NDLI: Purification and Characterization of a Cold-Adapted α-Amylase Produced by Nocardiopsis sp. 7326 Isolated from Prydz Bay, Antarctic

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Purification and Characterization of a Cold-Adapted α-Amylase Produced by Nocardiopsis sp. 7326 Isolated from Prydz Bay, Antarctic

Content Provider	Springer Nature Link
Author	Zhang, Jin Wei Zeng, Run Ying
Copyright Year	2007
Abstract	An actinomycete strain 7326 producing cold-adapted α-amylase was isolated from the deep sea sediment of Prydz Bay, Antarctic. It was identified as Nocardiopsis based on morphology, 16S rRNA gene sequence analysis, and physiological and biochemical characteristics. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and zymogram activity staining of purified amylase showed a single band equal to a molecular mass of about 55 kDa. The optimal activity temperature of Nocardiopsis sp. 7326 amylase was 35°C, and the activity decreased dramatically at temperatures above 45°C. The enzyme was stable between pH 5 and 10, and exhibited a maximal activity at pH 8.0. Ca2+, Mn2+, Mg2+, Cu2+, and Co2+ stimulated the activity of the enzyme significantly, and Rb2+, Hg2+, and EDTA inhibited the activity. The hydrolysates of soluble starch by the enzyme were mainly glucose, maltose, and maltotriose. This is the first report on the isolation and characterization of cold-adapted amylase from Nocardiopsis sp.
Starting Page	75
Ending Page	82
Page Count	8
File Format	PDF
ISSN	14362228
Journal	Marine Biotechnology
Volume Number	10
Issue Number	1
e-ISSN	14362236
Language	English
Publisher	Springer-Verlag
Publisher Date	2007-10-13
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	cold-adapted α-amylase Nocardiopsis purification and characterization Engineering Zoology Microbiology Freshwater & Marine Ecology
Content Type	Text
Resource Type	Article
Subject	Aquatic Science Biotechnology

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