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Insoluble complex formation between alpha-amylase from Aspergillus oryzae and polyacrylic acid of different molecular weight

Paper ID Volume ID Publish Year Pages File Format Full-Text
35522 45093 2010 4 PDF Available
Title
Insoluble complex formation between alpha-amylase from Aspergillus oryzae and polyacrylic acid of different molecular weight
Abstract

The insoluble complex formation between alpha-amylase and the strong anionic polyelectrolyte polyacrylic acid was studied by using turbidimetric and enzymatic activity. The highest molecular weight polyacrylic acid (100,000 Da and 240,000 Da) proved to be suitable precipitating agents. They were insoluble at pH lower than 4–5, with a stoichiometric ratio polymer mol per protein mol of 1:52 and 1:154, respectively. Electrostatic interactions are not the only factor in the formation of insoluble complexes. High percentage of alpha-amylase enzymatic activity maintains throughout time, even in the presence of polyelectrolyte.The application of precipitation conditions found when applying a bovine homogenate showed that it is not suitable for purification even if it proved to be useful methodology for the concentration of the enzyme and can be used as a first step of purification.

Keywords
Alpha-amylase; Polyacrylic acid; Polyelectrolyte; Polymer; Precipitation; Bioseparation
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Insoluble complex formation between alpha-amylase from Aspergillus oryzae and polyacrylic acid of different molecular weight
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 45, Issue 10, October 2010, Pages 1753–1756
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
Online Support
Any Questions? feel free to contact us