Abstract：
:(R)-2-hydroxy-4-phenylbutyric acid (R-HPBA) is a valuable intermediate for the synthesis of angiotensin-converting enzyme inhibitors. The asymmetric reduction of 2-oxo-4-phenylbutyric acid (OPBA) by oxidoreductases is an efficient approach for its synthesis. Here, we report a novel biocatalytic approach for asymmetric synthesis of R-HPBA using recombinant Pichia pastoris expressing the Tyr52Leu variant of D-lactate dehydrogenase (D-LDH) from Lactobacillus plantarum. The recombinant yeast cells showed impressive catalytic activity at a high concentration of NaOPBA (380 mM, 76 g/L) and achieved full conversion starting with 40 g/L NaOPBA or even at higher concentration. Under optimized reaction conditions (pH 7.5, 37 °C, and 2% glucose), a full conversion with > 95% reaction yield and ~ 100% product enantiomeric excess (ee) was achieved for the preparation of R-HPBA on a 2-g scale. The findings of this study promote both the biotransformation of R-HPBA and an extension of the application of recombinant yeast as biocatalysts.
journal_name
Bioprocess Biosyst Engjournal_title
Bioprocess and biosystems engineeringauthors
Wang X,Yu Z,Tang J,Yi D,Chen Sdoi
10.1007/s00449-018-1965-5subject
Has Abstractpub_date
2018-09-01 00:00:00pages
1383-1390issue
9eissn
1615-7591issn
1615-7605pii
10.1007/s00449-018-1965-5journal_volume
41pub_type
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