Review

Gelatin alternatives
for the food industry:
recent
developments,
challenges and
prospects
A.A. Karim
*
and Rajeev Bhat
Food Biopolymer Research Group, Food Technology
Division, School of Industrial Technology, Universiti
Sains Malaysia, 11800 Penang, Malaysia
(Tel.: D6046532268; fax: D6046573678;
e-mail: akarim@usm.my)
Gelatin is regarded as a special and unique hydrocolloid, serv-
ing multiple functions with a wide range of applications. The
main sources of gelatin include pigskin, cattle bones and cattle
hide. Gelatin replacement has been a major issue in recent
years due to the emerging and lucrative vegetarian, halal
and kosher markets. It has recently gained increased interest,
especially within Europe, with the emergence of bovine spon-
giform encephalopathy (BSE) in the 1980s. In this paper, we
will discuss the unique properties of gelatin, the rationale for
developing gelatin alternatives, the progress to date of research
in development of gelatin alternatives, possible approaches for
developing gelatin alternatives, and future directions for re-
search in this area.
Introduction
Among commercial hydrocolloids used in the food in-
dustry, gelatin has been regarded as special and unique,
serving multiple functions with a wide range of applica-
tions in various industries. Gelatin has long been used as
a food ingredient (e.g., gelling and foaming agent), in the
preparation of pharmaceutical products (e.g., soft and
hard capsule, microspheres), in the biomedical eld (wound
dressing and three-dimensional tissue regeneration) and in
numerous non-food applications (e.g., photography). It is
a product obtained by partial hydrolysis of collagen derived
from animal skin, white connective tissue, and bones (Mor-
rison, Sworn, Clark, Chen, & Talashek, 1999). So far, the
main sources for commercial gelatin are limited to pig
skins or cow skins and bones, perhaps due to the relatively
low cost of the nal gelatin product.
The issue of gelatin replacement has existed for many
years for the vegetarian, halal and kosher markets, but has
gained increased interest in the last decade, particularly
within Europe with the emergence of bovine spongiform
encephalopathy (mad cowdisease) in the 1980s (Morrison
et al., 1999). Since then, there has been much concern about
using gelatin derived from possibly infected animal parts.
Since most commercial gelatins are obtained from either
pigskin or cow hide, there has been considerable interest in
nding and using alternative substitutes. As a result, acade-
mia and industry have been trying for many years to develop
alternatives to gelatin that possess most or all of the unique
functional properties of mammalian gelatin. Driven by the
foreseeable demand for halal/kosher gelatin, industries are
now striving to develop gelatin-free products in which
mammalian gelatin is no longer used, either as a processing
aid or as an ingredient. The search for new gelling agents
to replace mammalian gelatin led to patents for sh gelatin
production (Grossman & Bergman, 1992) as well as several
published methods for sh gelatin extraction (Gomez-Guillen
et al., 2002; Gudmundsson & Hafsteinsson, 1997). In
addition, various patents have been published on the
development of gelatin alternatives or substitutes from plant
hydrocolloids such as starch/modied starch, pectin,
carrageenan and agar.
A number of review articles (Babel, 1996; Baziwane &
He, 2003; Djagny, Wang, & Xu, 2001; Ledward, 1996;
Veis, 1964; Wasswa, Tang, & Gu, 2007; de Wolf, 2003)
and books (Schrieber & Gareis, 2007; Ward & Courts,
1977) on gelatin have been published. To our knowledge,
a comprehensive review on gelatin alternatives is not yet
available. Therefore, in this paper we will discuss the
unique properties of gelatin, the rationale of developing
gelatin alternatives, the various studies and approaches
that have been undertaken to develop gelatin alternatives,
and some challenges and prospects. Direction for future
studies will also be suggested. * Corresponding author.
0924-2244/$ - see front matter 2008 Elsevier Ltd. All rights reserved.
doi:10.1016/j.tifs.2008.08.001
Trends in Food Science & Technology 19 (2008) 644e656
Rationale for developing gelatin alternatives
Religious and vegetarian lifestyle choices may prohibit
certain consumer groups from eating foods like yogurt,
whipped desserts, low-fat margarine spreads, marshmal-
lows, ice cream, and other products containing gelatin, an
animal-based ingredient. The worldwide production of gel-
atin in 2007 was about 326 000 tons, of which 46% were
from pigskin, 29.4% from bovine hides, 23.1% from bones,
and 1.5% from other parts (GME, 2008a, 2008b). Produc-
tion of gelatin from pig skins is not acceptable for Judaism
and Islam, and gelatin from cattle is acceptable only if it
has been prepared according to religious requirements.
Therefore, to cater to this market segment, the development
of gelatin alternatives is highly desirable to food processors
as the global market for foods certied halal is growing
very rapidly. Indeed, the halal marketplace is emerging
as one of the most lucrative and inuential market arenas
in the world. Global trade in halal food products has
been estimated to be around 80 billion US dollars, or
some 12% of total trade in agri-food products (Anony-
mous, 2007a). With expected increases in both population
and incomes of halal consumers, this percentage is certain
to increase. Furthermore, with Muslims projected to ac-
count for 30% of the worlds population by 2025, halal
food could easily account for 20% of world trade in food
products (Anonymous, 2007a). Gelatin alternatives would
also cater to other consumer groups such as Jews, Hindus
and vegetarians. It is obvious that with growing interest
in this market sector, development of gelatin alternatives
would enable the industry to tap the enormous potential
size of the halal market.
In addition to religious issues, the risk of potential con-
tamination with viruses and prions, such as the BSE prion,
which was responsible for the human CreutzfeldteJacob
disease (CJD) in the 1980s, causes concerns in the ingredi-
ent and food-processing industries as well as in medical and
pharmaceutical industries. Because gelatin is a slaughter-
house by-product, it is difcult to control and check its pro-
duction process and to completely guarantee its safety, even
though the gelatins that are produced can actually be qual-
ied as safe. A study released in 2004 (Grobben, Steele,
Somerville, & Taylor, 2004), however, demonstrated that
the gelatin production process destroys most of the BSE
prions that may be present in the raw material. Similarly,
subsequent to the evaluation of validation studies on the
manufacturing processes used for bovine gelatin, in 2003
the Food and Drug Administration (FDA) commented on
the safety aspects as follows: The data obtained from
these new studies show that the reduction in BSE infectivity
is sufcient to protect human health (Schrieber & Gareis,
2007). In another statement dated January 18, 2006, the
European Food Safety Authority (EFSA) stated that the
residual BSE risk in bone-derived gelatin is regarded as
being very small compared to the historical consumption
of meat or meat products in the UK (Schrieber & Gareis,
2007).
The chemistry and structure of collagen and gelatin
Collagen is the source protein from which gelatin is pre-
pared in bulk quantities. It functions as extracellular, struc-
tural protein in bone, tendon, skin and the connective tissue
of various organs. The characteristic feature of collagen is
the presence of one or more domain(s) with exceptional
amino acid composition (33% glycine and 22% proline)
and exceptional structure: the (rigid) triple extended helix.
The triple-helix structure is characterized by three extended
left-handed polyproline II-like helical chains that are super-
coiled into a right-handed triple helix. The three chains are
staggered by one residue with respect to each other, and are
linked through interchain hydrogen bonds. The triple-
helical conformation is associated with a distinctive amino
acid sequence with glycine as every third residue and a high
content of imino acids (de Wolf, 2003).
During gelatin production, the extraction of collagen
from conditioned tissue by hot water denatures the triple-
helical structure into individual soluble chains, or small
polymers or fragments. On cooling, the chains can rewind
into new triple-helical structures, but not necessarily in
the same register as the native collagen structure, limiting
the extent of re-formed triple helix. The re-forming of tri-
ple-helical segments leads to junction zones that are neces-
sary for gelation (de Wolf, 2003). The pyrrolidine-rich
regions act as nucleation sites for formation of potential
junction zones (Harrington & Rao, 1970) and the length
of a junction zone has been proposed to be at least 20e
30 amino acids. It is generally believed that the junction
zones in gelatin are stabilised by hydrogen bonds similar
to those in native collagen. The junction zones are intercon-
nected through exible peptide chains (elastic segments).
In the manufacture of gelatin, treatment of the animal
raw material with dilute acid (type A gelatin) or alkali
(type B gelatin) results in partial cleavage of protein
cross-links; the structure is broken down to such an extent
that warm water-soluble collagen, that is, gelatin, is
formed (Schrieber & Gareis, 2007). Breakdown is largely
dependent on the three factors of temperature, time, and
pH. High temperatures and long periods of exposure to
heat accelerate the process (Schrieber & Gareis, 2007).
Functional properties and uses of gelatin
Gelatin displays multiple functional roles in food pro-
cessing and formulations. The functional properties of gel-
atin can be divided into two groups (Schrieber & Gareis,
2007). The rst has properties that are associated with gel-
ling, for example, gel strength, gelling time, setting and
melting temperatures, viscosity, thickening, texturizing,
and water binding. The second group relates to the surface
behavior of the gelatin, for example, emulsion formation
and stabilization, protective colloid function, foam forma-
tion and stabilization (such as in marshmallow), lm forma-
tion, and adhesion/cohesion (Schrieber & Gareis, 2007).
None of the hydrocolloids currently on the market is capa-
ble of covering all of the above-mentioned properties in all
645 A.A. Karim, R. Bhat / Trends in Food Science & Technology 19 (2008) 644e656
applications (Schrieber & Gareis, 2007). Comparison of
rheological and functional properties of gelatin with other
common food hydrocolloids is shown in Tables 1 and 2.
The most common use of gelatin is its thermally revers-
ible gelling properties with water as, for example, in the
production of table jellies. An aqueous solution of a few
percent gelatin forms thermally reversible gels with water,
and the gel-melting temperature (<35

