Beef Gelatin Protein Has Which Amino Acids

Polymers for a Sustainable Environment and Green Energy

T.R. Keenan , in Polymer Science: A Comprehensive Reference, 2012

10.13.7.1 Food Products

Gelatin formulations in the food industry use almost exclusively water or aqueous polyhydric alcohols as solvents for candy, marshmallow, or dessert preparations. In dairy products and frozen foods, gelatin's protective colloid property prevents crystallization of ice and sugar. Gelatin products having a wide range of Bloom and viscosity values are utilized in the manufacture of food products, specific properties being selected depending on the needs of the application. For example, a 250-Bloom gelatin may be utilized at concentrations ranging from 0.25% in frozen pies to 0.5% in ice cream; the use of gelatin in ice cream has greatly diminished. In sour cream and cottage cheese, gelatin inhibits water separation, that is, syneresis. Marshmallows contain as much as 1.5% gelatin to restrain the crystallization of sugar, thereby keeping the marshmallows soft and plastic; gelatin also increases viscosity and stabilizes the foam in the manufacturing process. Many lozenges, wafers, and candy coatings contain up to 1% gelatin. In these instances, gelatin decreases the dissolution rate. In meat products, such as canned hams, various luncheon meats, corned beef, chicken rolls, jellied beef, and other similar products, gelatin in 1–5% concentration helps to retain the natural juices and enhance texture and flavor. Use of gelatin to form soft, chewy candies, so-called gummy candies, has increased worldwide gelatin demand significantly. Gelatin has also found new uses as an emulsifier and extender in the production of reduced-fat margarine products. The largest use of edible gelatin in the United States, however, is in the preparation of gelatin desserts in 1.5–2.5% concentrations. For this use, gelatin is sold either premixed with sugar and flavorings or as unflavored gelatin packets. Most edible gelatin is type A, but type B is also used ( Figure 6 ).

Figure 6. Food applications of gelatin.

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Environmental Biotechnology and Safety

M.R. Kosseva , in Comprehensive Biotechnology (Second Edition), 2011

6.44.4.8.3 Production of gelatin

The amount of gelatin used in the worldwide food industry is increasing annually [170]. The estimated world usage of gelatin is 200   000   MT yr⁻¹ [24]. Generally, gelatin is commercially made from skins and skeletons of bovine and porcine by alkaline or acidic extraction. However, the occurrences of bovine spongiform encephalopathy and foot/mouth diseases have led to the major concern of human health. Thus, byproducts of mammalians are limited for production of collagen and gelatin as the functional food, cosmetic, and pharmaceutical products [51]. Studies on extraction and functional properties of gelatin from fish byproducts, such as skin and bone, have been reported. Gelatin was extracted from precooked tuna caudal fin with the yield of 1.99% [3]. Tuna fin gelatin (TFG) contained high protein content (89.54%) with hydroxyproline content of 14.12   mg g⁻¹. TFG comprised a lower content of high-molecular-weight cross-links and hydroxyproline content than porcine skin gelatin (PSG). However, proline content in TFG was twofold higher than that of PSG. The highest bloom strength and turbidity of TFG were observed at pH 6, while the lowest solubility was noticeable at the same pH. The bloom strength of TFG gel was lower than that of PSG gel at all pHs. TFG exhibited the lower emulsifying activity but greater emulsifying stability than PSG (P  <   0.05). TFG showed poor foaming properties than PSG. The tensile strength, elongation at break, and water vapor permeability of film from PSG were greater than those of TFG (P  <   0.05). The study revealed that gelatin of good quality can be prepared from tuna-processing discards.

