan konten kolagen ( Herring et al 1967. ; Hunsley et al 1971. ), sementara yang lain menunjukkan bahwa otot rangka kaya kolagen adalah lebih keras dari yang dengan kandungan rendah kolagen ( Dransfield 1977 ; Light et al 1985. ; et al Nishiumi 1995. ). Skeletal muscle, which shows a low compressive-force value, generally contains only a small amount of collagen. otot rangka, yang menunjukkan nilai-gaya tekan rendah, umumnya hanya berisi sejumlah kecil kolagen. As an exception, the pectoralis profundus muscle, which has a high collagen content, has a lower compressive-force value than that of gastrocnemius muscle, which has a low collagen content ( Bailey & Light 1989 ). Sebagai pengecualian, otot pectoralis profunda, yang memiliki kandungan kolagen yang tinggi, memiliki nilai tekan force lebih rendah dari otot gastrocnemius, yang memiliki kandungan kolagen rendah ( Bailey & Light 1989 ). It seems likely that textural properties of various skeletal muscles are due to not only the total collagen content but also to other factors. Agaknya sifat tekstur berbagai otot rangka karena tidak hanya konten total kolagen tetapi juga faktor-faktor lain. The relationship between heat-stability of collagen and meat tenderness has been investigated. Hubungan antara panasstabilitas kolagen dan kelembutan daging telah diteliti. Some researchers show that the correlation between the tenderness of cooked meat and the heat-solubility of collagen is relatively low ( Renand et al. 2001 ; Berge et al. 2003 ; Chambaz et al. 2003 ) or non-significant ( Young et al. 1994 ). Beberapa peneliti menunjukkan bahwa hubungan antara kelembutan daging dimasak dan panas-kelarutan kolagen relatif rendah ( Renand et al 2001. ; Berge et al 2003. ; et. al Chambaz 2003 ) atau non-signifikan ( Young et al. 1994 ). However, Nishiumi et al. (1995 ) reported a significant correlation between heatsolubility of collagen and toughness of raw pork using 8 classes of skeletal muscle in miniature pigs. Namun, Nishiumi et

al. (1995 ) melaporkan hubungan yang signifikan antara panas-kelarutan kolagen dan ketangguhan daging babi mentah menggunakan 8 kelas otot rangka pada babi miniatur. In addition, Torrescano et al. (2003 ) showed a high positive correlation between heat-insoluble collagen and Warner-Bratzler shear force (WBSF) of raw beef. Selain itu, Torrescano et al 2003. ( ) menunjukkan korelasi positif yang tinggi antara-larut kolagen panas dan Warner-Bratzler gaya geser (WBSF) daging sapi mentah. The heat-solubility of collagen depends on crosslinks ( Tanzer 1973 ). Shimokomaki et al. (1972 ) showed that there is a low correlation between the amount of oxo-imine crosslinks and eating quality of meat, while Light et al. (1985 ) showed that tender beef has fewer crosslinks in endomysial and perimysial collagen. Panas-kelarutan kolagen tergantung pada crosslinks ( Tanzer 1973 ). Shimokomaki et al 1972. ( ) menunjukkan bahwa ada korelasi yang rendah antara jumlah-imina crosslinks okso dan kualitas makan daging, sedangkan Light et al 1985. ( ) menunjukkan bahwa daging sapi tender telah crosslinks lebih sedikit kolagen endomysial dan perimysial. The correlation between the number of crosslinks per collagen molecule and meat tenderness among different muscles varies from relatively high ( Bailey & Light 1989 ) to low or non-significant values ( Avery et al. 1996 ). Korelasi antara jumlah crosslinks per molekul kolagen dan kelembutan daging di antara otot-otot yang berbeda bervariasi dari yang relatif tinggi ( Bailey & Light 1989 ) atau nonsignifikan nilai-nilai rendah ( Avery et al 1996. ). Recently, Lepetit (2007 ) showed the total amount of crosslinks present per volume of cooked meat is approximately proportional to the elastic modulus of collagenous fractions of connective tissue, suggesting the contribution of collagen crosslinks to meat toughness. Baru-baru ini, Lepetit (2007 ) menunjukkan jumlah crosslinks sekarang per volume daging dimasak kira-kira sebanding dengan modulus elastisitas dari fraksi collagenous jaringan penghubung, menunjukkan kontribusi crosslinks kolagen untuk ketangguhan daging. Collagen crosslinks may have an additive effect on toughening meat, although the correlation between collagen crosslinks and toughness of cooked meat is still controversial. crosslinks Kolagen mungkin memiliki efek aditif pada ketangguhan daging, meskipun hubungan antara crosslinks kolagen dan ketangguhan daging dimasak masih kontroversial. Over 90% of intramuscular collagen is located in the perimysium ( McCormick 1994 ). Lewis and Purslow (1990 ) demonstrated in cooked beef that the perimysial strands have higher tensile strength than junctions between the endomysium and the perimysium. Lebih dari 90% dari kolagen intramuskuler terletak di perimysium ( McCormick 1994 ). Lewis dan Purslow (1990 ) menunjukkan daging sapi dimasak bahwa untaian perimysial memiliki kekuatan tarik lebih tinggi daripada sambungan antara endomysium dan perimysium tersebut. These results suggest that the nature of the perimysium is one of the most important factors that determine the toughness of meat. Hasil ini menunjukkan bahwa sifat perimysium merupakan salah satu faktor yang paling penting yang menentukan ketangguhan daging. In fact, thicker perimysium is associated with reduced tenderness ( Swatland et al. 1995 ). Bahkan, perimysium tebal dikaitkan dengan mengurangi kelembutan ( et al Swatland 1995. ). We have shown that the thickness of the secondary perimysium contributes to the toughness of raw meat ( Liu et al. 1996 ). Kami telah menunjukkan bahwa ketebalan perimysium sekunder memberikan kontribusi terhadap faktor ketangguhan daging mentah ( Liu et al 1996. ). However, the correlations between the WBSF of cooked muscles and perimysial content or thickness are poor ( Brooks & Savell 2004 ). Purslow (1999 ) also showed that correlations between shear force values of meat cooked to 80C and perimysial thickness are low. Namun, korelasi antara WBSF otot dimasak dan konten perimysial atau ketebalan miskin ( Brooks & Savell 2004 ). Purslow (1999 ) juga menunjukkan bahwa korelasi antara nilai-nilai gaya geser daging dimasak sampai 80 C dan ketebalan perimysial rendah. Toughness of meat increases with temperature of cooking. Ketangguhan meningkat daging dengan suhu memasak. However, the strength of perimysial connective tissue increases in meat cooked up to 50C and decreases above this temperature ( Lewis & Purslow 1989 ). Namun, peningkatan kekuatan perimysial jaringan ikat pada daging dimasak sampai 50 C dan menurun di atas suhu ini ( Lewis & Purslow 1989 ). Even though the nature of perimysial connective tissue affects raw meat toughness, its contribution to cooked meat toughness is controversial, because the texture of raw meat is poorly related to cooked meat toughness ( Palka 2003 ). Meskipun sifat jaringan ikat perimysial mempengaruhi ketangguhan daging mentah, kontribusinya terhadap ketangguhan daging dimasak adalah kontroversial, karena tekstur daging mentah yang buruk terkait dengan ketangguhan daging dimasak ( Palka 2003 ).

