کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9616795 | 48895 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and properties of d-hydantoin hydrolase and N-carbamoyl-d-amino acid amidohydrolase from Flavobacterium sp. AJ11199 and Pasteurella sp. AJ11221
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
کاتالیزور
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
We characterized recombinant d-hydantoin hydrolase (DHHase) and N-carbamoyl-d-amino acid amidohydrolase (DCHase) from Flavobacterium sp. AJ11199 and Pasteurella sp. AJ11221. The DHHases from these two strains showed a wide range of hydrolytic activity for various 5-monosubstituted d-hydantoin compounds, including a very high level activity for d-hydantoin compounds corresponding to d-aromatic amino acids such as d-tryptophan d-phenylalanine and d-tyrosine. The DCHases, in turn, were capable of catalyzing the hydrolysis of various N-carbamoyl-d-amino acids (NCD-A.A.) corresponding to d-aliphatic and d-aromatic amino acids. The combination of these enzymes was found to be applicable for the production of various d-amino acids.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 32, Issues 5â6, 1 March 2005, Pages 205-211
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 32, Issues 5â6, 1 March 2005, Pages 205-211
نویسندگان
Hiroyuki Nozaki, Ikuo Kira, Kunihiko Watanabe, Kenzo Yokozeki,