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Characterization of new β-galactosidase from acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1

Paper ID Volume ID Publish Year Pages File Format Full-Text
20758 43190 2013 5 PDF Available
Title
Characterization of new β-galactosidase from acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1
Abstract

The β-galactosidase exhibiting high activity from an extremely acidic pH region to neutral pH region was efficiently purified from an acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1, using affinity chromatography with Toyopearl resins immobilized 4-aminophenyl-β-d-galactopyranoside. The enzyme was stable in the pH range from 1.5 to 7.0, and exhibited optimal activity at pH 2.5–4.0 and 70°C. 2-Nitrophenyl-β-d-galactopyranoside, 4-nitrophenyl-β-d-galactopyranoside and lactose were rapidly hydrolyzed, and the apparent Km values were estimated to be 0.19 mM, 1.2 mM and 170 mM, respectively. Thus, the enzyme can be used in the wide pH range for hydrolysis of lactose. The molecular mass of the enzyme was estimated to be 140 kDa with two hetero subunits of 86 kDa and 50 kDa. The N-terminal amino acid sequence of the small subunit was found to be NTRMIIFNDK. These enzymatic and physicochemical characteristics are remarkably different from those of the previously known β-galactosidases.

Keywords
β-Galactosidase; Lactase; Acidophilic fungus; Teratosphaeria acidotherma; Lactose
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Characterization of new β-galactosidase from acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 116, Issue 3, September 2013, Pages 293–297
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
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us