Abstract
ABSTRACT Two plant enzymes, namely actinidin (A) and papain (P), were used to pretreat bovine skin at the respective optimum pH and temperature of the enzymes for 48 h at the level of 0, 5, 10, 15, 20, and 25 unit/g of skin, and gelatin extraction was done at 60°C for 6 h. Gelatin yield from actinidin at level 20 (A20) (22.67%) and papain at level 20 (P20) (23.59%) were significantly (P < 0.05) higher than control (17.90%). The gel strength values for gelatin extracted using actinidin enzyme (GEA) were significantly (P < 0.05) higher than the control (283.35 g), and the gel strength for A20 was 366.39 g. However, gelatin extracted using papain enzyme (GEP) showed relatively lower gel strength. The GEA sample viscosities were significantly (P < 0.05) higher than control (12.10 mPa.s). GEA samples revealed overall degradation of β chains and presence of α chains and lower molecular weight peptides, whereas β and α chains were completely absent and lower molecular weight peptides were seen in all the GEP samples. Fourier-transform infrared (FTIR) spectra indicated a greater loss of molecular order and more disruption in the α helical structure of P20 compared to A20 and control gelatins. Scanning electron microscopy (SEM) revealed interconnected bigger particle size and denser structure with least number of voids in A20 than P20 and control gelatin samples. Thus, it was concluded that actinidin, particularly at level 20 unit/g of skin, could be used to improve the yield and properties of gelatin from bovine skin.
Highlights
Gelatin being derived from collagen by its limited denaturation possesses high-molecular-weight biopolymer.[1]
N,N,N,N-tetramethyl ethylenediamine (TEMED), sodium dodecyl sulfate (SDS), acrylamide, 2-mercaptoethanol, and coomassie brilliant blue R-250 were acquired from Merck (Darmstadt, Germany)
The stabilizing hydrogen bonds of collagen are destroyed by heating at a higher temperature resulting in the conversion of native helix to coil structure, which leads to the transformation of collagen to gelatin.[31]
Summary
Gelatin being derived from collagen by its limited denaturation possesses high-molecular-weight biopolymer.[1]. A pretreatment process using either acid or alkali is required to convert insoluble collagen into soluble form This results in insoluble swollen collagen with lost native collagen structure.[7] During the gelatin extraction process, heat destroys the hydrogen and covalent bonds, thereby changing the triple-helical structure of collagen chains to random coil structure (helix-to-coil transition) resulting in gelatin production.[8] Noncovalent and covalent bonds are broken down to enable to release free oligomers as well as α chains.[5] In addition to it, some amide bonds are cleaved in the native collagen structure during hydrolysis.[9] the resultant gelatin contains a combination of lower molecular weight polypeptides, showing a molecular weight between 16 and 150 kDa. Crosslink bonds found in collagen triple-helical structure are resistant to heat and acid,[,11] and normally a low gelatin yield is obtained.[12] Earlier, few protease enzymes known to cleave crosslinked bonds of collagen were used to enhance the yield of gelatin.[12] Proctase extracted from
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