C) is below body
temperature, which gives gelatin products unique organo-
leptic properties and avor release (Glicksmann, 1969).
The thermoreversibility of this process gives the gelatin
gel its unique melt-in-mouth quality. Other gelling
agents such as starch, alginate, pectin, agar, and carra-
geenan are all polysaccharides from plant sources, but their
gels lack the melt-in-the-mouth, elastic properties of gelatin
gels. Gelatin is notable for its gelling properties and clean
avor prole. The gelatin gel has been described as having
a sparkling and clear appearance with clean melt-in-the-
mouth texture that has yet to be duplicated by any polysac-
charide (Baziwane & He, 2003).
The most important attribute of gelatin is its gel
strength and when determined by the standard method,
is called the Bloom strength or Bloom value. In de-
termining the value, the force required to depress the sur-
face of a 6.67% gel by a plunger with a specic shape and
size by 4 mm is measured 18 h after the gel has been
stored at exactly 10

C. Commercial products normally
have Bloom values between 50 and 280 (Schrieber &
Gareis, 2007).
Gelatin has a considerable number of food applications
and uses (Cole, 2000; Hudson, 1994; Keenan, 1994;
Poppe, 1997). Table 3 lists the advantages and advantages
of using gelatin in food applications. Gelatin has been
used in foods as a beverage clarier, a ning agent for
white wine, as a beer clarier, and to clarify fruit and veg-
etable juice (especially for claried apple juice and pear
juice). Gelatin is used in desserts at 8e10% of the dry
weight, in yogurt at 0.3e0.5% as a thickener, in ham coat-
ings at 2e3%, and in confectionery and capsules (vitamin
supplements) at 1.5e2.5% (Igoe, 1983). Further uses in-
clude: fruit toppings for pastry, instant gravy, instant sau-
ces and soups, edible lms for confectionery products
(McCormick, 1987), and as a stabilizer in ice cream,
cream cheese, and cottage cheese as well as in food foams
and fruit salads. Overall functional uses include as a stabi-
lizer, thickener, and texturizer. Schrieber and Gareis
(2007) have discussed in detailed various food and non-
food applications of gelatin.
The unique properties of gelatin
Gelatin offers many special properties that are not easily
imitated by other hydrocolloids. An ideal gelatin alternative
should, therefore, posses all or at least some of the follow-
ing properties:
Table 1. Comparison of frequently used hydrocolloidsdrheological properties
Hydrocolloids Gel formation Thickening
effect
Transparency
of the gel
Cold water solubility pH-stability
Gelatine
Thermoreversible, difference in
melting/gelling temperature low
0
With the exception of cold water-soluble
instant gelatins and gelatin hydrolysates

Agar-agar
Thermoreversible, difference in
melting/gelling temperature high
0
Alginates (with calcium)
Carrageenan Kappa/iota: (with cations)
Lambda: 0

Carboxymethyl
cellulose (CMC)
0 e (pH 3-11)
Gum arabic 0 e (pH 4-9)
Hydroxypropylmethyl
cellulose (HPMC)
(Gel formation on heating) (pH 1-10)
Locust bean gum 0 _ (pH 3-11)
Modied starches 0
With the exception of physically modied
starches

