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Isolation and characterization of a novel thermostable α-amylase from Korean pine seeds

Paper ID Volume ID Publish Year Pages File Format Full-Text
33859 44994 2009 7 PDF Available
Title
Isolation and characterization of a novel thermostable α-amylase from Korean pine seeds
Abstract

Amylases have significant importance in broad industrial application including bio-ethanol production. Although amylases are widely distributed in microbes, plants and animals, it has been sought for new amylases from various sources with special industrial potential. In this study we firstly isolated and characterized a novel thermostable α-amylase from Korean pine seed. Enzyme was purified to homogeneity level with purification fold of 1286.1 using several techniques such as self-precipitation, (NH4)2SO4 fractionation, DEAE anion exchange and starch affinity chromatography. The purified α-amylase showed two bands in SDS-PAGE with molecular weight of 44 and 45 kDa. The apparent molecular weight of native enzyme was calculated to be 46.7 kDa. Internal peptide sequencing confirmed that the purified α-amylase was a novel enzyme. The optimum pH and temperature for enzyme activity were pH 4.5 and 65 °C, respectively. This enzyme was fully stable for 48 h at 50 °C and retained 80% activity up to 96 h. The Km and Vmax were 0.84 mg/ml and 3.71 μmol/min, respectively. On the basis of high thermal stability and a broad range of pH stability, the pine seed α-amylase showed a good prospect of industrial application.

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Isolation and characterization of a novel thermostable α-amylase from Korean pine seeds
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Publisher
Database: Elsevier - ScienceDirect
Journal: New Biotechnology - Volume 26, Issues 3–4, 31 October 2009, Pages 143–149
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