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Polymers in Biology and Medicine

M. Guvendiren , ... J.A. Burdick , in Polymer Science: A Comprehensive Reference, 2012

9.22.3.3.2(i) Collagen and gelatin

Gelatin, or denatured collagen, is a natural ECM protein that provides tissue structure and is completely resorbable in vivo. ²¹⁶ Although gelatin forms physical cross-links naturally, these structures are not stable at physiological temperature. Therefore, it is necessary to stabilize gelatin-based materials with chemical cross-links. Van Den Bulcke et al. ²¹⁷ reacted gelatin with methacrylic anhydride to modify a gelatin backbone with methacrylamide groups for photopolymerization. Subsequent photopolymerization formed gelatin films with a high storage modulus, which could be controlled by the degree of substitution, polymer concentration, initiator concentration, and UV irradiation conditions. Alternatively, type I collagen has been modified with methacrylamide groups to photopolymerize collagen hydrogels in the presence of rat aortic smooth muscle cells. ²¹⁸ This system preserved both cell viability and the natural structure of collagen to produce constructs with enhanced mechanical properties. Gelatin has also been modified with styrene groups and photopolymerized for applications including drug delivery, ^219–221 cell carriers ²²² and wound healing. ^221,223 For example, Li et al. ²²³ developed a tissue-adhesive glue consisting of styrenated gelatin, PEG diacrylate, and carboxylated CQ in phosphate-buffered saline that was photocurable on an incised artery in less than 1   min. The gel tightly adhered to the injury site, allowed hemostasis to occur, and degraded within 4 weeks.

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Analogue Materials in Experimental Tectonics

Erika Di Giuseppe , in Reference Module in Earth Systems and Environmental Sciences, 2018

Rheological properties

Gelatins and polysaccharide biopolymers exhibit a complex rheology ranging from purely elastic to visco-elasto-brittle to purely viscous when gel–sol transition occurs ( Di Giuseppe et al., 2009). Rheological, mechanical and physical properties are strongly dependent on a wide range of parameters, such as temperature, composition, concentration, aging and applied strain rate (e.g., Bot et al., 1996; Di Giuseppe et al., 2009; Kavanagh et al., 2013; Ross-Murphy, 1994), as well as pH and ionic strength (e.g., Djabourov et al., 2013). The presence of electrolytes may impact on swelling, solubility, gelation and water binding capacity; moreover, the additive may act as stabilizer or not, depending on its nature and concentration (see Brizzi et al., 2016 and the references herein).

An extensive study of the properties of four biopolymers, such as pig skin, gellan gum, κ-carragenan and xanthan gum, as function of applied strain, composition, c, T, etc., was conducted in order to find the material that, properly scaled to nature, can be employed as crust analogue (Di Giuseppe et al., 2009). The composition of the macromolecules forming the gel network strongly affects gel's firmness: xanthan gum forms the weakest gel, while firmer network were formed by κ-carragenan, gellan gum and pig skin, listed from the stiffest to the weakest gel. The value of the linear viscoelastic range, marked by γ _VE , decreased with increasing firmness. Generally, gel temperature, T _g , and G′ and G′′ moduli increase as gel concentration increases. G′ and G′′ values change abruptly when T approaches T _g (Fig. 4A ). Compared to the other gels, xanthan gum exhibits a peculiar behavior being very stable under a wide range of T and the weakest gelatin but with relatively high η. It was found that pig skin samples with c  =   2.5 wt.% at 10°C was suitable as crust analogue, properly scaling elastic (G ^∗  =   10³  Pa), viscous (n  =   5.0, E _a   =   450   −   500   kJ/mol) and yield properties (10³  −   10⁴) of the natural prototype. On the contrary, pure gelatin-water solutions cannot be used as analogue of mantle because of their low viscosity values, that result in too high Reynolds numbers (Eq. 14) (Di Giuseppe et al., 2009).

Fig. 4. Temperature sweep test applied to (A) cooling Gellan Gum 1.5   wt.% sample (γ  =   1%, ω  =   10 rad/s); and (B) PEG wax P3515 (τ  =   1   Pa, ω  =   1   Hz). Black symbols mark the heating thermal path, gray ones the cooling path (ΔT  =   0.5^°C/min). For both samples the fluid/solid transition is very sharp.

(A) Modified after Di Giuseppe, E., Funiciello, F., Corbi, F., Ranalli, G., Mojoli, G. (2009). Gelatins as rock analogs: A systematic study of their rheological and physical properties. Tectonophysics 473, 391–403. (B) Modified after Garel, F., Kaminski, E., Tait, S., Limare, A. (2014). An analogue study of the influence of solidification on the advance and surface thermal signature of lava flows. Earth and Planetary Science Letters 396, 46–55.