Native starches 0
Pectin
- Low methoxy plus Ca
2
thermally
irreversible
- High methoxy plus sugar H

thermoreversible

- High methoxy:
pH 2.5-4.5
- Low methoxy:
pH 2.5-5.5
Reproduced with permission from Schrieber and Gareis (2007). Copyright Wiley-VCH Verlag GmbH & Co. KGaA. Qualitative assessment:
0 none; high.
646 A.A. Karim, R. Bhat / Trends in Food Science & Technology 19 (2008) 644e656
Melt-in-the-mouth propertydThe physical character-
istics of gelatin, such as melting slightly below the phys-
iological temperature of humans, gives the polymer the
special melt-in-mouth perception leading to intensive
avor and aroma release. This behavior is one of the
most important characteristics of gelatin systems (such
as gelatin-based gel desserts) and is hard to mimic in
other biopolymer systems. So far scientists have not
been able to nd a gelling protein or polysaccharide,
which universally can replace gelatin as a gelling agent
(Haug, Draget, & Smidsrod, 2004a).
Thermally reversible geldUnlike most protein and
polysaccharide gels, gelatin gels are thermoreversible,
since on warming the gel will dissolve. Some plant hy-
drocolloids such as carrageenan and agar form thermally
reversible gels too, but the melting points are signi-
cantly higher than for gelatin gels.
One other important feature of gelatin is also the surface
activity. Gelatin is not brilliant compared to gum arabic
when it comes to surface activity and emulsifying/stabil-
ising properties, but still this is an important characteris-
tic of gelatindespecially in combination with the gel
forming abilities of gelatin.
Versatile, multi-functional hydrocolloiddGelatin can be
considered one of the most versatile hydrocolloids in the
food industry. Gelatin is multi-functionaldit can be
used as a gelling, thickening, water-binding, emulsify-
ing, foaming, lm-forming agent. No other single hydro-
colloid offers the same combination of functionalities
(Schrieber & Gareis, 2007).
Tailor-made applicationdGelatin is available in differ-
ent gel strengths and particle sizes and can be tailor-
made for specic applications. Generally, other hydro-
colloids do not cover a range of gel strengthsdmodica-
tion of jelly strength is therefore achieved by blending
with other ingredients such as sugars and salts (GME,
2008a, 2008b).
Gelatin is easy to usedit gels within the normal pH
range of most foods and does not require the addition
of salts or sugars to set. Other gelling hydrocolloids
Table 2. Comparison of frequently used hydrocolloidsdfunctional properties
Hydrocolloid Syneresis Film
formation
Emulsier
effect
Protective
colloid
effect
Effects with other hydrocolloids
Gelatine 0 Flocculation possible with agar-agar, carrageenan, LM. Pectin,
alginates, gum arabic, CMC
Agar-agar 0 0 Locust bean gum or guar; low level of syneresis, more gel
elasticity
Alginates Locust bean gum or guar; low level of syneresis, more gel
elasticity
Carrageenan Kappa:

Iota:
Locust bean gum or guar; low level of syneresis, more gel
elasticity
Carboxymethyl cellulose
(CMC)
0 Technological potential as with locust bean gum, guar, and HM
pectin
Gum arabic 0 Gelatin: coacervate formation
Hydroxypropylmethyl
cellulose (HPMC)
0 Technological potential as with xanthan
Locust bean gum 0 0 Xanthan: increase in viscosity (gel)
Gelling agent: low level of syneresis
Modied starches 0 Gelatin: improved setting
Guar: increase in viscosity
Native starches 0 0 Gelatin: improved setting
Guar: increase in viscosity
Pectin 0 0 Flocculation possible with gelatin
Xanthan 0 Locust bean gum: increase in viscosity (gel)
Guar: increase in viscosity
Reproduced with permission from Schrieber and Gareis (2007); Copyright Wiley-VCH Verlag GmbH & Co. KGaA. Qualitative assessment:
0 none; high.
Table 3. Advantages and disadvantages of gelatin in food
applications
Advantages Disadvantages
Multifunctional (texture, surface
activity, emulsier, stabilizer,
lm former)
Low stability to heat
Melts at body temperature with
rapid and intense release of avor
Low gelation temperature
Slow gelation
Unique texture, elasticity and
brilliance
Soluble only at higher
temperatures (exceptions: Instant
gelatin and gelatin hydrolysates)
Easy to process BSE discussion
No. E-No. (food) Animal source (vegetarians/
vegans)
Preventive function in
osteoarthritis and osteoporosis
Religious reservations
Protein enrichment
Reproduced with permission from Schrieber and Gareis (2007);
Copyright Wiley-VCH Verlag GmbH & Co. KGaA.
647 A.A. Karim, R. Bhat / Trends in Food Science & Technology 19 (2008) 644e656
often require the addition of salts, food acids or sugars to
form a gel (GME, 2008a, 2008b).
Possible approaches for the development of gelatin
alternatives
It is evident that the task of nding an ideal alternative to
mammalian gelatin is very difcult, if not impossible. Ac-
cording to Morrison et al. (1999), the approach to develop-
ing gelatin alternatives for the food industry should be
application/process-specic. It is unlikely that a universal
ingredient will replace gelatin in every food application.
Morrison et al. (1999) have proposed some examples of
gelatin alternatives (Table 4). In the following discussion,
several gelatin alternatives will be considered, including
sh gelatin, thermoreversible gel from polysaccharides,
and mixed polysaccharide-based systems.
Fish gelatin
Gelatin from marine sources (warm- and cold-water sh
skins, bones, and ns), which has not been previously ex-
plored, is a possible alternative to bovine gelatin (Kim &
Mendis, 2006; Rustad, 2003; Wasswa et al., 2007). One
major advantage of marine gelatin sources is that they are
not associated with the risk of bovine spongiform enceph-
alopathy outbreaks. Fish gelatin is acceptable for Islam
and with a minimum restriction for Judaism. Furthermore,
sh skin is a major by-product of the sh-processing indus-
try, causing wastage and pollution, and could provide
a valuable source of gelatin (Badii & Howell, 2006).
Physicochemical and functional properties of sh
gelatin
Fish collagens, in general, have lower imino acid con-
tents than mammalian collagens and this may be the reason
for the lower temperature of denaturation (Grossman &
Bergman, 1992). Haug et al. (2004a) conducted similar
comparative study on rheological properties of sh and
mammalian gelatin and found that the main difference
between sh and mammalian gelatin is the content of the
imino acids proline and hydroxyproline, which stabilizes
the ordered conformation when gelatin forms a gel net-
work. The lower content of proline and hydroxyproline
probably gives sh gelatin its low gel modulus, gelling
and melting temperature.
Cold-water sh gelatins, such as those extracted from
pollock and salmon, have very low gelling (typically below
8

