Autolysis of bovine skin, its endogenous proteases, protease inhibitors and their effects on quality characteristics of extracted gelatin.

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-, ß- 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.

Effects of Ultrasound Assisted Extraction in Conjugation with Aid of Actinidin on the Molecular and Physicochemical Properties of Bovine Hide Gelatin.

Actinidin was used to pretreat the bovine hide and ultrasonic wave (53 kHz and 500 W) was used for the time durations of 2, 4 and 6 h at 60 °C to extract gelatin samples (UA2, UA4 and UA6, respectively). Control (UAC) gelatin was extracted using ultrasound for 6 h at 60 °C without enzyme pretreatment. There was significant (p < 0.05) increase in gelatin yield as the time duration of ultrasound treatment increased with UA6 giving the highest yield of 19.65%. Gel strength and viscosity of UAC and UA6 extracted gelatin samples were 627.53 and 502.16 g and 16.33 and 15.60 mPa.s, respectively. Longer duration of ultrasound treatment increased amino acids content of the extracted gelatin and UAC exhibited the highest content of amino acids. Progressive degradation of polypeptide chains was observed in the protein pattern of the extracted gelatin as the time duration of ultrasound extraction increased. Fourier transform infrared (FTIR) spectroscopy depicted loss of molecular order and degradation in UA6. Scanning electron microscopy (SEM) revealed protein aggregation and network formation in the gelatin samples with increasing time of ultrasound treatment. The study indicated that ultrasound assisted gelatin extraction using actinidin exhibited high yield with good quality gelatin.