Abstract
The inactivation of calpain II (EC 3.4.22.17) from tilapia muscle was investigated. The thermal stability was enhanced by decreasing the water activity with the addition of sucrose at temperatures below 67.8 o C (isokinetic temperature). Addition of 30% sucrose caused the increase of the transition temperature and of the activation energy. The optimal pH for the stability was 7.5. This proteinase was less stable at alkaline pH than at acidic pH
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