C) and melting temperatures compared to mammalian
and warm-water sh gelatins. Cold water sh, for example,
cod, have a very low hydroxyproline content and coupled
with this a very low gelling and melting temperature. For
example, 10% mammalian gelatin forms a gel at approxi-
mately room temperature, whereas 10% cod will just about
gel at w2

C (Gilsenan & Ross-Murphy, 2000). This is due
to the cold-water shes having lower concentrations of pro-
line and hydroxyproline than the other species (Haug et al.,
2004a). The amino acid compositions of mammalian gela-
tins are remarkably constant when compared to those from
different species of sh.
Choi and Regenstein (2000) found sh gelatin to have
similar physical and chemical properties compared to por-
cine gelatin and to be rated superior in a blind sensory test.
They also established that the lower melting point of cold-
water sh gelatin enhances avor release, fruit aroma, and
melt rate in water gel desserts.
Problems associated with sh gelatin
Although sh gelatin is considered an attractive alterna-
tive for mammalian gelatin, the commercial interest in uti-
lization of sh gelatin has thus far been relatively low.
There seem to be many challenges before sh gelatin nds
widespread usage as an alternative to mammalian gelatin in
the food industry. Typical problems associated with sh
gelatin from cold water species, which represent the major-
ity of the industrial sheries, are sub-optimal physical and
functional properties compared to mammalian gelatin (such
as low gelling and melting temperature and low gel
Table 4. Functional properties of gelatin in selected food applications with possible alternatives
Food application Desired gelatin properties Current alternatives Technical constraints of alternative
Desert gels RTE Clarity, elastic texture, melt in mouth Algin, gellan and carrageenan
systems
Hot viscosity, higher set temperature
High-solids
confectionery
Elastic texture, clarity, low hot
viscosity, low set temperature
Gellan gum blends, carrageenan
systems, thinned-starch systems
Set temperature and hot viscosity, texture-
elasticity gels
Foamed
confectioneryd
marshmallows
Whipping/aeration agent,
foam stabiliser, elastic texture
Gellan/starch/emulsier blends,
modied starch/emulsiers
Textural constraintsdlow elasticity and/or
high set temperature
Low-fat spreads Elastic gel texture, fatlike melt mouthfeel,
emulsion stabilization
Sodium alginate/gellan/inulin/
simplesse/maltodextrin/gum blends
Cost competitive, but good application for
alternatives
Stirred yogurt Creamy mouthfeel, gelled network
prevents separation or syneresis
Gellan/modied starch/xanthan/LBG/
pectin/modied starch
High viscosity and high set temperature in
culture/production process
Dessertsd
Mousses
Whipping agent, creamy
consistency, low set temperature
Alginate/starch blends Current production process, stored prior to
aeration chilling
Sour cream Smooth texture, creamy mouthfeel Gellan gum with modied starch High set temperature during processing
From Morrison et al. (1999), with kind permission of Springer Science Business Media.
648 A.A. Karim, R. Bhat / Trends in Food Science & Technology 19 (2008) 644e656
modulus) (Haug et al., 2004a; Leuenberger, 1991). Fish
gelatin (especially from cold water sh) does not gel at
room temperaturedthe gelling temperature of cold water
gelatin is typically below 8e10

C (depending on the gela-
tin concentration, average molecular weight, ionic strength,
pH, cooling rate and method of determination; Cheow, Nor-
izah, Kyaw, & Howell, 2007; Montero & Gomez-Guillen,
2000; Norland, 1990). Haug et al. (2004a) reported that
for type A sh gelatin (produced from skins of cold-water
sh species such as cod, haddock and pollock), the gels ex-
hibited considerably lower storage modulus, G
0
, lower gel-
ling (4e5

C) and melting temperature (12e13

C)
compared to mammalian gelatin gels. This makes these gel-
atins unsuited as mammalian gelatin replacements.
The inferior gelling property and the large variation in
quality between different sh species are issues that need
to be addressed. According to Gomez-Guillen et al.
(2002), the use of sh skin for gelatin production has to
take into account at least two different aspects. First, the
wide diversity among the sh species presents intrinsic
differences in the collagen molecules present in their skin.
Second, the collagenous material from sh skin is more sus-
ceptible to degradation during chemical treatment (acid or
alkali) due to the lower content of intra- and interchain
non-reducible cross-links (Montero, Border as, Turnay, &
Lizarbe, 1990; Norland, 1990), in contrast to the more stable
collagen from mammals (Asghar & Henrickson, 1982). As
reviewed by Stainsby (1987) and Johnston-Banks (1990),
the physical properties of gelatin depend not only on the
amino acid composition, but also on the relative content of
a-chains, b- or g-components and higher molecular weight
aggregates, as well as on the presence of low molecular-
weight protein fragments. Thus, in addition to the source
or species, gelatin properties will also strongly depend on
the preservation of the raw material.
Enhancing gel strength of sh gelatin
The quality of a food grade gelatin depends to a large ex-
tent on its rheological characteristics such as viscosity and
viscoelastic properties. From the preceding discussion, it is
obvious that sh gelatin is not directly exchangeable with
mammalian gelatin due to low gel strength as well as low
gelling and melting point. To overcome or minimize some
of the problems associated with inferior properties of sh
gelatin, three different approaches have been attempted:
enzymatic cross-linking of gelatin using enzymes such
as transglutaminase (Yi, Kim, Bae, Whiteside, & Park,
2006) or tyrosinase;
mixed gelling systems of sh gelatin and suitable plant
hydrocolloids which may give higher gel strength, gel-
ling and melting temperature;
manipulating the characteristics of gelatin by the addi-
tion of solutes, such as salts.
Transglutaminases (TGase) have been shown to cross-
link gelatin (Babin & Dickinson, 2001; Fuchsbauer et al.,
1996; Lim, Mine, & Tung, 1999). The enzyme acts by cat-
alyzing an acyl transfer reaction between the g-carboxa-
mide group of glutamine residues and the e-amino group
of lysine residues of peptide chains (Folk & Finlayson,
1977). The covalent cross-linking action of TGase is ex-
pected not only to modify rheological properties but also
to alter the reversibility of such gelatin gels. Babin and
Dickinson (2001) reported that the gel strength might be ei-
ther reduced or enhanced depending on whether covalent
cross-linking occurs predominantly before or after develop-
ment of the triple helical junction zones. Previous studies
(Fuchsbauer et al., 1996; Lim et al., 1999) have shown
that once gelatin is cross-linked by TGase, this protein loses
the ability to undergo thermally reversible transitions at
temperatures characteristic of gelatins coil-to-helix transi-
tion. Presumably TGase-catalyzed cross-linking occurs in
the tripeptide repeat region that is responsible for gelatins
helix-forming ability. Gomez-Guillen, Sarabia, Solas, and
Montero (2001) reported that the addition of microbial
TGase to a sh skin gelatin could considerably raise melt-
ing point, gel strength and viscosity at 60

