NDLI: Molecular cloning, expression and characterization of alpha-amylase gene from a marine bacterium Pseudoalteromonas sp. MY-1.

Content Provider	Semantic Scholar
Author	Tao, Xueying Jang, Moon-Sun Kim, Kyoung-Sook Yu, Ziniu Lee, Young-Choon
Copyright Year	2008
Abstract	A gene (amyA) encoding an extracellular alpha-amylase from a marine bacterium Pseudoalteromnonas sp. MY-1 was cloned and expressed in Escherichia coli. It comprised an open-reading-frame of 2,007 base pairs and encoded a protein of 669 amino acids with a predicted molecular weight of 73,770 daltons and a pI of 5.15. The entire amino acid sequence of amyA gene showed 86% similarity to the alpha-amylase preproprotein from Pseudoalteromonas haloplanktis. It consisted of a signal peptide, alpha-amylase catalytic domain and an amy C domain. The recombinant amylase was purified to homogeneity and biochemically characterized. The enzyme revealed maximum activity at pH 7.0 and 40 degrees C. The enzyme hydrolyzed soluble starch and some maltooligosaccharides to several oligosaccharides, and maltose was the common product from different substrates.
File Format	PDF HTM / HTML
PubMed reference number	19069841
Journal	Medline
Volume Number	45
Issue Number	5
Alternate Webpage(s)	http://nopr.niscair.res.in/bitstream/123456789/2371/1/IJBB%2045(5)%20305-309.pdf
Journal	Indian journal of biochemistry & biophysics
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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