*Lampiran Copyright © 2017, Mulono Apriyanto & Rujiah Hak ciptadilindungi oleh undang-undang. Dilarang memproduksi atau memperbanyak scluru atau sebagian dari buku ini dalam bentuk atau cara apa pun tanpa izin dari pemuis dan penerbit KIMIA PANGAN Penulis: Dr. Mulono Apriyanto, S.T.P,, MP. Rujiah, $.Tp. Editor/ Penyunting: Minan Nuri Rohman Cover: Wakhyudin Layout: St. Navisah Penerbit: Trussmedia Grafika JI, Dongkelan No. 357 Krapyak Kulon, Daerah Istimewa Yogyakarta (DIY) Phone, 081 903 717 727/0857 291 888 25 Email; one_trussmedia@yahoo.com www.trussmediagrafika.com Cetakan |, Maret 2017 xii +172; 14x 20,5 em ISBN: 978-602-0992-69-3,*Lampiran*Lampiran Jurnal Hmiah Bakti Farmasi, 2018, 11(2), hal. 1-6 peapupsa, peng war, pengeringan, penghancuran (breaking) dan pengayakan’ (Widowati, 2011), Teknik pengukusan —setelah pengecilan —ukuran diharapkan akan mempengaruhi kandungan total antosianin dari tepung ubi jalar ungu (Yahya, 2010), Pengukusan dilakukan setelah ngeciln ukuran, Hail tepung dan pati ub Pig mga ras! sea organoleptiks, kadar ar, randemen tepung dan pall dentifikasi kimia dan mikroskopis pat, METODE DAN PENELITIAN: ‘Bahan dan Alat Alat-alat yang digunakan pada penelitian in ep psa, maa oni ender, ayakan ukuran mesh 80, cawan penguap, timbangan analitk, oven, mikroskop cahaya, aca objek, bat uk, spate, gelas ain bette gage Bahan yang digunakan pada peneitian fini, bi alar ungu, air suling dan larutan fodium, Pengambilan noes da penelitian wo atch ul ingu eae dliperoleh di petkebunan bi Jalan. Sukarela, KM 7, Retshn Suk Kotamaya Palembang. Pembuatan Tepung Ubi Jalar Ungu Pembuatan tepung ubi dengan cara penusn: nb ol gu eg sh dius dan ders, dit ran. pang unl sal 413 eran du saa 20 met psi 100°C, wb yang telah dikukus terlebih dahl sebelum—dilakukan pengeringan dengan oven pengering pada suht $0-60°C selama 72 jam. Setelah itu Jakukan penghalusan dengan cara diblender dan selanjutnya di ayak dengan pengayak sha 9 meh Gea, 2010, Pembuatan tepun; tanpa cusan und ear tg arg saa gas dibesinkan, dtimbang sebanyak S00 gram, Umbi bl jalar ungu al iris tpis dengan ketebalan 2-3 mm, kemudian lakukan Pengeringan menggunakan oven pengering Ages Rendowaty dkk 50-60°C selama 48 jam, setelah kering irisan lumbi dligiling (blender), Hasil penggiling di ayak dengan menggunakan ayakan berukuran ‘80 mesh (Hasrini dkk, 2011). Pembyatan pati: Hall kedua tipe tepung bi ditimbang 50 gram dimasukkan Kedalam beler glass din tmbalan $0 mL a sling dan dt aduk menggunakan batang pengaduk hingga bercampur. Saring menggunakan kain tipis, lakukan pekerjaan int sebanyak 4 ali hingga larutan berwama ening, Hasil saringan dlendapkan selama 6-12 jam. Pisafkan antara endapan dan ait, hasil epee pa Pal ah kerngkan dalam oven 50°C selama 12 Jam hingga kering dan diayak dengan pengayak 80 mesh, Karakteristik Tepung dan Pati Ubi Jalar ungu. Randemen tepung dan pati yang dl petole dapat dihitung dengan rumus Renidemen (6) = ‘Berat endapan (g) x 100 % Brat simplisiabasah(g) Uji Organoleptk : Uji organoleptik yang dilakukan pada tepung bi jalar ungu ink meliput ui techadap aroma (bau), warta dan rasa (Basin dkk, 2016). Kadar_air’menurut Apriyantono kk (1999) : tepung ubi jalarditimbang sebanyak 3 gram (a) dan dimasukkan ke cawan yang. telah dikeringkan dan —diketahut Dobotnya (c). Kemudian sampel dan cawan dikerngkan dalam oven bersuhu 105°C eal Jam. Cavan ingan dn it (b). Kadar air samy at ding dengan meneguatin runs eae Derikut: (Naim, 2016) Kadar ar (6 bk) = =2=* Keterangan : a= beat sampel aval gram) b= berat sampel akhir dan cawan (gra) c= heat sampel aval dan cawan Identifikast pati dengan lartan Todium : pati ditambahkan larutan Jodjum, akan memberikan wama coKatdan-atau ungu.