PERUBAHAN STRUKTURAL IMCT SELAMA PEMBANGUNAN HEWAN

Mekanik dan stabilitas termal meningkat IMCT dengan pertumbuhan hewan ( Bailey & Light 1989 ; McCormick 1994 ; Nishimura et al 1996a. ). Meat tenderness generally decreases with animal age, and collagen-rich muscles show this effect more than those with low IMCT content ( Shorthose & Harris 1990 ). Daging kelembutan umumnya menurun dengan usia hewan, dan otot kaya kolagen menunjukkan pengaruh ini lebih dari yang dengan konten IMCT rendah ( Shorthose & Harris 1990 ). It is well established that the mechanical and chemical stability of collagen fibrils increase with chronological age. Hal ini juga ditetapkan bahwa stabilitas mekanik dan kimia meningkat fibril kolagen dengan usia kronologis. These changes are related to the chemical nature of the covalent intermolecular crosslinks of collagen ( Tanzer 1973 ). Perubahan ini terkait dengan sifat kimia dari crosslinks antarmolekul kovalen kolagen ( Tanzer 1973 ). Most crosslinks are in the unstable Schiff base form and are labile to acids and heat in connective tissues of young animals ( Bailey & Shimokomaki 1971 ). crosslinks Sebagian besar dalam bentuk dasar Schiff tidak stabil dan labil terhadap asam dan panas dalam jaringan ikat hewan muda ( Bailey & Shimokomaki 1971 ). The reducible crosslinks are transformed into more stable non-reducible compounds with ageing ( Bailey & Shimokomaki 1971 ; Robins et al. 1973 ). Para crosslinks direduksi diubah menjadi lebih senyawa non-direduksi stabil dengan penuaan ( Bailey & Shimokomaki 1971 ; Robins et al 1973. ). This brings about a decrease in collagen solubility, resulting in tougher beef ( Hill 1966 ; Dikeman et al. 1971 ). Hal ini membawa penurunan kelarutan kolagen, sehingga daging sapi sulit ( Hill 1966 ; Dikeman et al 1971. ). However, Avery et al. (1996 ) reported that the total collagen content and the nature of collagen intermolecular crosslinks are unrelated to texture of longissimus muscles in pigs of similar maturity. Namun, Avery et al. (1996 ) melaporkan bahwa kandungan kolagen total dan sifat kolagen crosslinks antarmolekul tidak ada hubungannya dengan tekstur otot Longissimus pada babi waktu yang sama. Thus, there must be other factors that determine meat texture. Jadi, harus ada faktor lain yang menentukan tekstur daging. The mechanical stability of IMCT depends not only on intermolecular crosslinks of collagen but also on the size and arrangement of collagen fibrils ( Rowe 1981 ). Bailey and Light (1989 ) suggested that larger fibrils are more tightly knit

and probably have a higher degree of structural integrity due to the presence of maximal amounts of multivalent intermolecular crosslinks. Kestabilan mekanik dari IMCT tidak hanya tergantung pada crosslinks antarmolekul kolagen tetapi juga pada ukuran dan susunan fibril kolagen ( Rowe 1981 ). Bailey dan Light (1989 ) menyatakan bahwa fibril yang lebih besar lebih erat merajut dan mungkin memiliki tingkat yang lebih tinggi struktural karena kehadiran jumlah maksimal crosslinks antarmolekul multivalent integritas. The arrangement of collagen fibrils and fibers in IMCT becomes more regular during the development of bovine semitendinosus muscle, and is closely related to an increase in the mechanical strength of IMCT during the development of bovine skeletal muscle ( Nishimura et al. 1996a ). Penataan fibril kolagen dan serat dalam IMCT menjadi lebih teratur selama pengembangan otot semitendinosus sapi, dan terkait erat dengan peningkatan kekuatan mekanik IMCT selama pengembangan otot rangka bovine ( Nishimura et al 1996a. ). These results suggest that the three-dimensional architecture of IMCT is an important factor in the determination of meat texture. Hasil ini menunjukkan bahwa arsitektur tiga-dimensi IMCT merupakan faktor penting dalam penentuan tekstur daging.

