NDLI: Improved thermostable -amylase activity of Bacillus amyloliquefaciens by low-energy ion implantation.

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Improved thermostable -amylase activity of Bacillus amyloliquefaciens by low-energy ion implantation.

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Improved thermostable -amylase activity of Bacillus amyloliquefaciens by low-energy ion implantation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zhang, J. L. Li, X. Y. Zhu, S. W.
Description	Country affiliation: China Author Affiliation: Li XY ( Key Laboratory of Crop Biology of Anhui Province, School of Life Science, Anhui Agricultural University, Hefei, China.)
Abstract	Thermostable -amylase is of great importance in the starch fermentation industry; it is extensively used in the manufacture of beverages, baby foods, medicines, and pharmaceuticals. Bacillus amyloliquefaciens produces thermostable -amylase; however, production of thermostable -amylase is limited. Ion-beam implantation is an effective method for mutation breeding in microbes. We conducted ion-beam implantation experiments using two different ions, Ar(+) and N(+), to determine the survival rate of and dose effect on a high -amylase activity strain of B. amyloliquefaciens that had been isolated from soil samples. N(+) implantation resulted in a higher survival rate than Ar(+) implantation. The optimum implantation dose was 2.08 × 10(15) ions/cm(2). Under this implantation condition, we obtained a thermally and genetically stable mutant -amylase strain (RL-1) with high enzyme activity for degrading -amylase. Compared to the parental strain (RL), the RL-1 strain had a 57.1% increase in -amylase activity. We conclude that ion implantation in B. amyloliquefaciens can produce strains with increased production of thermostable -amylase.
e-ISSN	16765680
Journal	Genetics and Molecular Research
Issue Number	3
Volume Number	10
Language	English
Publisher	Fundação de Pesquisas Científicas de Ribeirão Preto
Publisher Date	2011-09-23
Publisher Place	Brazil
Access Restriction	Open
Subject Keyword	Bacillus Enzymology Mutation Alpha-amylases Metabolism Argon Chemistry Genetics Isolation & Purification Enzyme Stability Hot Temperature Ions Nitrogen Research Support, Non-u.s. Gov't Discipline Genetics Discipline Molecular Biology Discipline Bioinformatics
Content Type	Text
Resource Type	Article

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