| Content Provider |
World Health Organization (WHO)-Global Index Medicus |
| Author |
Lee, Hyun Woo Jung, Won Kyeong Kim, Yong Ho Ryu, Bum Han Kim, T. Doohun Kim, Jungho Kim, Hoon |
| Description |
Author Affiliation: Lee HW ( Department of Pharmacy, and Research Institute of Life Pharmaceutical Sciences, Sunchon National University, Suncheon 57922, Republic of Korea.); Jung WK ( Department of Pharmacy, and Research Institute of Life Pharmaceutical Sciences, Sunchon National University, Suncheon 57922, Republic of Korea.); Kim YH ( Department of Agricultural Chemistry, Sunchon National University, Suncheon 57922, Republic of Korea.); Ryu BH ( Department of Chemistry, Sookmyung Women's University, Seoul 04312, Republic of Korea.); Kim TD ( Department of Chemistry, Sookmyung Women's University, Seoul 04312, Republic of Korea.); Kim J ( Department of Agricultural Chemistry, Sunchon National University, Suncheon 57922, Republic of Korea.); Kim H ( Department of Pharmacy, and Research Institute of Life Pharmaceutical Sciences, Sunchon National University, Suncheon 57922, Republic of Korea.) |
| Abstract |
A novel esterase gene, est7K, was isolated from a compost metagenomic library. The gene encoded a protein of 411 amino acids and the molecular mass of the Est7K was estimated to be 44,969 Da with no signal peptide. Est7K showed the highest identity of 57% to EstA3, which is an esterase from a drinking water metagenome, when compared with the enzymes with reported properties. Est7K had three motifs, SMTK, YSV, and WGG, which correspond to the typical motifs of family VIII esterases, SxxK, Yxx, and WGG, respectively. Est7K did not have the GxSxG motif in most lipolytic enzymes. Three additional motifs, LxxxPGxxW, PLGMxDTxF, and GGxG, were found to be conserved in family VIII enzymes. The results of the phylogenetic analysis and the alignment study suggest that family VIII enzymes could be classified into two subfamilies, VIII.1 and VIII.2. The purified Est7K was optimally active at 40°C and pH 10.0. It was activated to exhibit a 2.1-fold higher activity by the presence of 30% methanol. It preferred short-length p-nitrophenyl esters, particularly p-nitrophenyl butyrate, and efficiently hydrolyzed glyceryl tributyrate. It did not hydrolyze ß-lactamase substrates, tertiary alcohol esters, glyceryl trioleate, fish oil, and olive oil. Est7K preferred an Senantiomer, such as (S)-methyl-3-hydroxy-2-methylpropionate, as the substrate. The tolerance to methanol and the substrate specificity may provide potential advantage in the use of the enzyme in pharmaceutical and other biotechnological processes. |
| File Format |
HTM / HTML |
| ISSN |
10177825 |
| e-ISSN |
17388872 |
| Journal |
Journal of Microbiology and Biotechnology |
| Issue Number |
2 |
| Volume Number |
26 |
| Language |
English |
| Publisher |
Korean Society for Microbiology and Biotechnology |
| Publisher Date |
2016-02-01 |
| Publisher Place |
Korea (South) |
| Access Restriction |
Open |
| Subject Keyword |
Discipline Microbiology Discipline Biotechnology Esterases Genetics Metabolism Metagenome Soil Microbiology Amino Acid Sequence Butyrates Cloning, Molecular Chemistry Isolation & Purification Fish Oils Gene Library Hydrogen-ion Concentration Lipase Methanol Olive Oil Phylogeny Sequence Alignment Stereoisomerism Substrate Specificity Triglycerides Beta-lactamases Research Support, Non-u.s. Gov't |
| Content Type |
Text |
| Resource Type |
Article |
| Subject |
Medicine Applied Microbiology and Biotechnology Biotechnology |
