Isolation of an esterase-producing Trichosporon brassicae and its catalytic performance in kinetic resolution of ketoprofen

2001 ◽  
Vol 47 (12) ◽  
pp. 1101-1106 ◽  
Author(s):  
Duan Shen ◽  
Jian-He Xu ◽  
Peng-Fei Gong ◽  
Hui-Yuan Wu ◽  
You-Yan Liu
Keyword(s):  
Ethyl Ester ◽  
Sole Carbon Source ◽  
Kinetic Resolution ◽  
Enantiomeric Excess ◽  
Catalytic Performance ◽  
Soil Samples ◽  
Enantioselective Hydrolysis ◽  
Resting Cells ◽  
Enantiomeric Ratio ◽  
Hydrolysis Of

A yeast strain CGMCC 0574, identified as Trichosporon brassicae, was selected from 92 strains for its high (S) selectivity in the hydrolysis of ketoprofen ethyl ester. The effective strains of the microorganisms were isolated from soil samples with the ester as the sole carbon source. The ethyl ester proved to be the best substrate for resolution of ketoprofen among several ketoprofen esters examined. The resting cells of CGMCC 0574 could catalyze the hydrolysis of ketoprofen ethyl ester with an enantiomeric ratio of 44.9, giving (S)-ketoprofen an enantiomeric excess of 91.5% at 42% conversion.Key words: ketoprofen, biocatalytic resolution, enantioselective hydrolysis, microbial esterase, Trichosporon brassicae.

scholarly journals Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-Carboxymethylphosphonates

Catalysts ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 956
Author(s):  
Paulina Majewska
Keyword(s):  
Burkholderia Cepacia ◽  
Kinetic Resolution ◽  
Wide Spectrum ◽  
Candida Rugosa ◽  
Enantiomeric Excess ◽  
Optically Active ◽  
Enantiomeric Ratio ◽  
Catalyzed Reactions ◽  
Hydrolysis Of ◽  
Different Sources

The main objective of this study is the enantioselective synthesis of carboxyhydroxyphosphonates by lipase-catalyzed reactions. For this purpose, racemic dimethyl and dibutyl 1-butyryloxy-1-carboxymethylphosphonates were synthesized and hydrolyzed, using a wide spectrum of commercially available lipases from different sources (e.g., fungi and bacteria). The best hydrolysis results of dimethyl 1-butyryloxy-1-carboxymethylphosphonate were obtained with the use of lipases from Candida rugosa, Candida antarctica, and Aspergillus niger, leading to optically active dimethyl 1-carboxy-1-hydroxymethylphosphonate (58%–98% enantiomeric excess) with high enantiomeric ratio (reaching up to 126). However, in the case of hydrolysis of dibutyl 1-butyryloxy-1-carboxymethylphosphonate, the best results were obtained by lipases from Burkholderia cepacia and Termomyces lanuginosus, leading to optically active dibutyl 1-carboxy-1-hydroxymethylphosphonate (66%–68% enantiomeric excess) with moderate enantiomeric ratio (reaching up to 8.6). The absolute configuration of the products after biotransformation was also determined. In most cases, lipases hydrolyzed (R) enantiomers of both compounds.

scholarly journals Application of Lecitase® Ultra-Catalyzed Hydrolysis to the Kinetic Resolution of (E)-4-phenylbut-3-en-2-yl Esters

Catalysts ◽  
2018 ◽  
Vol 8 (10) ◽  
pp. 423 ◽  
Author(s):  
Aleksandra Leśniarek ◽  
Anna Chojnacka ◽  
Witold Gładkowski
Keyword(s):  
Kinetic Resolution ◽  
Enantiomeric Excess ◽  
Optical Purity ◽  
Enantioselective Hydrolysis ◽  
Hydrolysis Of ◽  
Allyl Esters

The possibility of using Lecitase® Ultra as a novel alternative biocatalyst for the kinetic resolution of model racemic allyl esters of (E)-4-phenylbut-3-en-3-ol: Acetate (4a) and propionate (4b) through their enantioselective hydrolysis was investigated. Reaction afforded (+)-(R)-alcohol (3) and unreacted (−)-(S)-ester (4a or 4b). Hydrolysis of propionate 4b proceeded with higher enantioselectivity than acetate 4a. (R)-Alcohol (3) with highest enantiomeric excess (93–99%) was obtained at 20–30 °C by hydrolysis of propionate 4b, while the highest optical purity of unreacted substrate was observed for (S)-acetate 4a (ee = 34–56%). The highest enantioselectivity was found for the hydrolysis of propionate 4b catalyzed at 30 °C (E = 38). Reaction carried out at 40 °C significantly lowered enantiomeric excess of produced alcohol 3 and enantioselectivity in resolution. Lecitase® Ultra catalyzed the enantioselective hydrolysis of allyl esters 4a,b according to Kazlauskas’ rule to produce (R)-alcohol 3 and can find application as a novel biocatalyst in the processes of kinetic resolution of racemic allyl esters.