PENGARUH intramuskular ENDAPAN FAT PADA STRUKTUR IMCT dan kelembutan DAGING
Marbling (lemak intramuskular) adalah salah satu faktor yang paling penting dalam menentukan kualitas daging, khususnya tekstur dan rasa. Most of the earlier studies have demonstrated small positive relationships between the degree of marbling and sensory tenderness, and a small inverse relationship with shear force value of cooked beef ( Pearson 1966 ; Smith et al. 1988 ). Sebagian besar penelitian sebelumnya telah menunjukkan hubungan positif yang kecil antara tingkat dan sensorik kelembutan marmer, dan hubungan terbalik kecil dengan nilai kekuatan geser daging sapi dimasak ( Pearson 1966 ; Smith et al 1988. ). The degree of marbling accounts for only 3 to 10% of the variation in sensory tenderness of beef ( Campion et al. 1975 ; Crouse et al. 1978 ; Tatum et al. 1980 ). Tingkat account marmer hanya 3 hingga 10% variasi dalam kelembutan sensorik daging sapi ( Campion et al 1975. ; Crouse et al 1978. ; Tatum et al 1980. ). However, May et al. (1992 ) have shown that the marbling score is moderately related to sensory panel tenderness (r = 0.51) and shear force (r = 0.61) in Angus Hereford steers, which are known for a relatively high ability to marble. Namun, dkk Mei 1992. ( ) telah menunjukkan bahwa skor marbling ini cukup terkait dengan kelembutan panel sensori (r = 0,51) dan gaya geser (r = -0,61) di Angus Hereford sapi jantan, yang dikenal untuk kemampuan relatif tinggi untuk marmer. Japanese Black cattle are characterized by the ability to deposit very large amounts of intramuscular fat ( Lunt et al. 1992 ; Zembayashi 1994 ). Jepang Black sapi dicirikan oleh kemampuan untuk deposit dalam jumlah besar sangat lemak intramuskular ( Luntungan et al 1992. ; Zembayashi 1994 ). We have shown that the shear force value of longissimus muscle of Japanese Black steers decreases after 20 months of age, concomitantly with the rapid increase in the crude fat content ( Nishimura et al. 1999 ). Kami telah menunjukkan bahwa nilai kekuatan geser otot Longissimus Jepang Black mengarahkan menurun setelah berumur 20 bulan, bersamaan dengan peningkatan pesat dalam kandungan lemak kasar ( Nishimura et al. 1999 ). There was a high and inverse correlation coefficient between the crude fat content and the shear force value of raw longissimus muscle for Japanese Black cattle after 20 months of age. Ada korelasi yang tinggi dan invers koefisien antara kandungan lemak kasar dan nilai gaya geser dari otot Longissimus baku untuk ternak Black Jepang setelah berumur 20 bulan. It seems likely that a higher level of marbling is closely related to the tenderness of meat. Agaknya tingkat yang lebih tinggi dari marmer terkait erat dengan kelembutan daging. Why is highly marbled beef extremely tender? Mengapa sangat marmer daging sapi sangat lembut? We have shown by scanning electron micrography that the adipose tissues are formed between muscle fiber bundles, that the honeycomb structure of endomysia is partially broken, and that the perimysium is separated into thinner collagen fibers in longissimus muscle dissected from 32-month-old Japanese Black steers ( Nishimura et al. 1999 ). Kami telah menunjukkan dengan memindai mikrografi elektron bahwa jaringan adiposa terbentuk antara bundel serat otot, bahwa struktur sarang lebah endomysia sebagian rusak, dan bahwa perimysium dipisahkan menjadi serat kolagen tipis dalam otot Longissimus dibedah dari Black Jepang 32-bulan-tua mengarahkan ( Nishimura et al 1999. ). On the other hand, in semitendinosus muscle, in which the crude fat content was lower than that of longissimus muscle, the structure of IMCT remained rigid at 32 months of age, and the shear force value of the muscle increased even in the late fattening period from 20 to 32 months of age. Di sisi lain, di otot semitendinosus, di mana kandungan lemak kasar lebih rendah daripada otot Longissimus, struktur IMCT tetap kaku pada usia 32 bulan, dan nilai gaya geser dari otot meningkat bahkan di akhir periode penggemukan 20-32 bulan. Thus, the development of adipose tissues in longissimus muscle appears to disorganize the structure of IMCT and contributes to the tenderization of highly marbled beef from Japanese Black cattle ( Fig. 1 ). Dengan demikian, pengembangan jaringan lemak pada otot Longissimus tampaknya mengacaukan struktur IMCT dan berkontribusi terhadap keempukan daging sapi dari marmer yang sangat dari sapi Black Jepang ( Gambar. 1 ). Figure 1. Effect of intramuscular fat deposition on the structure of intramuscular connective tissue (IMCT). Gambar 1. Pengaruh penumpukan lemak intramuskular pada struktur jaringan ikat intramuskuler (IMCT). With animal growth, collagen crosslinks become more stable, and the structural integrity of IMCT increases. Dengan pertumbuhan hewan, crosslinks kolagen menjadi lebih stabil, dan integritas struktural meningkat IMCT. These changes increase the mechanical properties of IMCT, contributing to the toughening of meat. Perubahan ini meningkatkan sifat mekanik IMCT, memberikan kontribusi bagi ketangguhan daging. The intramuscular fat deposits mainly in the perimysium (between muscle fiber bundles), resulting in marbling. Deposito lemak intramuskuler terutama dalam perimysium (antara bundel serat otot), mengakibatkan marmer. This causes the remodeling of extracellular matrix (ECM) and reduces the mechanical strength of IMCT, contributing to the tenderization of beef. Hal ini menyebabkan remodelling matriks ekstraselular (ECM) dan mengurangi kekuatan mekanik IMCT, kontribusi terhadap keempukan daging sapi.

