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Stability of calcium autolyzed calpain ii from tilapia muscle tilapia nilotica x tilapia aurea


Stability of calcium autolyzed calpain ii from tilapia muscle tilapia nilotica x tilapia aurea



Journal of Agricultural and Food Chemistry 40(4): 535-539



ISSN/ISBN: 0021-8561

DOI: 10.1021/jf00016a001

The inactivation of calpain II (EC 3.4.22.17) from tilapia muscle (Tilapia nilotica .times. Tilapia aurea) was investigated. The thermal stability was enhanced by decreasing the water activity with the addition of sucrose at temperatures below 67.8.degree. C (isokinetic temperature). Addition of 30% sucrose caused the increase of the transition temperature from 61.9 to 63.8.degree. C and of the activation energy from 70.0 to 104.6 kcal/mol. The optimal pH for the stability was 7.5. This proteinase was less stable at alkaline pH than at acidic pH. The molecular weight of this proteinase was substantially autolyzed from 80,000 to 61,000 and 65,000 in the presence of calcium; the activation energy was calculated to be 26.61 kcal/mol by second-order rate constant.

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Accession: 007815297

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Related references

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