*Lampiran Biomolecules 2014 4 259 108s of function, isnot a major toxicity mechanism. On the other hand! the proteins that aggregate upon arsenite exposure are enriched for multiple protein-protein interactions [50], suggesting that misfolded forms of these proteins might engage in extensive aberrant protein-protein interactions during exposure, thereby affecting cell vibility. Consistent with this notion, in vitro data indicate that arsenite induced protein aggregates, in a gain-of-function mechanism, act as seeds committing other, labile proteins to misfold and aggregate [9] Widespread aggregation of nascent proteins also observed in cadmium exposed yeast cals [9,48 5] In addition, cadmium has been shown to cause endoplasmic reticulum (ER) stress in yeast [54 and probably also in mammalian calls [55-58]. Neither arsenite nor mercury provoke any ER stress in yeast [54]. ER stress is characterized by an accumulation of unfolded proteins in the ER, which, in ‘ur, activates the unfolded protein response (UPR), The UPR, which is operative in most eukaryotic cals from yeast to mammals induces the expression of proteins th facilitate protein folding in the ER, thus mitigating the ER stress [59]. Y east mutants that cannot induce the UPR are hypersensitive to ‘cadmium, suggesting that toxicity might be @ consequence of cadmium accumulation in the ER [54] Whilst cadmium does not interfere with the formation of disulfide bonds in the ER, it appears to perturb calcium metabelism [54], a condition that may result in ER stress [60]. The mechanistic details of how cadium cases protain misfldingin the cytosol andthe ER remain tobe elucicted Chromium (Cr(VI)) has been shown to trigger oxidative protein damage [61] and protein aggregation in yeast [9,10]. Whilst arsenite and cadmium directly interfere with protein folding, chromium induces protein aggregation by enhencing mRNA mistransation. Mistrenslation appears to be a primary cause of cdlular chromium toxicity [10]. Although the mechanistic details of how chromium provokes mRNA mistranstation remain unknovin, misincorporation of amino acids may result in misfolding and aggregation of the corresponding proteins. Neither arsenite nor cadmium ‘cause mRNA mistranslation to any major extent [9,48] To conde, these recent studies in yeast demonstrated that heavy metals and metalloids interfere with protein folding in living cells through common, as wall as distinct mechanisms, nascent or non flded proteins being the prime targets. Quite likely, heavy metals and metalloids other than those already tested will perturb protein folding and manifest their toxicity through similar mechanisms. 6. How Cells Deal with Heavy Metal- and Metalloid-Induced Protein Misfolding and Aggregation Protein quality-control systems monitor the correct functionality of the proteome and protect calls against the harmful accumulation of protein aggregates during environmental tress conditions, as well ‘a during disease and ageing processes [11,20]. In response to heavy meta exposure, calls adjust their ‘gene expression programs (1) chaperone: and other heat-shock-response genes are activated, probably to enhance the folding capacity of the cell [62-70]; (2) proteasome-encoding genes are activated to enhance the protein degradation capacity of the calls [64-67,71-73]; and (3) the expression of genes encoding aggregetion-prone proteins is downregulated, presumably to prevent excessive accumulation of harmful aggregates [50,74]. Failure to adjust the protein quality-control systems will result in increased metal metalloid sensitivity (9,65-67, 75. ‘Thermotolerance in yeast and bacterial cells has been shown to be based on chaperone-mediated protein rescue rather than the degradation of aggregated proteins [76,77]. Albeit chaperones and other*Lampiran Biomolecules 2014, 4, 252-267; dol:10.3990/biom4010252 ene biomolecules ISSN 2218-278X ‘www. dl.confournal biomolecules! Review Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation Markus J. Tamés “*, Sandeep K. Sharma, Sebastian Ibstedt ', Therese Jaccbson * ‘and Philipp Christen? * Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg S-405 30, ‘Sweden; E-Mails sebastian ibstedi@ cmb quse (S.); theresejacobeon@.emb.gu.se (TJ) 2 Department of Biocheristry, University of Zurich Ztrich CH-8087, Switzerand, E-Mails: ssharma@biocuzh ch (SKS); christen@bioc uzh.ch (P.C.) * Author to whom correspondence should be adiressed, E-Mail: markus tamas@emb.gu.9«, Tel: +46-31-786-2548; Fax: +46-31-786-3910. Received: 17 January 2014; in revised form: 14 February 2014 / Accepted: 19 February 2014 / Published: 25 February 2014 Abstract: While the toxicity of metals and metalloids lke arsenic, cadmium, mercury, lead and chromium, is undisputed, the