PERUBAHAN STRUKTURAL IMCT SELAMA postmortem AGEING DAGING

Kelembutan daging ditentukan oleh sifat-sifat myofibrils dan IMCT ( Bailey 1972 ) dan terus ditingkatkan dengan penuaan postmortem ( Hakim & Aberle 1982 ; Etherington 1987 ). In early studies it has been shown that the solubility of collagen is affected by neither temperature nor time of conditioning ( Pierson & Fox 1976 ; Chizzolini et al. 1977 ). Dalam studi awal telah menunjukkan bahwa kelarutan kolagen dipengaruhi oleh suhu atau tidak waktu AC ( Pierson & Fox 1976 ; Chizzolini et al 1977. ). These results suggest that collagen remains unchanged at the molecular level during conditioning. Hasil ini menunjukkan kolagen yang tetap tidak berubah pada tingkat molekuler selama pengkondisian. However, Stanton and Light (1987, 1988, 1990 ) have presented data which proved that perimysial collagen is damaged and partially solubilised during conditioning. Namun, Stanton dan Light (1987, 1988, 1990 ) telah menyajikan data yang membuktikan bahwa perimysial kolagen rusak dan sebagian solubilised selama pengkondisian. Using differential scanning calorimetry, Judge and Aberle (1982 ) have shown that the thermal shrinkage temperature of bovine intramuscular collagen decreases by 78C within 7 days post mortem . Menggunakan diferensial kalorimetri pemindaian, Hakim dan Aberle (1982 ) menunjukkan bahwa suhu penyusutan termal sapi menurun kolagen intramuskuler dengan 7-8 C dalam post mortem hari 7. It has also been shown that the isometric tension of the intramuscular collagen decreases at 21 days post mortem in beef ( Etherington 1987 ). Hal ini juga telah menunjukkan bahwa ketegangan isometrik dari kolagen intramuskuler menurun pada 21 hari pasca mortem daging sapi ( Etherington 1987 ). Furthermore, Lewis and Purslow (1989 ) developed a method for measuring the mechanical strength of isolated, yet intact, perimysial connective tissue. Selanjutnya, Lewis dan Purslow (1989 ) mengembangkan metode untuk mengukur kekuatan mekanik terisolasi, utuh, perimysial jaringan ikat belum. Using this method, Lewis et al. (1991 ) revealed that the breaking strength of the perimysial connective tissue in raw beef decreases during postmortem ageing. Dengan menggunakan metode ini, Lewis et al. (1991 ) mengungkapkan bahwa kekuatan putus dari jaringan ikat perimysial berkurang daging sapi mentah selama penuaan postmortem. We showed that the structural integrity of the IMCT decreases during postmortem ageing of chickens ( Liu et al. 1994, 1995 ), beef ( Nishimura et al. 1995 ) and pork ( Nishimura et al. 2008b ). Kami menunjukkan bahwa integritas struktural IMCT menurun selama postmortem umur ayam ( Liu et al 1995. 1994, (), daging sapi Nishimura et al 1995. ) dan babi ( Nishimura et al. 2008b ). These structural changes are well related to the mechanical strength of meat as demonstrated by shear measurements on raw muscle or uncooked IMCT structures embedded in acrylamide gels ( Nishimura et al. 1998 ). Perubahan-perubahan struktural yang baik berkaitan dengan kekuatan mekanik daging seperti yang ditunjukkan oleh pengukuran geser pada otot mentah atau struktur IMCT mentah tertanam dalam gel akrilamida ( et al Nishimura 1998. ). The weakening mechanism of IMCT is unknown. Mekanisme melemahnya IMCT tidak diketahui. Even though ECM components are degraded by metalloproteinases and lysosomal enzymes in vitro ( Bailey & Light 1989 ; Alexander & Werb 1991 ), it is not clear whether the extracellular matrix in muscle is degraded by these enzymes during postmortem ageing. Meskipun komponen ECM terdegradasi oleh metaloproteinase dan enzim lisosomal in vitro ( Bailey & Light 1989 ; Alexander & Werb 1991 ), tidak jelas apakah matriks ekstraseluler di otot rusak oleh enzim selama proses penuaan postmortem. -glucuronidase, which is known to attack PGs, is released from lysosomes in postmortem muscle ( Moeller et al. 1976 ). -glucuronidase, yang dikenal menyerang PG, dilepaskan dari lisosom dalam otot postmortem ( Moeller et al. 1976 ). The activity of free -glucuronidase increases with postmortem ageing, concomitant with an increase in the tenderness of beef ( Dutson & Lawrie 1974 ). Kegiatan peningkatan -glucuronidase bebas dengan penuaan postmortem, bersamaan dengan peningkatan kelembutan daging sapi ( Dutson & Lawrie 1974 ). We have shown that the amount of PGs in bovine semitendinosus muscle decreases with time postmortem, and that collagen fibril-associated PGs in the perimysium mostly disappear during postmortem ageing of beef ( Nishimura et al. 1996b ). Etherington (1987 ) has shown that the type and quantity of associated PGs are important in determining the level of susceptibility of collagen to enzymatic digestion. Kami telah menunjukkan bahwa jumlah PG di sapi menurun otot semitendinosus dengan postmortem waktu, dan fibril kolagen terkait PG bahwa dalam perimysium yang sebagian besar hilang selama postmortem umur daging sapi ( Nishimura et al 1996b. ). Etherington (1987 ) telah menunjukkan bahwa jenis dan kuantitas PG terkait yang penting dalam menentukan tingkat kerentanan kolagen untuk pencernaan enzimatik. Furthermore, Wu et al. (1981 ) have shown an increase in collagen solubility due to the combined action of collagenase with -glucuronidase or hyaluronidase. Selain itu, Wu et al 1981. ( ) telah menunjukkan peningkatan kelarutan kolagen karena aksi gabungan kolagenase dengan glucuronidase atau hialuronidase. Thus, there is a possibility that lysosomal glycosidases cause an exposure of collagen fibrils from surrounding PGs and facilitate their degradation by collagenase, resulting in structural changes in IMCT during postmortem ageing of meat ( Fig. 2 ). Dengan demikian, ada kemungkinan bahwa glycosidases lisosomal menyebabkan eksposur fibril kolagen dari PG sekitarnya dan memfasilitasi degradasi mereka dengan kolagenase, mengakibatkan perubahan struktural dalam IMCT selama umur daging postmortem ( Gambar 2. ). Proteoglycans may protect collagenous tissue from enzyme attack. Proteoglikan dapat melindungi jaringan kolagen dari serangan enzim. Further investigation is needed to elucidate molecular mechanisms by which ECM is degraded during postmortem ageing of meat. penyelidikan lebih lanjut diperlukan untuk menjelaskan mekanisme molekul dengan yang ECM rusak selama umur daging postmortem.

