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Characterization and application of a l-specific amino acid oxidase from Rhodococcus sp. AIU LAB-3

Paper ID Volume ID Publish Year Pages File Format Full-Text
20719 43188 2013 5 PDF Available
Title
Characterization and application of a l-specific amino acid oxidase from Rhodococcus sp. AIU LAB-3
Abstract

An l-specific amino acid oxidase (l-AAO) suitable for assay of N-acyl-l-amino acid amidohydrolase (l-aminoacylase) activity was purified from Rhodococcus sp. AIU LAB-3. The enzyme exhibited broad substrate specificity and catalyzed an oxidative deamination of the α-amino group of l-amino acids. The optimal enzyme activities for l-amino acids tested were observed in the pH range from 6.0 to 8.5, and more than 80% of the maximum activity was obtained at pH 7.5. The enzyme was stable in the pH range from 7.0 to 8.5, and the apparent Km values for those l-amino acids were small. We, therefore, developed a new enzymatic method for assay of l-aminoacylase activity using the l-AAO at pH 7.5. The new enzymatic method had advantages that the l-aminoacylase reaction was spectrophotometrically followed by measuring absorbance at 555 nm. The l-aminoacylase activity was assayed within 10 min using a small reaction volume. Thus, the new enzymatic method was simple and sensitive compared to the ninhydrin method.

Keywords
l-Amino acid oxidase; l-Aminoacylase; Rhodococcus; Ninhydrin; N-Acyl-amino acid amidohydrolase
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Characterization and application of a l-specific amino acid oxidase from Rhodococcus sp. AIU LAB-3
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 115, Issue 6, June 2013, Pages 613–617
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
100% Money Back Guarantee
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Any Questions? feel free to contact us