Agar-agar gels, that are polysaccharides extracted from red algae, exhibit rheological properties similar to those of carrageenan gels (Nishinari and Watanase, 1983). Oscillation measurements indicated that agar-agar is a highly crosslinked biopolymer even at low c (0.5%–1.5%) (Schwarzlos et al., 1997), whose rheology is strongly dependent on its origin and on the pretreatment at which is subjected during the extraction (Nishinari and Watanase, 1983). The alkali treatment may act as a structure stabilizer (resulting in a G′ increase) or can cause chain breakage (decrease of G′) depending on the agar origin. Moreover, agar is a 'sugar reactive' polymer, that is, the presence of sugar increases the strength of the gel.

A certain amount of time is needed for pure gelatin to stabilize and reach a plateau value (Di Giuseppe et al., 2009; Kavanagh et al., 2013). A series of experiments has been carried out to analyze how the elastic properties evolve with time, by varying the gel concentration and the volume used (Kavanagh et al., 2013). A fracture can take place and propagate when the strength of the host rock, characterized by the fracture toughness, K _c , is exceeded (e.g., Rivalta et al., 2005; Kavanagh et al., 2006). Measurements of gelatin fracture toughness showed that K _c follows the same relationship as ideal elastic-brittle solids, $K_c=\sqrt{2{\gamma }_{s}E}$ (Griffith, 1921), where E is Young's modulus of the host medium and γ _s the a surface energy. γ _s has been estimated experimentally as 1.0   ±   0.2   J/m² (Kavanagh et al., 2013). The Young's modulus has been found to evolve exponentially with time, E  = E _∞(1   − e ^{t/t _tr} ), up to a constant plateau value, E _∞. For low concentrations (2   ≤ c  <   5   wt. %) E _∞ is linearly correlated to c.

Brizzi et al. (2016) investigated how the rheological and physical properties of pig skin gelatin changes when salt, that is, NaCl, is added. The concentration of the gelatin was kept constant, while salt's concentration was increased from 0   wt.% up to 20   wt.%. A weakening of the gelatin structure was observed with the presence of the NaCl as both viscosity and material rigidity decrease. As c _NaCl increased, G′ and G′′ plateau values decreased at different rates showing: G′′ reduction occurred at a lower rate than G′ and at c _NaC1  =   20 wt.% the difference between G′ and G′′ was reduced to 1 order of magnitude. In addition, the duration of the phase during which the gelatin stabilizes and reaches a plateau value, is strongly affected by the salt, showing longer interval of time.

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Foods, Materials, Technologies and Risks

M.M. Chaudry , M.N. Riaz , in Encyclopedia of Food Safety, 2014

Gelatin

Important in many food products, gelatin is probably the most controversial of all modern halal ingredients. Gelatin can be derived from pig skin, cattle bones, and cattle hides. In recent years, some gelatins from fish skins have also entered the market. Fish gelatins can be produced halal with proper supervision, and acceptable to almost all of the mainstream religious supervision organizations. Most currently available gelatins – even if called kosher – are not acceptable to the mainstream US kosher supervision organizations and Islamic scholars. Many are, in fact, totally unacceptable to halal consumers because they may be pork-based gelatin. All major manufacturers and some smaller ones are currently producing certified halal gelatin from cattle bones and hides of animals that have been slaughtered by Muslims.

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Foods, Materials, Technologies and Risks

J.M. Regenstein , CE Regenstein , in Encyclopedia of Food Safety, 2014

Gelatin

Important in many food products, gelatin is probably the most controversial of all modern kosher and halal ingredients. Gelatin can be derived from pork skin, beef bones, or beef skin. In recent years, some gelatins from fish skins have also entered the market.

Most currently available gelatins – even if called 'kosher' – are not acceptable to the mainstream US kosher supervision organizations as they may be from pork or from nonreligiously slaughtered cattle.

A recent development has been the manufacture of kosher gelatin from the hides of kosher slaughtered cattle.

One finds a wide range of attitudes towards gelatin among the lenient kosher supervision agencies. The most liberal view holds that gelatin, being made from bones and skin, is not being made from a food (flesh). Further, the process used to make the product goes through a stage where the product is so 'unfit' that it is not edible by man or dog, and as such becomes a new entity. Rabbis holding this view may accept pork gelatin. Most water gelatin desserts and yogurts with a generic 'K' follow this ruling.