Figure 2. Schematic representation of changes in IMCT during postmortem ageing. Gambar 2. Skema representasi perubahan IMCT selama penuaan postmortem. In muscle immediately postmortem, proteoglycans (PGs) link collagen fibrils and stabilize the IMCT. Dalam otot segera postmortem, proteoglikan fibril link (PG) kolagen dan menstabilkan IMCT tersebut. During postmortem aging, PGs are degraded and the linkage between collagen fibrils is weakened. Selama penuaan postmortem, PG yang terdegradasi dan hubungan antara fibril kolagen melemah. This structural change in IMCT contributes to the tenderization of aged meat. Perubahan struktural dalam IMCT berkontribusi pada keempukan daging berusia.

Bouton and Harris (1972 ) showed that the connective tissue toughness is unaffected by extensive postmortem ageing when followed by cooking. Lewis et al. (1991 ) demonstrated that there is a reduction in strength of IMCT with postmortem ageing in raw meat, whereas these effects are negated after cooking to temperatures of 60C and above, where both aged and unaged perimysial IMCT have the same strength. Purslow (2005 ) pointed out that the properties of IMCT in raw meat and degradations during postmortem ageing do not directly reflect cooked meat texture. Bouton dan Harris (1972 ) menunjukkan bahwa ketangguhan jaringan ikat tidak dipengaruhi oleh penuaan postmortem luas bila diikuti dengan memasak. Lewis et al. (1991 ) menunjukkan bahwa ada pengurangan kekuatan IMCT dengan postmortem penuaan pada daging mentah, sedangkan efek ini adalah ditiadakan setelah dimasak dengan suhu 60 C dan di atas, dimana kedua tanpa penuaan perimysial IMCT dan berusia memiliki kekuatan yang sama. Purslow (2005 ) menunjukkan bahwa sifat-sifat IMCT dalam daging mentah dan degradasi selama postmortem penuaan tidak secara langsung mencerminkan daging dimasak tekstur. Further investigation is needed to elucidate cooking influences on the IMCT and its contributions to meat toughness, because cooking drastically affects the nature of IMCT and its effect is different from that on myofibrillar components. penyelidikan lebih lanjut diperlukan untuk menjelaskan pengaruh memasak pada IMCT dan kontribusi terhadap ketangguhan daging, karena memasak secara drastis mempengaruhi sifat IMCT dan pengaruhnya berbeda dari yang pada komponen myofibrillar.

KESIMPULAN
otot rangka pembangunan adalah proses yang sangat terorganisir diatur oleh interaksi yang rumit antara serat otot dan lingkungan mereka, IMCT tersebut. During embryonic development, IMCT forms synchronously with muscle fibers. Selama perkembangan embrio, IMCT bentuk serentak dengan serat otot. During postnatal development, IMCT must be reconstructed with muscle hypertrophy and intramuscular fat deposition. Selama perkembangan pasca melahirkan, IMCT harus direkonstruksi dengan hipertrofi otot dan penumpukan lemak intramuskular. These structural changes affect the mechanical strength of IMCT and contribute to variation of meat texture. Perubahan struktural mempengaruhi kekuatan mekanik IMCT dan berkontribusi terhadap variasi tekstur daging. Thus, the turnover of IMCT must be a future target for manipulation of meat texture. Dengan demikian, omzet IMCT harus menjadi sasaran masa depan untuk manipulasi tekstur daging. Postmortem ageing increases collagen extractability from muscle, degrades PG components of the IMCT, disintegrates the structure of the IMCT network, and significantly reduces the strength of IMCT in raw meat, although it is still controversial whether these IMCT changes in raw meat are related to cooked meat toughness. Penuaan postmortem meningkat extractability kolagen dari otot, komponen PG menurunkan dari IMCT itu, terurai struktur jaringan IMCT, dan secara signifikan mengurangi kekuatan IMCT dalam daging mentah, meskipun masih kontroversial apakah perubahan ini IMCT dalam daging mentah berkaitan dengan dimasak daging ketangguhan. Further elucidations of precise mechanisms by which IMCT disintegrates during postmortem ageing will give a better understanding of the control of meat tenderness after slaughter. penjelasannya lebih lanjut mekanisme yang tepat dimana IMCT hancur selama proses penuaan postmortem akan memberikan pemahaman yang lebih baik dari kontrol kelembutan daging setelah pembantaian.

