دورية أكاديمية
Rational identification of a high catalytic efficiency leucine dehydrogenase and process development for efficient synthesis of l-phenylglycine.
العنوان: | Rational identification of a high catalytic efficiency leucine dehydrogenase and process development for efficient synthesis of l-phenylglycine. |
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المؤلفون: | Meng X; State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China., Liu Y; State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China., Yang L; State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China., Li R; State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China., Wang H; State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China., Shen Y; State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China., Wei D; State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China. |
المصدر: | Biotechnology journal [Biotechnol J] 2023 May; Vol. 18 (5), pp. e2200465. Date of Electronic Publication: 2023 Feb 20. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: Wiley-VCH Verlag Country of Publication: Germany NLM ID: 101265833 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1860-7314 (Electronic) Linking ISSN: 18606768 NLM ISO Abbreviation: Biotechnol J Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: Weinheim : Wiley-VCH Verlag, c2006- |
مواضيع طبية MeSH: | Glycine* , Amino Acids*, Leucine Dehydrogenase/genetics ; Leucine Dehydrogenase/metabolism ; Catalysis ; Substrate Specificity ; Leucine |
مستخلص: | Enzymatic asymmetric synthesis of chiral amino acids has great industrial potential. However, the low catalytic efficiency of high-concentration substrates limits their industrial application. Herein, using a combination of substrate catalytic efficiency prediction based on "open to closed" conformational change and substrate specificity prediction, a novel leucine dehydrogenase (TsLeuDH), with high substrate catalytic efficiency toward benzoylformic acid (BFA) for producing l-phenylglycine (l-Phg), was directly identified from 4695 putative leucine dehydrogenases in a public database. The specific activity of TsLeuDH was determined to be as high as 4253.8 U mg -1 . Through reaction process optimization, a high-concentration substrate (0.7 m) was efficiently and completely converted within 90 min in a single batch, without any external coenzyme addition. Moreover, a continuous flow-feeding approach was designed using gradient control of the feed rate to reduce substrate accumulation. Finally, the highest overall substrate concentration of up to 1.2 m BFA could be aminated to l-Phg with conversion of >99% in 3 h, demonstrating that this new combination of enzyme process development is promising for large-scale application of l-Phg. (© 2023 Wiley-VCH GmbH.) |
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معلومات مُعتمدة: | 2021YFC2102100 National Key Research and Development Program of China |
فهرسة مساهمة: | Keywords: bioprocess development; conformational change; genome mining; l-phenylglycine; leucine dehydrogenase |
المشرفين على المادة: | EC 1.4.1.9 (Leucine Dehydrogenase) 69-91-0 (2-phenylglycine) TE7660XO1C (Glycine) 0 (Amino Acids) GMW67QNF9C (Leucine) |
تواريخ الأحداث: | Date Created: 20230204 Date Completed: 20230510 Latest Revision: 20230510 |
رمز التحديث: | 20231215 |
DOI: | 10.1002/biot.202200465 |
PMID: | 36738237 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1860-7314 |
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DOI: | 10.1002/biot.202200465 |