Production of l-tryptophan by enantioselective hydrolysis of d,l-tryptophanamide using a newly isolated bacterium

2013 ◽  
Vol 67 (10) ◽  
Author(s):  
Jian-Miao Xu ◽  
Ben Chen ◽  
Yuan-Shan Wang ◽  
Yu-Guo Zheng
Keyword(s):  
Enantiomeric Excess ◽  
Fold Increase ◽  
Fermentation Medium ◽  
High Yield ◽  
Enantioselective Hydrolysis ◽  
16S Rdna Sequence ◽  
16S Rdna Sequence Analysis ◽  
Enantiomeric Ratio ◽  
Physiological Tests ◽  
Hydrolysis Of

AbstractBacterial strain ZJB-09211 capable of amidase production has recently been isolated from soil samples. The strain is able to asymmetrically hydrolyze l-tryptophanamide from d,l-tryptophanamide to produce l-tryptophan in high yield and with excellent stereoselectivity (enantiomeric excess > 99.9 %, and enantiomeric ratio > 200). Strain ZJB-09211 has been identified as Flavobacterium aquatile based on the cell morphology analysis, physiological tests, and the 16S rDNA sequence analysis. Optimization of the fermentation medium led to an about six-fold increase in the amidase activity of strain ZJB-09211, which reached 501.5 U L−1. Substrate specifity and stereoselectivity investigations revealed that amidase of F. aquatile possessed a broad substrate spectrum and high enantioselectivity.

Enantioselective Hydrolysis of a Schiff's Base of D,L-Phenylalanine Ethyl Ester in Water-Poor Media Via the Reaction Catalyzed with α-Chymotrypsin Immobilized on Hydrophilic Macroporous Gel Support

2000 ◽  
Vol 88 (1-3) ◽  
pp. 097-106 ◽  
Author(s):  
Yury N Belokon ◽  
Konstantin A Kochetkov ◽  
Fatima M Pleiva ◽  
Nikolai S Ikonnikov ◽  
Viktor I Maleev ◽  
...  
Keyword(s):  
Ethyl Ester ◽  
Enantioselective Hydrolysis ◽  
Schiff’S Base ◽  
Hydrolysis Of

Enantioselective hydrolysis of amino acid esters by apomyoglobin: perfect kinetic resolution of a phenylalanine derivative

2001 ◽  
pp. 133-134 ◽  
Author(s):  
Katsuhiko Tomisaka ◽  
Yasuhiro Ishida ◽  
Katsuaki Konishi ◽  
Takuzo Aida
Keyword(s):  
Amino Acid ◽  
Kinetic Resolution ◽  
Enantioselective Hydrolysis ◽  
Amino Acid Esters ◽  
Hydrolysis Of ◽  
Acid Esters

SCREENING OF STRAINS FOR ENANTIOSELECTIVE HYDROLYSIS OF RACEMIC MENTHYL BENZOATE TO PRODUCT L-MENTHOL

2013 ◽  
pp. 63-69
Author(s):  
Thi Minh Thu Ngo ◽  
Gao-Wei Zheng ◽  
Jian-He Xu
Keyword(s):  
Catalytic Properties ◽  
Hydrolytic Activity ◽  
Soil Samples ◽  
Enantioselective Hydrolysis ◽  
16S Rdna Sequence ◽  
Optimum Ph ◽  
Acinetobacter Sp ◽  
Hydrolysis Of ◽  
Dry Cell ◽  
Biocatalytic Process

Background: Because of pleasant flavor and aroma as well as cooling-anesthetic effect, menthol and mint oils are widely used in the flavor industry and biocatalytic processes for production of l-menthol are more interested nowadays. Herein, we attempted to develop a biocatalytic process for production of l-menthol through enantioselective hydrolysis of dl-menthyl benzoate using a strain newly isolated from soil. Methods: From soil samples, we were isolated one strain exhibited the best hydrolytic activity and excellent enantioselectivity as compared to others. So, it was selected as the best enzyme producer and subsequently identified as Acinetobacter sp. based on the 99% similarity of its 16S rDNA sequence, and named Acinetobacter sp. ECU2040. The fermentation process was studied and the fermentation gave about 130 g wet cell, which was equivalent to 18 g dry cell. The catalytic properties of Acinetobacter sp. ECU2040 were also studied. The results showed that the optimum pH and temperature of reaction were 7.5 and 37ºC, respectively. Results and conclusion: The strain Acinetobacter sp. ECU2040 strain exhibited the production of l-menthol ability with the best hydrolytic activity and excellent enantioselectivity. Key words: l-menthol, enantioselective, isolated strain

Kinetic resolution of unnatural and rarely occurring amino acids: enantioselective hydrolysis of N-acyl amino acids catalyzed by acylase I

1989 ◽  
Vol 111 (16) ◽  
pp. 6354-6364 ◽  
Author(s):  
H. Keith Chenault ◽  
Juergen Dahmer ◽  
George M. Whitesides
Keyword(s):  
Amino Acids ◽  
Kinetic Resolution ◽  
Enantioselective Hydrolysis ◽  
Acylase I ◽  
Hydrolysis Of
Sign in / Sign up

Export Citation Format

Share Document