Journal
FOOD CHEMISTRY
Volume 173, Issue -, Pages 147-155Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2014.09.160
Keywords
Crustacean proteases; Chymotrypsin; Substrate specificity; Sensitivity to inhibitors; Collagenolytic activity; Shrimp
Funding
- Consejo Nacional de Ciencias y Tecnologia (CONACYT) [80935]
- CONACYT
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Chymotrypsin from shrimp, Penaeus californiensis, was compared to Bos taurus chymotrypsin, and its structure function relationship was studied. Catalytic efficiency toward synthetic substrate is lower, but it has a broad specificity and higher activity toward protein substrates, including collagen. It is active at pH 4-10 and fully active up to 50 degrees C for 2 h and at least nine days at room temperature. The activation peptide is twice as long as bovine chymotrypsinogen, has less disulfide bridges, and is a single polypeptide. Only one activation step is necessary from chymotrypsinogen to the mature enzyme. Postmortem implications in muscle softening and melanisation, resistance to temperature and pH and efficiency with proteinaceous substrates make chymotrypsin useful as a biotechnological tool in food processing. This makes shrimp processing wastes useful as a material for production of fine reagents. (C) 2014 Elsevier Ltd. All rights reserved.
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