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Immobilization–stabilization of glucoamylase: Chemical modification of the enzyme surface followed by covalent attachment on highly activated glyoxyl-agarose supports

Paper ID Volume ID Publish Year Pages File Format Full-Text
35407 45088 2011 4 PDF Available
Title
Immobilization–stabilization of glucoamylase: Chemical modification of the enzyme surface followed by covalent attachment on highly activated glyoxyl-agarose supports
Abstract

Commercial glucoamylase immobilizes very slowly on highly activated glyoxyl-agarose supports. The resulting derivatives were only 6-fold more stable than soluble enzyme. The unmodified glucoamylase, highly glycosylated, seems to have a low number of Lys able to react with glyoxyl groups on the support. Thus, the enzyme surface was highly enriched in amino groups by chemical modification of carboxyl groups (activated with carbodiimide) with ethylenediamine. The aminated enzyme preserves a good percentage of activity (80%) and it exhibits the same stability than unmodified enzyme. The aminated enzyme was immobilized very rapidly on highly activated glyoxyl-agarose support. The new resulting derivatives preserved 50% of activity and were more than 500-fold more stable than soluble enzyme in experiments of thermal inactivation.

Keywords
Amyloglucosidase, Rigidification of glycosilated enzymes, Thermal stabilization
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Immobilization–stabilization of glucoamylase: Chemical modification of the enzyme surface followed by covalent attachment on highly activated glyoxyl-agarose supports
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 46, Issue 1, January 2011, Pages 409–412
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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Any Questions? feel free to contact us