Abstract
The subject of the study was analysis of enzymatic degradation of fish gelatin and fish gelatin-chitosan films cross-linked with transglutaminase (TGase) and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC). Unmodified gelatin films were almost completely hydrolysed by trypsin and proteinase N, and in about 60% by pepsin. Gelatin films modified with TGase in concentration of 0.2 mg/ml and with EDC (30 mM) were hydrolysed by trypsin in 90–100% while by pepsin in about 40 and 25%, respectively. Fish gelatin from gelatin-chitosan films, unmodified and modified with TGase, was almost completely hydrolysed by trypsin. The presence of chitosan in two-components films cross-linked with EDC decreased hydrolysis by pepsin and trypsin, respectively, by about 65, and 20% more in comparison to that of one-component chemical modified films. Applied modifications had no significant influence on degradation of fish gelatin and gelatin-chitosan films by proteinase N.
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