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Fish trypsin immobilized on ferromagnetic Dacron

Paper ID Volume ID Publish Year Pages File Format Full-Text
36099 45120 2006 4 PDF Available
Title
Fish trypsin immobilized on ferromagnetic Dacron
Abstract

Trypsin can be obtained from waste disposal of Nile tilapia (Oreochromis niloticus) intestine, the most important fish species in Brazilian aquaculture. This protease was covalently immobilized on ferromagnetic Dacron (polyethyleneterephthalate or PET). Dacron film was converted to Dacron-hydrazide powder and further magnetized. Then the enzyme was covalently bound to the magnetic particles. The protein amount and specific activity of the immobilized enzyme on 0.6 mM BAPNA (pH 8.0 at 25 °C) were 25.6 mg/g of particles and 18.5 ± 0.253 mU/mg protein (29 ± 1%) of that estimated for the soluble enzyme), respectively. The derivative showed an apparent Km (0.132 ± 0.044 mM) and optimum pH (7.0) lower than those found for the soluble enzyme (0.735 ± 0.141 mM and 8. 0). The enzyme was inhibited by benzamidine and TLCK (typical trypsin inhibitors) and metallic ions, especially aluminium and copper. This water insoluble enzyme was stable during about two months stored at 10 °C and can be reused.

Keywords
Protease; Trypsin; Ferromagnetic Dacron; Immobilization; Oreochromis niloticus; Tilapia
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Fish trypsin immobilized on ferromagnetic Dacron
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 41, Issue 5, May 2006, Pages 1213–1216
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
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