Dataset Information

Surfactant-modified Aspergillus oryzae lipase as a highly active and enantioselective catalyst for the kinetic resolution of (RS)-1-phenylethanol.

ABSTRACT: The lipase from Aspergillus oryzae was modified with a surfactant and then observed to exhibit high catalytic efficiency and enantioselectivity for the kinetic resolution of (RS)-1-phenylethanol. The influential factors of the modified-lipase preparation were investigated, including the surfactant source, the organic cosolvent, and the buffer pH. The optimum modification conditions were found with a surfactant of polyoxyethylene sorbitan monopalmitate, an organic cosolvent of tetrahydrofuran and a phosphate buffer of pH 7.0. In the transesterification of (RS)-1-phenylethanol with vinyl acetate, the surfactant-modified lipase showed excellent enantioselectivity for the R-isomer (E?>?200), giving an enantiomeric excess of higher than 99% for (R)-1-phenylethyl acetate at 46.8% conversion with the reaction time of 2 h at 30 °C. The enzymatic activity had barely altered after 30 days even at 50 °C when it was saved in a powdered state. The results indicated that the modification strategy was useful and highly efficient, and that modified A. oryzae lipase was a promising biocatalyst in the kinetic resolution of (RS)-1-phenylethanol.

SUBMITTER: Yan H

PROVIDER: S-EPMC6562008 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

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Surfactant-modified Aspergillus oryzae lipase as a highly active and enantioselective catalyst for the kinetic resolution of (RS)-1-phenylethanol.

Yan Hong De H Guo Bing Han BH Wang Zhao Z Qian Jun Qing JQ

3 Biotech 20190612 7

The lipase from Aspergillus oryzae was modified with a surfactant and then observed to exhibit high catalytic efficiency and enantioselectivity for the kinetic resolution of (RS)-1-phenylethanol. The influential factors of the modified-lipase preparation were investigated, including the surfactant source, the organic cosolvent, and the buffer pH. The optimum modification conditions were found with a surfactant of polyoxyethylene sorbitan monopalmitate, an organic cosolvent of tetra ...[more]

PMID: 31218176

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Project description:BACKGROUND:Obesity and its related diseases are increasing worldwide. One of the best therapeutic strategies for obesity management is through the inhibition of pancreatic lipase (PL) enzyme. So far orlistat is the only FDA approved PL inhibitor, but with unpleasant side effects. New efficacious anti-obesity drugs are needed to achieve a successful reduction in the incidence and prevalence of obesity. Many microbial metabolites have PL inhibitory activity. Screening soil inhabitants for PL inhibitors could help in increasing the available anti-obesity drugs. We aimed to isolate and identify alternative PL inhibitors from soil flora. RESULTS:We screened the crude mycelial methanolic extracts of 39 soil samples for PL inhibitory activity by the quantitative lipase colorimetric assay, using the substrate p-nitrophenyl palmitate and orlistat as positive control. AspsarO, a PL inhibitor producer, was isolated from an agricultural field soil in Giza, Egypt. It was identified as Aspergillus oryzae using colony morphology, microscopical characteristics, 18S rDNA sequencing, and molecular phylogeny. Increasing the PL inhibitor activity, in AspsarO cultures, from 25.9?±?2% to 61.4?±?1.8% was achieved by optimizing the fermentation process using a Placket-Burman design. The dried 100% methanolic fraction of the AspsarO culture had an IC50 of 7.48??g/ml compared to 3.72??g/ml for orlistat. It decreased the percent weight gain, significantly reduced the food intake and serum triglycerides levels in high-fat diet-fed Sprague-Dawley rats. Kojic acid, the active metabolite, was identified using several biological guided chromatographic and 1H and 13C NMR techniques and had an IC50 of 6.62??g/ml. Docking pattern attributed this effect to the interaction of kojic acid with the key amino acids (Lys80, Trp252, and Asn84) in PL enzyme binding site. CONCLUSION:Combining the results of the induced obesity animal model, in silico molecular docking and the lipase inhibitory assay, suggests that kojic acid can be a new therapeutic option for obesity management. Besides, it can lower serum triglycerides in obese patients.

Dataset Information

Surfactant-modified Aspergillus oryzae lipase as a highly active and enantioselective catalyst for the kinetic resolution of (RS)-1-phenylethanol.

Publications

Surfactant-modified <i>Aspergillus oryzae</i> lipase as a highly active and enantioselective catalyst for the kinetic resolution of (<i>RS</i>)-1-phenylethanol.

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