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The role of intramuscular connective tissue in meat texture 1. Takanori NISHIMURA

Article first published online: 3 NOV 2009 DOI: 10.1111/j.1740-0929.2009.00696.x 2009 The Author. Journal compilation 2009 Japanese Society of Animal Science Keywords: collagen; intramuscular connective tissue; meat; proteoglycan; texture

ABSTRACT
The structure, composition and amount of intramuscular connective tissue (IMCT) vary tremendously between muscles, species and breeds, and certainly contribute to meat texture. With animal growth, collagen crosslinks become more stable, and the structural integrity of IMCT increases. These changes increase the mechanical properties of IMCT, contributing to the toughening of meat. Intramuscular fat deposits, mainly in the perimysium between muscle fiber bundles, result in marbling. This causes the remodeling of IMCT structures and reduces the mechanical strength of IMCT, contributing to the tenderization of beef. The IMCT has been thought to be rather immutable compared to myofibrils during postmortem ageing of meat. However, recent studies have shown the disintegration of IMCT during postmortem ageing of meat and its relationship to tenderization of raw meat, although its contribution to cooked meat is still controversial. Given the large influence of IMCT on meat texture, further elucidations of molecular mechanisms which change the structural integrity of IMCT during chronological ageing of animals and postmortem ageing of meat are needed.

INTRODUCTION
Texture is the most important factor in determining the quality of meat from the consumers' point of view (Dransfield et al. 1984). Meat texture depends on the structures and composition of skeletal muscle, which is mainly composed of muscle fibers and surrounding intramuscular connective tissues (IMCT). Muscle fibers consist of myofibrils, which are made of thin (actin) and thick (myosin) filaments. The structural integrity of myofibrils changes during postmortem ageing of meat, which contributes to the tenderness of aged meat (Dransfield et al. 1984; Takahashi 1996). Myofibrils form so-called actomyosin toughness. On the other hand, the amount, composition and structure of IMCT vary tremendously between muscles, species, breeds, and with animal age (Bailey & Light 1989). Whilst IMCT contribution to meat texture is certainly important, it has been thought to be rather immutable compared to myofibrils during postmortem ageing of meat (Purslow 2005). Thus it is called background toughness. In the present article, the structural changes in IMCT during development and postmortem ageing of meat and their contributions to meat texture are reviewed

STRUCTURE AND COMPOSITION OF IMCT

The basic structure and composition of IMCT have been reviewed by several previous authors (Borg & Caulfield 1980; Bailey & Light 1989; McCormick 1994; Purslow 2002), so only a brief description will be given here as background. The structural integrity of muscle fibers is maintained by three layers of IMCT: (i) the endomysium that surrounds individual skeletal muscle fibers, (ii) the perimysium that bundles a group of muscle fibers, and (iii) the epimysium that ensheathes the whole muscle. These connective tissues are composed of cells and extracellular matrix (ECM), which is composed of collagen, proteoglycans (PGs) and glycoproteins. There are various types of collagen with tissue-specific distribution and unique functional properties. Skeletal muscle contains collagen types I, III, IV, V, VI, XII and XIV (Nishimura et al. 1997; Listrat et al. 1999, 2000). The major types of collagen in skeletal muscle are type I and III (Bailey & Light 1989), which align into a quarter-stagger array to form fibrils in tissues. The endomysium is composed of sheaths which consist of collagen fibril networks, the perimysium is composed of sheets of collagen fibers (a bundle of collagen fibrils) which show a regular wavy pattern, and the epimysium is composed of thick sheets constructed of several layers which consist of collagen fibers (Nishimura et al. 1994). The other principal component of the ECM is PG. This macromolecule is composed of a central core protein with covalently attached glycosaminoglycan (GAG) chains. The GAG is a polymer of disaccharide repeats that are highly sulfated and negatively charged. Some PGs have only a single or limited number of GAGs, whereas others have up to 100 GAG chains. Typical GAGs attached to the core protein of PGs are chondroitin sulfate, dermatan sulfate, heparan sulfate and keratan sulfate. The core proteins are highly variable in structure and size with a molecular weight of approximately 40,000350,000 (Iozzo & Murdoch 1996). Different GAG chains can be attached to the same core protein. Decorin, a small leucine-rich PG (SLRP), regulates collagen fibrillogenesis (Danielson et al. 1997) and plays an important role in the stabilization of collagen fibrils (Scott & Thomlinson 1998). Decorin is identified in IMCT (Eggen et al. 1994; Nakano et al. 1997), and plays an important role in morphogenesis of IMCT during bovine fetal development (Nishimura et al. 2002).

Decorin also plays important roles in the quiescence of muscle cells (Nishimura et al. 2008a) and muscle cell growth by modulating growth factors (Miura et al. 2006; Zhu et al. 2007; Kishioka et al. 2008).