C, depending on
the concentration of the enzyme and incubation time.
The results of these cross-linking studies indicate the po-
tential of using food-grade TGase to control properties of
sh gelatin gels. However, apart from the high cost of the
enzyme, achieving compromise between gel strength and
thermoreversibility would depend on getting good control
of the degree of cross-linking and perhaps other factors
(e.g., molecular weight of gelatin). As pointed out by Babin
and Dickinson (2001), the challenge is to maintain the
physical character of the gelation, even after substantial co-
valent cross-linking (i.e., the cold-set gelatin gel melts
again on heating to >35

C). Babin and Dickinson also
suggested that another interesting possibility for further
work would be to cross-link gelatin with another protein.
This approach has been examined by Nokana, Matsuura,
and Motoki (1997) with casein.
Combinations of gelling agents are often used in food
products to achieve a desirable texture. Gelation is either
inhibited or enhanced and the texture of the gel can be
very different from those of the gels formed by the compo-
nents alone (Oakenfull, 1987). With some ingenuity, phys-
ical properties of mixed biopolymer systems can be more
nely controlled. For this reason, mixed systems are of
great technological importance and can be used as one of
the approaches to modulate the strength of the gelatin
gel. Improvement of gel strength of gelatin using modied
starch has been described in several patents (Helmstetter,
1977; Szymanski & Helmstetter, 1975). Haug, Draget,
and Smidsrd (2004b) reported that a mixed gelatin-k-car-
rageenan gel system could be formulated carefully leading
to systems with improved gel strength, gelling and melting
temperature.
The outcome of blending gelatin with other hydrocol-
loids can be both positive and negative (Schrieber & Gareis,
2007). Gellan gum, for example, accelerates the gelling
649 A.A. Karim, R. Bhat / Trends in Food Science & Technology 19 (2008) 644e656
speed of gelatin and substantially increases gel rmness,
but reduces color and clarity. On the other hand, blending
of gelatin with citrus pectin reduced the rmness of the gel-
atin gel. Carrageenan has an even stronger negative effect
on rmness, color, and clarity of gelatin gels (Schrieber
& Gareis, 2007).
Combinations of gelatin and agar-agar, however, have
created new opportunities. According to Schrieber and Gar-
eis (2007), combination of these two hydrocolloids consid-
erably increased the degrees of rmness than with gelatin
alone, and the melting point of the gel can increase up to
80

C. In the case of fruit gummies, the melting tempera-
ture can be increased to about 50

C, hence making the
product suitable for marketing in tropical climates. How-
ever, if these hydrocolloids are to be fully utilized in prac-
tice, numerous other factors have to be taken into
consideration (Schrieber & Gareis, 2007).
Another possible means of manipulating the characteris-
tics of a given gelatin is to trigger interactions by the addi-
tion of solutes such as salts (Elysee-Collen & Lencki, 1996;
Fernadez-D az, Montero, & Gomez-Guillen, 2001). Sara-
bia, Gomez-Guillen, and Montero (2000) found that it
was possible to improve the functional properties of sh
gelatins such as megrim skin gelatin to achieve characteris-
tics similar to those of gelatins from warm-blooded ani-
mals, chiey with regard to melting point, by the addition
of neutral salts in appropriate conditions of pH and ionic
strength.
Development of thermoreversible gel from
polysaccharides
An interesting and perhaps signicant development in
the search for gelatin alternatives is the development of
starch gel that is thermally reversible. A number of studies
(Hansen, Blennow, Pederson, Nrgaard, & Engelson, 2008;
Kaper et al., 2005; Lee, Yong-Ro Kim, Park, & Lee, 2006;
van der Maarel et al., 2005) and patents (Buwalda, Meima,
& Woltjes, 2005; Euverink & Binnema, 2005; Trzasko,
Tessler, & Dirscherl, 1986) have been published on the de-
velopment of thermally reversible gel from starch/modied
starch. Most of these studies or inventions are based on the
application of carbohydrate-active enzymes (4-a-glucano-
transferase, E.C. 2.4.1.25 or also called D-enzyme) that cat-
alyzes the transfer of glucan units from one a-glucan to
another in a disproportionation reaction. These enzymes
are involved in starch metabolism in plants or maltose/gly-
cogen metabolism in many microorganisms. Typically, en-
zymatic modication of starch employs hydrolyzing
enzymes such as a-amylase, pullulanase and glucoamylase
which hydrolyze the a-1,4- or a-1,6-glycosidic bonds in
amylose and amylopectin by rst breaking the glycosidic
linkage and subsequently using a water molecule as accep-
tor substrate. D-enzyme also initially breaks the glycosidic
linkage but instead of water they use another oligosaccha-
ride as an acceptor substrate and form a new glycosidic
linkage. This new linkage can either be intramolecular,
a reaction catalyzed by the enzyme cyclodextrin glycosyl-
transferase, or intermolecular, for example, catalyzed by
amylomaltase or glucan-branching enzyme (van der Maarel
et al., 2005). D-enzyme can use high molecular-weight
starch as both donor and acceptor molecule and can cata-
lyze the transfer of long a-1,4-glucan chains (Takaha,
Yanase, Takata, Okada, & Smith, 1996), or even highly
branched cluster units of amylopectin.
Kaper et al. (2005) reported that thermostable amylo-
maltase modies potato starch to form a thermoreversible
gel with gelatin-like properties. The enzyme was able to
produce starch product that formed a strong white gel
upon incubation at 4

