Journal
JOURNAL OF BIOTECHNOLOGY
Volume 306, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.btecx.2019.100008
Keywords
Enzymatic cascade reaction; Oleate hydratase; Alcohol dehydrogenase; Hydration; 10-Hydroxystearic acid; 10-0xostearic acid
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Funding
- National Natural Science Foundation of China [21536004, 21871085, 21776085]
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Hydroxy fatty acids and carbonyl fatty acids are important multi-functional materials for the manufacture of fragrances and other fine chemicals. In this study, a novel oleate hydratase (PaOH) was cloned from Paracoccus aminophilus DSM 8538 and solubly expressed in Escherichia coll. The recombinant PaOH efficiently catalyzed the hydration of oleic acid, with a specific activity of 5.21 U mg(-1) protein. Enzymatic hydration of oleic acid was optimized for the production of 10-hydroxystearic acid. Under the optimal conditions, a pilot reaction was performed on a 1-L scale, where 90 g L-1 of oleic acid was converted into 10-hydroxystearic acid by 10 g L-1 of lyophilized enzyme within 4 h, achieving a conversion of 96.1% and a space-time yield of up to 552 g L-1 d(-1). The resultant 10-hydroxystearic acid was further converted into 10-oxostearic acid, via enzymatic cascade with a secondary alcohol dehydrogenase (MIADH) from Micrococcus luteus WIUJH2O, using a lactate dehydrogenase (LdLDH) from Lactobacillus delbrueckii to drive the co-enzyme regeneration. The cascade reaction was carried out stepwise in one pot. Total conversion reached 95.0% after 10 h reaction at a scale of 1 L, with a space time yield of 217 g L-1 d(-1). The final yield of 10-oxostearic acid isolated was 52.2% (mol mol(-1)), with a purity of >99.0%.
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