THE ROLE OF IMCT IN MEAT TEXTURE

Collagen is a major component of IMCT. The total collagen content in bovine muscles varies from 1% to 15% of dry weight, while elastin is a smaller component varying from 0.6% to 3.7% (Bendall 1967). Many researchers have attempted to clarify the relationship between collagen content and toughness of meat using a combination of organoleptic evaluation and some mechanical tests, but no clear relationship has been established. Some researchers suggested that the eating quality of meat does not correlate to collagen content (Herring et al. 1967; Hunsley et al. 1971), while others showed that skeletal muscle rich in collagen is tougher than that with a low content of collagen (Dransfield 1977; Light et al. 1985; Nishiumi et al. 1995). Skeletal muscle, which shows a low compressive-force value, generally contains only a small amount of collagen. As an exception, the pectoralis profundus muscle, which has a high collagen content, has a lower compressiveforce value than that of gastrocnemius muscle, which has a low collagen content (Bailey & Light 1989). It seems likely that textural properties of various skeletal muscles are due to not only the total collagen content but also to other factors. The relationship between heat-stability of collagen and meat tenderness has been investigated. Some researchers show that the correlation between the tenderness of cooked meat and the heat-solubility of collagen is relatively low (Renand et al. 2001; Berge et al. 2003; Chambaz et al. 2003) or non-significant (Young et al. 1994). However, Nishiumi et al. (1995) reported a significant correlation between heat-solubility of collagen and toughness of raw pork using 8 classes of skeletal muscle in miniature pigs. In addition, Torrescano et al. (2003) showed a high positive correlation between heat-insoluble collagen and Warner-Bratzler shear force (WBSF) of raw beef. The heat-solubility of collagen depends on crosslinks (Tanzer 1973). Shimokomaki et al. (1972) showed that there is a low correlation between the amount of oxo-imine crosslinks and eating quality of meat, while Light et al. (1985) showed that tender beef has fewer crosslinks in endomysial and perimysial collagen. The correlation between the number of crosslinks per collagen molecule and meat tenderness among different muscles varies from relatively high (Bailey & Light 1989) to low or non-significant values (Avery et al. 1996). Recently, Lepetit (2007) showed the total amount of crosslinks present per volume of cooked meat is approximately proportional to the elastic modulus of collagenous fractions of connective tissue, suggesting the contribution of collagen crosslinks to meat toughness. Collagen crosslinks may have an additive effect on toughening meat, although the correlation between collagen crosslinks and toughness of cooked meat is still controversial. Over 90% of intramuscular collagen is located in the perimysium (McCormick 1994). Lewis and Purslow (1990) demonstrated in cooked beef that the perimysial strands have higher tensile strength than junctions between the endomysium and the perimysium. These results suggest that the nature of the perimysium is one of the most important factors that determine the toughness of meat. In fact, thicker perimysium is associated with reduced tenderness (Swatland et al. 1995). We have shown that the thickness of the secondary perimysium contributes to the toughness of raw meat (Liu et al. 1996). However, the correlations between the WBSF of cooked muscles and perimysial content or thickness are poor (Brooks & Savell 2004). Purslow (1999) also showed that correlations between shear force values of meat cooked to 80C and perimysial thickness are low. Toughness of meat increases with temperature of cooking. However, the strength of perimysial connective tissue increases in meat cooked up to 50C and decreases above this temperature (Lewis & Purslow 1989). Even though the nature of perimysial connective tissue affects raw meat toughness, its contribution to cooked meat toughness is controversial, because the texture of raw meat is poorly related to cooked meat toughness (Palka 2003).

STRUCTURAL CHANGES IN IMCT DURING DEVELOPMENT OF ANIMALS

The thermal and mechanical stability of IMCT increases with animal growth (Bailey & Light 1989; McCormick 1994; Nishimura et al. 1996a). Meat tenderness generally decreases with animal age, and collagen-rich muscles show this effect more than those with low IMCT content (Shorthose & Harris 1990). It is well established that the mechanical and chemical stability of collagen fibrils increase with chronological age. These changes are related to the chemical nature of the covalent intermolecular crosslinks of collagen (Tanzer 1973). Most crosslinks are in the unstable Schiff base form and are labile to acids and heat in connective tissues of young animals (Bailey & Shimokomaki 1971). The reducible crosslinks are transformed into more stable non-reducible compounds with ageing (Bailey & Shimokomaki 1971; Robins et al. 1973). This brings about a decrease in collagen solubility, resulting in tougher beef (Hill 1966; Dikeman et al. 1971). However, Avery et al. (1996) reported that the total collagen content and the nature of collagen intermolecular crosslinks are unrelated to texture of longissimus muscles in pigs of similar maturity. Thus, there must be other factors that determine meat texture. The mechanical stability of IMCT depends not only on intermolecular crosslinks of collagen but also on the size and arrangement of collagen fibrils (Rowe 1981). Bailey and Light (1989) suggested that larger fibrils are more tightly knit and probably have a higher degree of structural integrity due to the presence of maximal amounts of multivalent intermolecular crosslinks. The arrangement of collagen fibrils and fibers in IMCT becomes more regular during the development of bovine semitendinosus muscle, and is closely related to an increase in the mechanical strength of IMCT during the development of bovine skeletal muscle (Nishimura et al. 1996a). These results suggest that the three-dimensional architecture of IMCT is an important factor in the determination of meat texture.

INFLUENCE OF INTRAMUSCULAR FAT DEPOSITION ON IMCT STRUCTURE AND MEAT TENDERNESS

Marbling (intramuscular fat) is one of the most important factors in determining meat quality, especially texture and flavor. Most of the earlier studies have demonstrated small positive relationships between the degree of marbling and sensory tenderness, and a small inverse relationship with shear force value of cooked beef (Pearson 1966; Smith et al. 1988). The degree of marbling accounts for only 3 to 10% of the variation in sensory tenderness of beef (Campion et al. 1975; Crouse et al. 1978; Tatum et al. 1980). However, May et al. (1992) have shown that the marbling score is moderately related to sensory panel tenderness (r = 0.51) and shear force (r = 0.61) in Angus Hereford steers, which are known for a relatively high ability to marble. Japanese Black cattle are characterized by the ability to deposit very large amounts of intramuscular fat (Lunt et al. 1992; Zembayashi 1994). We have shown that the shear force value of longissimus muscle of Japanese Black steers decreases after 20 months of age, concomitantly with the rapid increase in the crude fat content (Nishimura et al. 1999). There was a high and inverse correlation coefficient between the crude fat content and the shear force value of raw longissimus muscle for Japanese Black cattle after 20 months of age. It seems likely that a higher level of marbling is closely related to the tenderness of meat. Why is highly marbled beef extremely tender? We have shown by scanning electron micrography that the adipose tissues are formed between muscle fiber bundles, that the honeycomb structure of endomysia is partially broken, and that the perimysium is separated into thinner collagen fibers in longissimus muscle dissected from 32-month-old Japanese Black steers (Nishimura et al. 1999). On the other hand, in semitendinosus muscle, in which the crude fat content was lower than that of longissimus muscle, the structure of IMCT remained rigid at 32 months of age, and the shear force value of the muscle increased even in the late fattening period from 20 to 32 months of age. Thus, the development of adipose tissues in longissimus muscle appears to disorganize the structure of IMCT and contributes to the tenderization of highly marbled beef from Japanese Black cattle (Fig. 1). Figure 1. Effect of intramuscular fat deposition on the structure of intramuscular connective tissue (IMCT). With animal growth, collagen crosslinks become more stable, and the structural integrity of IMCT increases. These changes increase the mechanical properties of IMCT, contributing to the toughening of meat. The intramuscular fat deposits mainly in the perimysium (between muscle fiber bundles), resulting in marbling. This causes the remodeling of extracellular matrix (ECM) and reduces the mechanical strength of IMCT, contributing to the tenderization of beef.

