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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

Bovine skin was incubated with plant enzymes bromelain (B) and zingibain (Z) at the level of 0, 5, 10, 15, 20 and 25 unit/g of skin and gelatin was extracted at 60 °C for 6 h. Control gelatin was extracted without enzymatic pretreatment. The yield and gel strength were 17.90% and 283.35 g for the control samples and 22.26% and 160.88 g for B20 samples. The zingibain extracted gelatin (GEZ) samples failed to form gel. Viscosities of GEZ gelatins were significantly (P

The autolysis of pretreated bovine skin (PBS) (treated with 0.1 M NaOH and 1% HCl), its endogenous proteases, inhibitors and their effects on quality attributes of gelatin were examined. PBS was subjected to different temperatures (20–90 °C) and pH (2–9) and treated with different protease inhibitors. Maximum autolytic activity of PBS was observed at 40 °C and pH 5. Ethylene-bis (oxyethylenenitrilo) tetraacetic acid (EGTA) was the most effective in impeding the degradation of γ-, β- and α- chains of PBS protein indicating that metallocollagenases were the predominant endogenous proteases in bovine skin. Gelatin was extracted in the absence (GAE) and presence (GPE) of EGTA, and EGTA with papain enzyme (GPEP). GPEP had a higher yield and lower gel strength than GEA and GPE. Metallocollagenases partook in the degradation of gelatin thereby affecting its functional properties. Pretreating PBS with or without EGTA, and papain influenced the quality attributes of gelatin.