Other rabbis only permit gelatin from beef bones and hides, and not pork. Still other rabbis only accept 'India dry bones' as a source of beef gelatin. These bones, found naturally in India from the animals that fell and die in the fields, because of the Hindu custom of not killing the cows, are aged for over a year and are 'dry as wood.' Again, none of these products is accepted by the 'mainstream' kosher or halal supervisions, and are therefore not accepted by a significant part of the kosher and halal community.

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Biopolymers

Christopher Brigham , in Green Chemistry, 2018

3.22.2.1 Collagen and Gelatin

The structural proteins collagen and gelatin constitute >30% of the total proteins of most animals. These two polymers are used in a variety of applications, many of which are medical due mainly to their biodegradability and biocompatibility. ⁴

A collagen molecule consists of a trimer of α-chains, each of which has a molecular mass of approximately 100,000. The average amino acid molecular weight in collagen is low, compared with most proteins, because of the high content of the amino acid glycine. ^4,5 Depending on the origin of collagen, the individual subunits of the collagen trimer can make up a homotrimer of identical chains or a heterotrimer of different chains. ⁴ Collagen fibers tend to have high tensile strength and stability, aspects that make the molecule useful in many applications. Individual α-chains of collagen can form left-handed helical structures by themselves, and three of these chains will then intertwine to form a right-handed "superhelix." ⁴ The helical regions of the collagen α-chains possess a "Gly-X-Y" repeating triplet motif, where a glycine residue is flanked by two amino acids "X" and "Y," which are predominantly proline and hydroxyproline, respectively (Fig. 3.22.2). The presence of the glycine at every third residue in the collagen α-chain is necessary for the helical structure. As is evident, the architecture of collagen is due to its primary amino acid sequence.

Figure 3.22.2. A schematic representation of the Gly-Pro-Hyp motif found in collagen α-chains.

In the body, collagen forms elastic molecular networks that can strengthen tendons, as well as sheets that support skin and internal organs. ⁶ Studies in rats and clinical trials in humans have demonstrated that type II collagen, commonly isolated from chicken combs, reduces cartilage destruction in patients suffering from osteoarthritis. ^7–9 As collagen is a very strong molecule, it is often used in bone grafts. ¹⁰ Collagen has also been widely used in the cosmetic surgery and as tissue engineering scaffold material. ¹¹ For nonmedical uses, collagen is also used as sausage casings. When collagen is denatured by heating, the three strands separate (either partially or completely) into globular domains and random coils, thus becoming gelatin.

Gelatin is a mixture of peptides derived from collagen by breakage of cross-linkages and some peptide bonds. Typically, this breakage of bonds to convert collagen to gelatin is performed by enzymatic degradation. ⁴ Any protease could be used to convert collagen to gelatin peptides, such as pepsin, trypsin, papain, and other enzymes. Hydrolysis to peptides is performed to improve the functional as well as nutritional properties of the protein molecules. Several fish-based gelatin peptides have been shown to possess antioxidant properties. ⁴ The molecular weight of gelatin is significantly lower than that of collagen, typically in the range of 1400–26,000. ⁴ Just as glycine, proline and hydroxyproline are predominant amino acid residues in collagen, these three amino acids are often found in gelatin peptides.

There are many uses for gelatin peptides. When one thinks of gelatin, the typical applications associated are food related. Indeed, gelatin is a constituent of "gummy" candy products, and is also used as a thickening agent in foods like ice cream, yogurt, and marshmallow (synthetic). ¹² However, in the pharmaceutical industry, gelatin has been used for decades as coatings for pills and capsules to aid in swallowing. Also, ballistic gelatin is used as a medium for testing guns and ammunition, due to its similar consistency to muscle tissue. Gelatin can also be used as a binder in a variety of applications, including match and sandpaper making. ¹³

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Mechanisms of Magma Transport in the Upper Crust—Dyking

