Biosynthesis of 3‑Hydroxy-3-Methylbutyrate from l‑Leucine by Whole-Cell Catalysis
3-Hydroxy-3-methylbutyrate (HMB) is an important compound that can be used for the synthesis of a variety of chemicals in the food and pharmaceutical fields. Here, a biocatalytic method using l-leucine as a substrate was designed and constructed by expressing l-amino acid deaminase (l-AAD) and 4-hyd...
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Published in | Journal of agricultural and food chemistry Vol. 69; no. 12; pp. 3712 - 3719 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
31.03.2021
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Subjects | |
Online Access | Get full text |
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Summary: | 3-Hydroxy-3-methylbutyrate (HMB) is an important compound that can be used for the synthesis of a variety of chemicals in the food and pharmaceutical fields. Here, a biocatalytic method using l-leucine as a substrate was designed and constructed by expressing l-amino acid deaminase (l-AAD) and 4-hydroxyphenylpyruvate dioxygenase (4-HPPD) in Escherichia coli. To reduce the influence of the rate-limiting step on the cascade reaction, two 4-HPPD mutants were screened by rational design and both showed improved catalytic activity. Under optimal reaction conditions, the maximum conversion rate and production rate were 80% and 0.257 g/L·h, respectively. HMB production could be realized with high efficiency without an additional supply of adenosine triphosphate (ATP), which successfully overcomes the shortcomings of chemical production and fermentation methods. This design-based strategy of constructing a whole-cell catalyst system from l-leucine might serve as an alternative route to HMB synthesis. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-8561 1520-5118 |
DOI: | 10.1021/acs.jafc.1c00494 |