NDLI: Trypsin from the viscera of Bogue (Boops boops): isolation and characterisation

Content Provider	Springer Nature Link
Author	Barkia, Ahmed Bougatef, Ali Nasri, Rim Fetoui, Emna Balti, Rafik Nasri, Moncef
Copyright Year	2009
Abstract	Trypsin from the viscera of Bogue (Boops boops) was purified to homogeneity by precipitation with ammonium sulphate, Sephadex G-100 gel filtration and Mono Q-Sepharose anion exchange chromatography, with an 8.5-fold increase in specific activity and 36% recovery. The molecular weight of the purified enzyme was estimated to be 23 kDa by SDS–PAGE and size exclusion chromatography. The purified trypsin appeared as a single band on native-PAGE and zymography staining. The purified enzyme showed esterase-specific activity on N-α-benzoyl-l-arginine ethyl ester (BAEE) and amidase activity on N-α-benzoyl-dl-arginine-p-nitroanilide (BAPNA). The optimum pH and temperature for the enzyme activity, after 10 min incubation, were pH 9.0 and 55°C, respectively, using BAPNA as a substrate. The trypsin kinetic constants K m and k cat on BAPNA were 0.13 mM and 1.56 s−1, respectively, while the catalytic efficiency k cat /K m was 12 s−1 mM−1. Biochemical characterisation of B. boops trypsin showed that this enzyme can be used as a possible biotechnological tool in the fish processing and food industries.
Starting Page	893
Ending Page	902
Page Count	10
File Format	PDF
ISSN	09201742
Journal	Fish Physiology and Biochemistry
Volume Number	36
Issue Number	4
e-ISSN	15735168
Language	English
Publisher	Springer Netherlands
Publisher Date	2009-11-08
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biochemical characterisation Protease Purification Bogue Boops boops Trypsin Viscera Zoology Animal Biochemistry Animal Anatomy / Morphology / Histology Animal Physiology Freshwater & Marine Ecology
Content Type	Text
Resource Type	Article
Subject	Physiology Medicine Biochemistry Aquatic Science

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