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Covalent bonding of protease to different sized enteric polymers and their potential use in wool processing

Paper ID Volume ID Publish Year Pages File Format Full-Text
17620 42684 2010 7 PDF Available
Title
Covalent bonding of protease to different sized enteric polymers and their potential use in wool processing
Abstract

A range of enteric polymeric molecules of different molecular masses and chemical structures were coupled to the protease Esperase (EC 3.4.21.62) using carbodiimide. The activities of the range of chemically modified enzymes of enlarged molecular weight were measured with a standard assay on casein as substrate. Gel filtration confirmed covalent bonding had taken place. Using the same activity value per gram of fibre, the range of modified enzymes were used to treat wool to see if the size of the enlarged enzyme would effect the location of enzyme attack and penetration ability. Less fibre damage in terms of weight loss and tensile strength of treated wool was observed for all six modified enzymes and was less than native enzyme of a similar activity level. All modified enzymes showed similar levels of improved shrink-resistance.

Keywords
Enteric polymer; Enzyme; Protease; Modified protease; Wool; Shrink-resistance
First Page Preview
Covalent bonding of protease to different sized enteric polymers and their potential use in wool processing
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 47, Issue 3, 5 August 2010, Pages 105–111
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering