Journal
FOOD CHEMISTRY
Volume 124, Issue 1, Pages 29-35Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2010.05.098
Keywords
Collagenolytic activity; Hepatopancreas; Fresh water prawn; Trypsin; Collagenase
Funding
- Office of the Higher Education Commission, Ministry of Education, Thailand
- CHE Ph.D. Scholarship
- National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), Thailand
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Proteolytic activity of crude protease extract (CPE) from the hepatopancreas of fresh water prawn (Macrobrachium rosenbergii) was studied. Optimal activity of CPE was found at pH 7 and 60 degrees C when casein was used as a substrate. The activity was strongly inhibited by 10 mM N-p-tosyl-L-lysine chloromethylketone (TLCK), suggesting that trypsin-like protease was dominant. CPE also showed the collagenolytic activity toward pepsin soluble collagen extracted from prawn muscle. During extended iced storage of 4 days, proteolytic and trypsin activities were found in the first segment of prawn abdomen. These activities were detected in the second segment after 4 days of storage. Heat soluble collagen content was continuously increased during the storage. Nevertheless, no changes in proteolytic activity and heat soluble collagen content were obtained in the abdomen of prawn with the removal of hepatopancreas. Therefore, the release of trypsin-like collagenase from hepatopancreas was most likely responsible for the softening of prawn meat during iced storage. (C) 2010 Elsevier Ltd. All rights reserved.
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