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Enzymatic activities of proteases immobilized on tri(4-formyl phenoxy) cyanurate

Paper ID Volume ID Publish Year Pages File Format Full-Text
18547 42725 2006 5 PDF Available
Title
Enzymatic activities of proteases immobilized on tri(4-formyl phenoxy) cyanurate
Abstract

The proteases viz. α-chymotrypsin, trypsin and papain were immobilized on tri(4-formyl phenoxy) cyanurate to form Schiffs base. The native and immobilized proteases were used for catalyzing the hydrolysis of proteins in an aqueous medium. Immobilized α-chymotrypsin exhibited shift in optimal pH from 8.5 to 9.0, while both trypsin and papain exhibits shift in optimal pH from 8.0 to 8.5. The shift in optimal temperature from 40 to 50 °C was recorded for α-chymotrypsin and trypsin, while papain shifted the optimal temperature from 50 to 60 °C. The immobilized protease revealed 15–20% increased in thermal stability and retained 70–80% of its initial activity after 8 cycles. The optimum in vitro proteolytic activity on animal intestine was recorded for papain in comparison with trypsin and α-chymotrypsin. These results support the diet-related plasticity of proteases.

Keywords
Proteases; Multi point binding; Immobilization; Animal intestines
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Enzymatic activities of proteases immobilized on tri(4-formyl phenoxy) cyanurate
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 4, 2 August 2006, Pages 958–962
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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