alexa Digestive enzyme patterns and evaluation of protease classes in Catla catla (family: Cyprinidae) during early developmental stages.
Agri and Aquaculture

Agri and Aquaculture

Journal of Aquaculture Research & Development

Author(s): Rathore RM, Kumar S, Chakrabarti R

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Abstract Digestive enzymes of Catla catla were studied during ontogenic development. Specific amylase activity was 0.12+/-0.01 mg maltose mg protein(-1) h(-1) in fish 4 days after hatching (DAH) and reached a maximum on (0.41+/-0.12 mg maltose mg protein(-1) h(-1)) 34 DAH. Total protease activity was minimum (123.2+/-16.5 mU mg protein(-1) min(-1)) on day-8 and reached its highest level (2713+/-147.2 mU mg protein(-1) min(-1)) on day-32. Trypsin activity showed constant increasing trend from day-16 onwards and was maximum on day-34 (118.1+/-7.09 mU mg protein(-1) min(-1)). Highest chymotrypsin activity was found on day-32 (1789.0+/-111.7 mU mg protein(-1) min(-1)). Lipase activity was detected in 4 DAH catla. Lipase activity increased steadily from day-22 onwards. SDS-PAGE of crude enzyme extracts showed that high molecular mass bands (41.8-127.8 kDa) appeared during the early stages followed by low molecular mass bands (17.8-37.2 kDa). The number of protease activity bands in substrate SDS-PAGE increased with age of fish. During ontogenesis of carp, soybean trypsin inhibitor (SBTI), PMSF and TLCK inhibited 75.5+/-1.19\% to 92.8+/-0.85\%, 53.3+/-9.47\% to 90.5+/-2.6\% and 39.8+/-3.8\% to 84.7+/-1.54\% of total protease activity, respectively. There was only 2.58+/-0.66\% to 10.21+/-0.09\% inhibition of protease activity with EDTA. SBTI and PMSF inhibited 8 and 4 activity bands, respectively. TLCK, a specific trypsin inhibitor, inhibited four trypsin-like enzymes in carp during ontogenesis. This article was published in Comp Biochem Physiol B Biochem Mol Biol and referenced in Journal of Aquaculture Research & Development

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