C with a thermoreversible character.
Iodine complex formation and an analysis of the side chain
distribution demonstrated that the amylomaltase transfers
the amylose molecules in part to the side chains of the am-
ylopectin. As a result, amylomaltase-modied gels retro-
graded reversibly, comparable to gelatin gels. They also
observed that both amylomaltase-modied starch and gela-
tin form rm gels but the gelatin bloom 250 gel is stronger
and sets faster. Furthermore, the two gels were found to
have different mouthfeel. As for the melting point, gelatin
bloom 250 gels melt completely at 37

C. On the other
hand, amylomaltase-modied starch gels are 50% melted
at 37

C, while 100% melting is reached at 60

C. The au-
thors suggested that amylomaltase-modied starch should
not be regarded as a replacement for gelatin but rather as
an extension of the variety of available gelling products
with their own specic applications.
Other potential polysaccharide-based gelatin
alternatives
Many gelatin alternatives proposed for the food industry
are polysaccharides, which gel based on cation-induced
junction zones, and which do not have the dened melt-
set characteristics of gelatin, such as gellan, alginate or
carrageenan-based gels. The polysaccharide-based gelatin
alternatives generally have less exible molecular
backbones, leading to higher viscosities than gelatin
(Morrison et al., 1999).
The ability of some hydrocolloids to form a synergistic
gelation could be exploited to produce gels having similar
melt-in-mouth properties as gelatin gels. For example,
it is well known that xanthan, the extracellular bacterial
polysaccharide from Xanthomonas campestris, cannot
form a gel on its own but can form strong, cohesive gels
with certain plant polysaccharides, notably locust bean
gum (LBG) and konjac glucomannan (KGM) (Dea & Mor-
rison, 1975; Fitzsimons, Tobin, & Morris, 2008).
Agoub, Smith, Giannouli, Richardson, and Morris
(2007) have suggested that mixtures of pyruvate-free xan-
than and konjac glucomannan (KGM) could provide a use-
ful replacement in applications where melt-in-mouth
characteristics are important for product quality, and where
moderate acidity is acceptable or necessary (e.g., fruit
jellies). They observed that mixtures prepared at pH values
650 A.A. Karim, R. Bhat / Trends in Food Science & Technology 19 (2008) 644e656
in the range 4.0e3.5 gave comparable moduli at room tem-
perature (20

C) to those obtained at neutral pH, but
showed substantial softening on heating to body tempera-
ture, suggesting possible applications in replacement of
gelatin in products where melt-in-the-mouth characteris-
tics are important for acceptability to the consumer.
Mixed high methoxyl/low methoxyl pectin gels
Both high methoxyl (HM) and low methoxyl (HM) pec-
tins have their own limitation with respect to requirements
for gelation. HM pectin is not considered a good candidate
as gelatin alternative because it forms thermally irreversible
gel, in addition to the strict requirements of low pH and
high soluble solids. On the other hand, LM pectin appears
to be more exible in terms of manipulation of gelling con-
ditions but at high sucrose concentrations LM pectin too
tends to pregel (May, 1990). Mixtures of pectins are often
used in food applications to obtain products with certain
functionalities. Therefore, modulation of gel properties
could be achieved perhaps through mixtures of HM and
LM pectin at certain proportion, together with judicious
control of Ca
2
, sugar, pH, and types (degree of esterica-
tion) of HM pectin. It has been shown (Lofgren, Walken-
strom, & Hermansson, 2002) that large variations in
rheological behavior and microstructure can be obtained
in mixtures of HM and LM pectin gels by altering the gel
formation conditions.
Moorehouse (2004) suggested that pectin could be used
as a replacement for gelatin in the production of marshmal-
lows. Typically this aerated product is produced from gela-
tin, which gives a strong elastic texture. While pectin does
not exactly reproduce this texture, the non-animal raw ma-
terial source or natural fruit basis of pectin, together with
excellent avor release and heat stability (for hot climate)
makes the use of specic HM pectins which gel at low
pH an interesting possibility. Among the many hydrocol-
loids that have been evaluated as gelatin replacers, only
pectin, carrageenan or combinations of pectin/carrageenan
give similar texture but not quite the exact melt-in-mouth
temperature as for gelatin.
Modied starch/wheat ber gel
In another study, Wang (2000) described gelatin replace-
ment in yogurt applications using combination of a dual
modied starch and wheat ber gel. He observed that the
ratio of starch to wheat ber gel is critical to the success
of complete replacement of gelatin. The optimum ratio
was found to be 60% starch to 40% wheat ber gel. The
starch portion contributes to the smooth texture and the im-
proved water holding ability of the nal products. Yogurts
made with gelatin replacer show higher stability against
storage temperatures higher than 20