Janine L. Kavanagh , in Volcanic and Igneous Plumbing Systems, 2018

3.3.3 Dyke Geometry in Laboratory Models

The first analogue experiments to study dyke propagation used gelatine solids injected by dyed water to create hydraulic fractures. Fiske and Jackson (1972) created free-standing gelatine blocks moulded into the shape of elongated volcanic rift zones, and injected these with water to study the controls on dyke emplacement in Hawaii. The similarity of their laterally propagating, blade-like experimental dykes compared to the observations of dykes in the field was compelling, and the ability of the laboratory experiments to explain the overall growth of volcanic rifts (see Chapter 4) using physics affirmed the potential of laboratory experiments to model dykes. Gelatine's evident versatility as a transparent elastic medium also paved the way for its use as a crustal analogue material to model dyke propagation in the laboratory ever since.

3.3.3.1 Newtonian Fluids

Takada (1990) used gelatine slabs supported in an experimental tank to study dyke propagation by injecting it with fluids of various density, viscosity and volume. His experiments showed that a buoyant fluid-filled fracture (dyke) propagating in a homogeneous, isotropic, elastic solid with an initially hydrostatic stress field is broadly controlled by the density difference between the injected fluid and the host solid (Fig. 3.6A). The dyke shape changed as it grew due to increased buoyancy; transitioning from penny-shaped in front view (y–z-plane) and elliptical in side view (x–z-plane), to a flat teardrop shape in front view (y–z-plane) and narrow teardrop shape in side view (x–z-plane). This type of behaviour can be attributed to a Peach–Koehler force that acts on dislocations, which Weertman (1971) noted as a 'pseudo-Archimedean force' acting on a fluid-filled crack. The teardrop shape has a distinctive head region where buoyancy forces are important (Fig. 3.6B and C), and its length L _h or h _b depends on the density difference between the injected fluid and host (Taisne and Tait, 2011). Experiments where air and water were injected simultaneously demonstrated how the air collected in the dyke tip; its buoyancy exerted control on the dyke ascent dynamics and geometry, causing an elongated, buoyant head to form (Menand and Tait, 2001).

Figure 3.6. Laboratory experiments of dyke ascent modelled as a hydrofracture using gelatine as a crust analogue.

(A) Series of photographs showing injection of buoyant silicon oil into a gelatine solid, viewed in front (y–z-plane) and side view (x–z-plane). The numbers on the photos are the injected volumes in ml (Takada, 1990). (B) Photograph using polarised light showing injection of fixed volume of buoyant heptane into a gelatine solid viewed from the side (x–z-plane). The length of the buoyant dyke head (l _h) is indicated, and interference colours focused at the dyke tip relate to stress concentration in the gelatine (Taisne and Tait, 2011). (C) Photograph (I) and annotated sketch (II) of an air and dilute hydroxyethylcellulose liquid-filled crack propagating in a gelatine solid viewed from the side and front, respectively. Air collects at the dyke tip and, once its buoyancy pressure overcomes the fracture resistance of the gelatine, it controls the crack tip growth (Menand and Tait, 2001).

Mathieu et al. (2008) carried out experiments using sand or fine-grained ignimbrite powder (the crust analogue) and injected honey and golden syrup (the magma analogue). By injecting along the wall of their square-based experimental tank (in the so-called 'half-box' experiments), they directly observed the growth of their intrusions as they propagated through the host material, which was otherwise obscured when injecting into the centre of the experimental tank (in the so-called 'full-box' experiments). Their experimental dykes grew with an irregular but sharp margin, with occasional branching and en echelon segmentation during ascent. Abdelmalak et al. (2012) carried out similar experiments but used a form of Hele-Shaw cell (two-dimensional experimental tank) and compacted silica flour as their crust analogue (Fig. 3.7A). The golden syrup injections were described as 'viscous indenters' with a rounded tip when deforming their host by shear failure. Thinner dyke tips and higher cohesion materials produced dykes that caused the host material to fail in tension.

Figure 3.7. Dyke emplacement modelled as a viscous indenter in laboratory experiments using compacted silica flour as a crust analogue material.