STRUCTURAL CHANGES IN IMCT DURING POSTMORTEM AGEING OF MEAT

The tenderness of meat is determined by the properties of myofibrils and IMCT (Bailey 1972) and is improved with postmortem ageing (Judge & Aberle 1982; Etherington 1987). In early studies it has been shown that the solubility of collagen is affected by neither temperature nor time of conditioning (Pierson & Fox 1976; Chizzolini et al. 1977). These results suggest that collagen remains unchanged at the molecular level during conditioning. However, Stanton and Light (1987, 1988, 1990) have presented data which proved that perimysial collagen is damaged and partially solubilised during conditioning. Using differential scanning calorimetry, Judge and Aberle (1982) have shown that the thermal shrinkage temperature of bovine intramuscular collagen decreases by 78C within 7 days post mortem. It has also been shown that the isometric tension of the intramuscular collagen decreases at 21 days post mortem in beef (Etherington 1987). Furthermore, Lewis and Purslow (1989) developed a method for measuring the mechanical strength of isolated, yet intact, perimysial connective tissue. Using this method, Lewis et al. (1991) revealed that the breaking strength of the perimysial connective tissue in raw beef decreases during postmortem ageing. We showed that the structural integrity of the IMCT decreases during postmortem ageing of chickens (Liu et al. 1994, 1995), beef (Nishimura et al. 1995) and pork (Nishimura et al. 2008b). These structural changes are well related to the mechanical strength of meat as demonstrated by shear measurements on raw muscle or uncooked IMCT structures embedded in acrylamide gels (Nishimura et al. 1998). The weakening mechanism of IMCT is unknown. Even though ECM components are degraded by metalloproteinases and lysosomal enzymes in vitro (Bailey & Light 1989; Alexander & Werb 1991), it is not clear whether the extracellular matrix in muscle is degraded by these enzymes during postmortem ageing. -glucuronidase, which is known to attack PGs, is released from lysosomes in postmortem muscle (Moeller et al. 1976). The activity of free -glucuronidase increases with postmortem ageing, concomitant with an increase in the tenderness of beef (Dutson & Lawrie 1974). We have shown that the amount of PGs in bovine semitendinosus muscle decreases with time postmortem, and that collagen fibril-associated PGs in the perimysium mostly disappear during postmortem ageing of beef (Nishimura et al. 1996b). Etherington (1987) has shown that the type and quantity of associated PGs are important in determining the level of susceptibility of collagen to enzymatic digestion. Furthermore, Wu et al. (1981) have shown an increase in collagen solubility due to the combined action of collagenase with -glucuronidase or hyaluronidase. Thus, there is a possibility that lysosomal glycosidases cause an exposure of collagen fibrils from surrounding PGs and facilitate their degradation by collagenase, resulting in structural changes in IMCT during postmortem ageing of meat (Fig. 2). Proteoglycans may protect collagenous tissue from enzyme attack. Further investigation is needed to elucidate molecular mechanisms by which ECM is degraded during postmortem ageing of meat. Figure 2. Schematic representation of changes in IMCT during postmortem ageing. In muscle immediately postmortem, proteoglycans (PGs) link collagen fibrils and stabilize the IMCT. During postmortem aging, PGs are degraded and the linkage between collagen fibrils is weakened. This structural change in IMCT contributes to the tenderization of aged meat.

Bouton and Harris (1972) showed that the connective tissue toughness is unaffected by extensive postmortem ageing when followed by cooking. Lewis et al. (1991) demonstrated that there is a reduction in strength of IMCT with postmortem ageing in raw meat, whereas these effects are negated after cooking to temperatures of 60C and above, where both aged and unaged perimysial IMCT have the same strength. Purslow (2005) pointed out that the properties of IMCT in raw meat and degradations during postmortem ageing do not directly reflect cooked meat texture. Further investigation is needed to elucidate cooking influences on the IMCT and its contributions to meat toughness, because cooking drastically affects the nature of IMCT and its effect is different from that on myofibrillar components.

CONCLUSION
Skeletal muscle development is a highly organized process regulated by complicated interactions between muscle fibers and their environment, the IMCT. During embryonic development, IMCT forms synchronously with muscle fibers. During postnatal development, IMCT must be reconstructed with muscle hypertrophy and intramuscular fat deposition. These structural changes affect the mechanical strength of IMCT and contribute to variation of meat texture. Thus, the turnover of IMCT must be a future target for manipulation of meat texture. Postmortem ageing increases collagen extractability from muscle, degrades PG components of the IMCT, disintegrates the structure of the IMCT network, and significantly reduces the strength of IMCT in raw meat, although it is still controversial whether these IMCT changes in raw meat are related to cooked meat toughness. Further elucidations of precise mechanisms by which IMCT disintegrates during postmortem ageing will give a better understanding of the control of meat tenderness after slaughter.

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