C and display less
syneresis during storage. There are no signicant sensorial
differences between the yogurts made with gelatin and gel-
atin replacer.
High acyl gellan gum
High acyl gellan gum has been considered as a potential
gelatin alternative (Morrison, 2000). Gellan gum is a versa-
tile food ingredient providing a wide range of textures from
soft, elastic gels to rm, brittle gels with one label declara-
tion. Recent studies have shown that both the levels of glyc-
erate and acetate substituents in gellan gum can be
controlled independently (Morrison et al., 1999). Blends
of high (HA) and low (LA) acyl gellan gum can produce
intermediate gel textures. High acyl gellan produces soft,
elastic gels, which are thermoreversible. Applications in-
clude cultured dairy, dressings, jams and jellies, dessert
gels, dairy and fruit beverages, milk puddings and confec-
tionery. Actual examples are shown in two common food
applications of gelatin, that is, water jellies and high-solid
systems (Morrison et al., 1999) (Fig. 1). It can be seen
that in the water-based dessert gel formation (15% solids),
a partially deacylated form of HA gellan can closely match
the gelatin texture. This product will also be distinct from
gelatin, in that it will have a higher melt-set temperature,
which is advantageous for rapid-set formulations and for
stability in hot climates. In the high-solids example, the
partially deacylated product is much closer to the gelatin
texture than simple blends of HA and LA gellan gum
Brittleness Elasticity
Cohesiveness
Modulus
Hardness Hardness
Brittleness
Elasticity
Cohesiveness
Modulus
Gelatin
Partially deacylated gellan
(f
g
= 0.26, f
a
= 0.43)
Gelatin
LA/HA blend
Modified blend
a b
Fig. 1. Comparison of the texture of partially deacylated gellan gum samples with commercial gelatin formulations in (a) water-based dessert gels
(15% solids) and (b) a high-solids system (72% soluble solids). Residual glycerate and acetate substituents per repeat unit are denoted by f
g
and f
a
,
respectively (Morrison et al., 1999, with kind permission of Springer Science Business Media).
651 A.A. Karim, R. Bhat / Trends in Food Science & Technology 19 (2008) 644e656
components in terms of properties such as brittleness, elas-
ticity and cohesiveness (Morrison et al., 1999).
Carrageenan
Cash (2000) described the development of new iota car-
rageenan extract by using a new, proprietary extraction pro-
cess. A specic line of products has been developed for use
in the confectionery industry, particularly for gummi-type,
or moulded candies. These products are said to be suitable
alternatives for gelatin conventionally used in these prod-
ucts. The new iota carrageenan-based products allow for
shorter conditioning times, easier demoulding, and alter-
nate moulding processes. Cash also claimed that the use
of carrageenan instead of gelatin produced nished prod-
ucts that are more tolerant of excessively high temperatures
that may occur during shipping or storage.
Direction for future studies
As has been highlighted in the preceding discussion,
current commercial application of sh gelatin as an alterna-
tive to porcine/bovine gelatin is limited due to inherent
properties such as low melting point and weak gel strength
of sh gelatin gels. Currently sh gelatin is being used
mainly for niche markets only (Schrieber & Gareis,
2007). To get around these shortcomings, modication via
cross-linking has been attempted. Enzyme-catalyzed reac-
tions that are known to cross-link proteins are those cata-
lyzed by transglutaminase, lipoxygenase, polyphenol
oxidase, lysyl oxidase, tyrosinase, and peroxidase. Trans-
glutaminase cross-linking of sh gelatin for enhancing
gel strength has been studied quite extensively but other
enzymes have received less attention. Chen, Embreea,
Brown, Taylor, and Payne (2003) reported that mushroom
tyrosinase was able to catalyze gel formation for gelatine
chitosan blends. In contrast to transglutaminase,
tyrosinase-catalyzed reactions did not lead to gel formation
unless chitosan was present (i.e., chitosan is required for
tyrosinase-catalyzed gel formation). Tyrosinase-catalyzed
gelatinechitosan gels were observed to be considerably
weaker than transglutaminase-catalyzed gels. The ability
of other enzymes for modifying functional properties of
sh gelatin should be explored to enhance its value
comparable to mammalian gelatin.
Due to the large number of functional side groups, gel-
atin readily undergoes chemical cross-linking. Gel strength
of gelatin could therefore be improved through chemical
cross-linking, but this approach has not been explored as
much as enzymatic cross-linking. In chemical cross-linking
methods, cross-linkers are used to bond functional groups
of amino acids. Commonly used chemical cross-linkers in-
clude formaldehyde and glutaraldehyde, but these synthetic
cross-linking reagents are relatively highly cytotoxic and
not suitable for food applications. Thus, new food-compat-
ible cross-linking agents had to be identied. A search for
possible candidates led to polyphenols, which are widely
distributed as minor but functionally important constituents
of plant tissues. Polyphenols are known to react under ox-
idizing conditions with side chain amino groups of pep-
tides, leading to formation of cross-links in proteins
(Strauss & Gibson, 2004). Strauss and Gibson (2004) re-
ported that gelatin gels cross-linked with plant-derived phe-
nolic acids (caffeic, chlorogenic, ferulic) and avonoids
had greater mechanical strength, reduced swelling, and
fewer free amino groups. Dynamic light scattering analyses
showed that such cross-linking results in denser polymeric
networks and prevents extension of the peptide chains when
the pH is moved away from the isoelectric point.
It is interesting to further investigate the utilization of
natural plant-derived components for protein (gelatin)
cross-linking. The effect of phenolic acids on thermorever-
sibility of gelatin gel, for example, has not been investi-
gated. For lm-making purposes, the mechanical
properties of sh gelatin apparently can be improved by
chemical cross-linking. The role of ferulic acid and tannin
especially warrant further investigation. These natural
cross-linking agents, obtained from plant kingdom, have
been shown to have cross-linking effects on gelatin lm
(Cao, Fu, & He, 2007; Ou & Kwok, 2004; Ou, Wang,
Tang, Huang, & Jackson, 2005).
Another food-compatible chemical cross-linking agent
that has received attention recently is genipin. Covalent
cross-linking of gelatin can be achieved using genipin,
a naturally occurring cross-linker extracted from either
Gardenia jasmindides Ellis (Asia) or Genipa americana
(tropical America) fruit (Nickerson et al., 2006). Genipin
is an aglycone derivative from an iridoid glycoside called
geniposide, obtained via enzymatic hydrolysis with b-glu-
cosidase (Butler, NG, & Pudney, 2003). Genipin has been
approved for food use in Japan, Korea, Taiwan and south-
eastern Asia. Most studies with genipin to date have fo-
cused solely on porcine or bovine gelatin (Bigi, Cojazzi,
Panzavolta, Roveri, & Rubini, 2002; Nickerson et al.,
2006) and very few studies (Chiou et al., 2006) on sh
gelatin.
Protein cross-linking via Maillard reaction (so-called
Maillard cross-link) could also be exploited to enhance
the strength of sh gelatin gel. Maillard cross-link can be
dened as cross-links derived from the Maillard reaction
(Gerrard, 2002). The Maillard reaction is a complex cas-
cade of chemical reactions, initiated by the deceptively
simple condensation of an amine with a carbonyl group, of-
ten within a reducing sugar or fat breakdown product (Fayle
& Gerrard, 2002). It is known that the incubation of pro-
teins with sugars often results in a loss of solubility, and
it has been suggested that this is due to the polymerization
of protein molecules by covalent cross-links formed as a re-
sult of the Maillard reaction (Mitchell & Hill, 1995). Other
than reducing sugars, L-ascorbic acid has also been reported
to undergo a Maillard-type reaction. Ascorbic acid is com-
monly used in food products and is notable for its potential
to be involved in both Maillard reactions and free radical
cycles (Farahnaky, Gray, Mitchell, & Hill, 2003). Gerrard,