(A) Sketch of 2D experiment apparatus where a thin, vertical experimental tank is intruded by golden syrup (Abdelmalak et al., 2012). The growth of the dyke is observed, and photographs show the final stages of emplacement as the dyke fractures and uplifts its host, either propagating to the surface directly (A1) or intruding a surface fracture (A2). (B) Sketch of 3D experimental apparatus where oil is injected into a square-based tank filled with compacted silica flour (Galland et al., 2014). Surface deformation occurs during injection, and post-emplacement solidification enables the dyke to be excavated and its final morphology observed (B1).

3.3.3.2 Solidification Effects

Experiments where a solidifying fluid is intruded into the crust analogue produce different morphologies to water or air injection, but share similarities independent of the host material. Hot, liquid vegetable oil (often Vegetaline) injected into gelatine has produced morphologies that are thicker than their water counterparts (e.g. Taisne and Tait, 2011; Daniels and Menand, 2015). This can be explained by potential melting of the host gelatine during intrusion, or by heating and softening of the surroundings as the intrusions form. These experimental dykes grow by progressive breakout of fluid from the chilled propagation front and often form an irregular en echelon tip that is thought to reflect shear stress. Laboratory models studying dykes as viscous indenters have intruded Vegetaline into compacted, crystalline and cohesive silica flour (e.g. Galland et al., 2014). Excavation of the intrusion after the oil has solidified reveals an experimental dyke morphology that is broadly elliptical, with an irregular surface morphology and en echelon tips (Fig. 3.7B).

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Bio-based aerogels and their environment applications: an overview

Fohad Mabood Husain , ... Hurija Dzudzevic Cancar , in Advances in Aerogel Composites for Environmental Remediation, 2021

2.1.8 Gelatin

Freeze-drying process was used to fabricate gelatin aerogels from mixture of gelatin gel and formaldehyde (cGel). Further, methyltrichlorosilane (MTCS) was subjected to thermal chemical vapor deposition to synthesize MTCS-cGel aerogel (hydrophobic adsorbent material). This MTCS-cGel aerogel demonstrated low density, high porosity, and unique 3D networks [32]. Multi-component bio-based aerogels were synthesized by the formation of interpenetrating polymer network (IPN). Interpenetration of alginate and gelatin was successfully accomplished and maintained by super-critical drying using different combination of alginate and gelatin [33]. Gelatin-silica hybrid aerogels of high porosity and low-density possessing adsorption capabilities were prepared. In the first step, gel formation with stable 3D network was achieved using sol-gel method. Then, the prepared gel was soaked in hexamethyldisilazane solution and freeze dried to obtain aerogel. These aerogels were coated with hexamethyldisilazane [34]. Facile synthesis of eco-friendly gelatin-based hybrid aerogels has been reported. Aqueous solution of gelatin powder was prepared and titanium dioxide solution was added to it and left for stirring at 60°C for 6 h, resulting solution was refrigerated for gelation. After 2 h, gelatin hydrogels were soaked in ammonium sulfate solution for 24 h. Then, these hydrogels were immersed in poly(ethyleneimine) polymer (PEI) solution for a day. These gelatin hydrogels were precooled at −20°C and then freeze dried to obtain GTP composite aerogels possessing hierarchical porosity and superamphiphilic surface [35]. In a very recent research, mesoporous silica-gelatin containing 4–24 wt% gelatin was prepared by super-critical drying. These synthesized hybrid aerogels demonstrated high selectivity for adsorption of mercury [36].

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Immobilized Cells

E. de Alteriis , ... P. Parascandola , in Progress in Biotechnology, 1996

Immobilization of cells and digestion of the immobilizate

Yeast cells were immobilized by entrapment within oxystarch-hardened gelatin discs (1). The following standard procedure was carried out to obtain 50   cm³ of gel: five g of gelatin were dissolved in 29   ml of dist. water by heating for 20   min in a boiling water bath. After this solution was cooled down to 40   °C, 16   ml of an 11% (w/v) oxystarch aqueous solution and 5   ml of a yeast suspension (28   mg cells, d.w. cm^{-   3}) were added. The mixture was poured into a cylindrical mould (0.8   cm diameter) and kept at room temperature for 12   h. The resulting stiff gel was cut into 0.4   cm-thick discs.

Discs sampled at 48   h of incubation were dissolved by digesting the gelatin network with trypsin and the released cells were used for all the following experiments (5).

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