Catalytic and stereoselective properties of the immobilized amidase of Rhodococcus rhodochrous 4-1

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• 作者：A. N. Gorbunova ; Yu. G. Maksimova ; G. V. Ovechkina…
• 关键词：amidase ; immobilized enzyme ; stereoselectivity ; cross ; linked enzyme aggregates
• 刊名：Applied Biochemistry and Microbiology
• 出版年：2015
• 出版时间：September 2015
• 年：2015
• 卷：51
• 期：5
• 页码：539-545
• 全文大小：296 KB
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• 作者单位：A. N. Gorbunova (1)
  Yu. G. Maksimova (1) (2)
  G. V. Ovechkina (1)
  A. Yu. Maksimov (1) (2)
  
  1. Institute of Ecology and Genetics of Microorganisms, Ural Branch of the Russian Academy of Sciences, Perm, 614081, Russia
  2. Perm National State Research University, Perm, 614990, Russia
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Microbiology
  Medical Microbiology
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3024

文摘

The amidase of Rhodococcus rhodochrous 4-1 was immobilized by covalent attachment to activated chitosan by physical sorption on carbon adsorbents and by the formation of cross-linked aggregates in the absence of carrier. Comparative analysis of particular catalytic properties of the free and chitosan-immobilized amidase was performed. It was shown that the enzyme retained 50-0% of its initial activity after covalent immobilization on chitosan and was characterized by increased temperature stability as compared to soluble amidase. Moreover, the immobilized enzyme retained more than 20% of its activity after five 24-h cycles of acrylamide transformation. The effects of different types of immobilization on amidase stereoselective properties were studied by the model reaction of racemic lactamide hydrolysis to D-lactic acid and L-lactic acid. It was shown that cross-linked amidase aggregates possessed high D-stereoselectivity (up to 77-4%). The immobilized enzyme showed the highest enantioselectivity at 60°C. Keywords amidase immobilized enzyme stereoselectivity cross-linked enzyme aggregates