652 A.A. Karim, R. Bhat / Trends in Food Science & Technology 19 (2008) 644e656
Fayle, Sutton, and Pratt (1998) studied the reaction between
dehydroascorbic acid and proteins and reported that the
model protein, ribonuclease A, underwent covalent cross-
linking. The potential of these reactions for enhancement
of sh gelatin gel strength has yet to be explored.
Depending on the degree of modication required,
different cross-linking treatments can be used, including
enzymatic, chemical, and physical methods. Physical
cross-linking methods include exposure to gamma or ultra-
violet radiation. The primary advantage of physical
methods is that they do not cause potential harm. However,
the limitation of such methods is that obtaining the desired
amount of cross-linking is difcult.
Despite the limitations in some functional properties,
gelatin derived from sh seems to be a viable alternative
to mammalian gelatin. Although sh gelatin does not
form particularly strong gels, it is well-suited for certain in-
dustrial applications, such as micro-encapsulations, light-
sensitive coatings, and low set time glues. There is also
a market for non-gelling gelatin in the cosmetic industry
as an active ingredient (e.g., shampoo with protein)
(Wasswa et al., 2007). Using sh collagen and gelatin
may generate new applications as a food ingredient. For ex-
ample, unmodied cold water sh gelatins could possibly
be used in refrigerated products and in situations where
low gelling temperature is needed (Rustad, 2003). In order
to increase the value of sh gelatin, more specic applica-
tions for sh gelatin should be identied.
Extraction of gelatin from marine sources has mainly fo-
cused on a limited number of cold and warm water sh spe-
cies. Extraction of gelatin from other marine invertebrates
such as sponges, tunicates, and molluscs has not so far
been reported. These invertebrates are being studied for
new pharmacologically active constituents but they could
as well be a promising source of gelatin.
Collagen from sh has recently been identied as a po-
tential allergen. This could become a problem for the use of
sh gelatin in commercial products (Hamada, Nagashima,
& Shiomi, 2001; Sakaguchi et al., 1999). More research
is required to elucidate the nature of the allergenic reactions
and possible ways to circumvent the problem.
From the preceding discussion, manipulation of starch
molecular properties by amylomaltase enzymes from vari-
ous microbial sources seems to be a promising approach
to produce a thermally reversible starch gel as a potential
gelatin alternative. With proper control of reaction condi-
tions, the molecular weight of starch chains could be re-
duced to a level that is small enough to signicantly
decrease the viscosity of the paste, yet large enough to
form a rigid but thermally reversible gel through re-associ-
ation. However, certain issues need to be considered before
amylomaltase-modied starch can nd application as
a gelatin alternative. As pointed out by Hansen et al.
(2008), the textural prole of starch gels was very different
from gelatin. The elasticity of gelatin gels was much
higher, making them rmer than starch gels. In addition,
amylomaltase-modied starches formed opaque gels, while
gelatin gels were fully transparent. Therefore, a conclusion
from most studies is that amylomaltase-modied starches
could be used in certain food applications but it cannot
match the complete functional spectrum of gelatin. Several
combinations of enzymatic and/or chemical modication
may be needed. More extensive research needs to be carried
out to further elucidate the mechanism of the enzyme
action and to identify key factors of the reaction conditions
to enable proper control of the process. Chemometrics
approach may provide insight into some main structural
requirements towards generating gelatin-like textures
(Hansen et al., 2008). Detailed rheological and sensory
evaluation of the thermoreversible starch gels are also
needed to assess the suitability and acceptability of these
products as gelatin alternatives.
Genetic engineering has made great progress in the areas
of recombinant collagen and gelatin expression to produce
biomaterial for biomedical applications. This approach
could be extended to produce bovine collagen/gelatin.
Olsen et al. (2003) have described several recombinant sys-
tems that have been developed for bovine as well as sh
gelatin. Recombinant gelatin has been expressed in Pichia
pastoris and Hansenula polymorpha in both non-hydroxyl-
ated and hydroxylated forms. Pichia was shown to be
a highly productive system for gelatin production. How-
ever, the functional, rheological, and sensory properties of
the recombinant gelatin have not been reported. The au-
thors suggested that recombinant collagen and gelatin ex-
pression could be alternatives to bovine material that
offer an enhanced safety prole, greater reproducibility
and quality, and the ability of these materials to be tailored
to enhance product performance. The prospect of producing
microbial gelatin through genetic engineering akin to mi-
crobial polysaccharide via fermentation systems (e.g., xan-
than, gellan) is very exciting, and more extensive efforts
should be directed on this area. Plant-derived gelatin has
also been developed by scientists at Iowa State University
in Ames (Anonymous, 2007b). Their studies established
transgenic corn as a viable way to produce gelatin and po-
tentially other products. It is not impossible that the tech-
nique could someday be used to produce high-grade
designer gelatin in a safe and inexpensive manner
(Anonymous, 2007b).
Conclusions and future outlook
Gelatin, a multifunctional hydrocolloid, is used exten-
sively in food and non-food industries for a variety of appli-
cations. However, there is an ever-growing concern among
consumers regarding the origin of these gelatins mainly due
to religious sentiments and the risk of potential contamina-
tion with viruses and prions (such as the BSE prion) as it is
widely extracted from animal sources. Fish gelatin is
a promising alternative. Even though sh gelatin will not
be able to completely replace mammalian gelatin, it is en-
visaged that it might become a niche product offering
653 A.A. Karim, R. Bhat / Trends in Food Science & Technology 19 (2008) 644e656
unique and competitive properties to other biopolymers, as
well as meeting the demand of global halal/kosher market.
However, while sh gelatin seems to be a promising alter-
native, some problems persist, including inferior gelling
property and quality variations from batch to batch and
from species to species. Hence, to overcome this hindrance,
exploration is underway for a better alternative source of
gelatin, possibly from microbes or plants that could possi-
bly replace the animal source, possessing similar or even
superior physicochemical, functional and sensory attri-
butes. Some recent inventions have pointed towards the de-
velopment of thermally reversible gel from modied starch,
based on the application of carbohydrate-active enzymes.
Extensive studies are also being undertaken into possibili-
ties of using mixed gelling systems from plant-based source
such as pectin, agar, carrageenan, etc. Complex blends of
different hydrocolloids or hydrolyzed fractions are neces-
sary in order to obtain a dened property prole. Such ap-
proach, however, tend to be expensive both in manufacture
and in further processing, especially in comparison with
gelatin. Thus, using plant hydrocolloid blends as gelatin al-
ternatives frequently involves accepting sensory or techno-
logical disadvantages and higher prices, unless high
temperatures or extreme pH values have to be used
(Schrieber & Gareis, 2007). There are possibilities of ex-
ploring the genetic engineering approach to develop re-
combinant collagen and gelatin expression to produce
required outputs. It is clear that the development of an ef-
fective and cheap alternative source for mammalian-based
gelatin will denitely be a boon not only for consumers,
but also for the food industry.
Acknowledgments
We gratefully acknowledge and are indebted to our
anonymous referees for comments and constructive sugges-
tions for improving the manuscript.
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