underlying molecular mechanisms are not entirely lear. Genera consensus holds that proteins are the prime targets; heavy metals interfere with the physiological activity of specific, particularly susceptible proteins, either by forming a complex with functional side chain groups or by displacing essential metal ions in metalloproteins. Recent studies have revesled an axditional mode of metal action targeted at proteins in a non-netive state; certain heavy metals and metalloids have been found to inhibit the in vitro refolding of chemically denatured proteins, to interfere with Protein folding in vivo and to cause aggregation of nascent proteins in living cells Apparently, unfolded proteins with motile backbone and side chains are considerably more Prone to engage in stable, pluridentate metal complexes than naive proteins with their wal-defined 3D structure, By interfering withthe folding process, heavy metal ions and rmetaloids profoundly affect protein homeostasis and call vicilty. This review describes how heavy metas impede protein folding and promote protein aggregation, how cals regulate qualty control systems to protec themselves from metal toxicity and how metas ‘might contribute to protein misfokding disorders,DTA CHUE STO CULC SM Ace AA VELAPerubahan Warna Sebelum CuSO« Setelah CuSOs Kesimpulan Daftar Pustaka DokumentasiNama NIM Kelas Kelompok Prinsip Kerja Prosedur Kerja*Lampiran Jural Hmiah Bakti Farmasi, 2018, 11(2), hal. 1-6 ISOLASI PATI DARI TEPUNG UBI JALAR UNGU ‘Agnes Rendowaty', Ensiwi Munarsih, Fizmawatt Sekolah Tinggi timu Farmasi Bhakti Pert Pi 3 Aah No, 24 i Tn 1 alenbng Sumter Sean e-mail: ‘arendowaty@gmallcom, ABSTRAK ‘Ubi jalar ungu merupakan salah satu sumber karbohidrat dan serat serta dapat dimanfatkan dalam perbuatan produk olahan pangan berbahan dasartepung. Pengolahan ubijalarungu menjadi tepung selain dapat meningkatkan umur simpan, dan memudahkan untuk pengolahan menjadi produk makanan. Tepung ubi jalar diperoleh dengan cara pengukusan dan tanpa pengukusan dengan rendemen masing-masing 19,76 % dan 30,16 %. Tepung dengan pengukusan mempunyai aroma sedikit ubi jalar ungu, berwarna kecoklatan dan berasa manis. Tepung tanpa pengukusan ‘mempunyai aroma khas ubi jalar ungu, warna keunguandan rasa agak manis. Pati yang terkandung dlidalam tepung dapat diperoleh dengan tekhnik pengendapan dengan pelarut air. Rendeman pati dar tepung dengan pengukusan 16,26 % dan tanpa pengukusan 7,74 %. Pati dengan pengukusan dengan penambahan larutan Iodium membentuk wara kuning Kecoklatan dan pati tanpa pemanasan berwama kebiruan, Pengamatan mikroskopis pati dengan pengukusandiperolehbentuk ‘ulat lonjong dengan ukuran yang lebih besardibandingkan pati tanpa pengukusan. ata Kunci: pati bi alr ungu, tepung, pengukusan, PENDAHULUAN Ubi jalar merupakan umber seayara nos yang moe sebagai antioksdan,antosinin adalah flavonoid yang bertanggung jawab terhadap wama pigmen ‘wama iru, ungu, vile, merah (Armanzah dan Hendrawati, 2016). ‘Umbi-umbian tinge arbohidrat dimanfatkan dalam ”-pembuatan produk olahan pangan berbahan dasar_ tepung (Widitmoko dan Estiasih, 2015). Tepung merupakan salah sat bentuk altenatifproduk setengah jadi yang lebih lama dsimpan, Cyan ht 201. Pembuatan t peneltian Husna (2010) dibuat dengan eng ping obi le pa the 100°C, dilanjutkan dengan pengeringan (oven dan matahar), dan tepang ubi jalan diasan ea potorganb iis ten yang ‘ui jalar berdasarkan dlikukus selama 10 menit dan likeringkan dengan oven pengering memilik Karabterstik ‘terbaik dengan kadar air 7,17 %b/b. Waktu oven. yang ‘60°C selama 1-3 hari (Zahro dkk, 2009) ‘Ubi ungu sebagai sumber pati an tinge! antosianin (Widiatmoko dan Estiasih, 2015). Patt vera berth Dentuk tama karbohidrat yang tesimpan di tanaman yang terri dari ‘nam cincin glukosa (glucopyranosa) (Jane, 158), Pe ee al eh iced dengan pelarut yang berbeda yaitu natrium lorida (0.5 %) dan atrium metabisufit (0,01%) dan_diperoleh pati. masing-masing 26,80 % dan 59,86 % (Kale dik, 2017) Oleh arena itu, penulis tertarik untuk melakukan peneitian solast pati dari tepung bi fala tungu. Tepung ibu jalar un Ape dng dengan dat mee ya dengan pengukusan dan tampa pengukusan, Pembuatan tepung secara umum meliputi ‘Agnes Rendowaty dk