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A serine hydroxymethyltransferase from marine bacterium Shewanella algae: Isolation, purification, characterization and l-serine production.
Microbiol Res. 2013 Oct 01; 168(8):477-84.MR

Abstract

Currently, l-serine is mainly produced by enzymatic conversion, in which serine hydroxymethyltransferase (SHMT) is the key enzyme, suggesting the importance of searching for a SHMT with high activity. Shewanella algae, a methanol-utilizing marine bacterium showing high SHMT activity, was selected based on screening bacterial strains and comparison of the activities of SHMTs. A glyA was isolated from the S. algae through thermal asymmetric interlaced PCR (TAIL-PCR) and it encoded a 417 amino acid polypeptide. The SaSHMT, encoded by the glyA, showed the optimal activity at 50°C and pH 7.0, and retained over 45% of its maximal activity after incubation at 40°C for 3h. The enzyme showed better stability under alkaline environment (pH 6.5-9.0) than Hyphomicrobium methylovorum GM2's SHMT (pH 6.0-7.5). The SaSHMT can produce 77.76mM of l-serine by enzymatic conversion, with the molecular conversion rate in catalyzing glycine to l-serine being 1.41-fold higher than that of Escherichia coli. Therefore, the SaSHMT has the potential for industrial applications due to its tolerance of alkaline environment and a relatively high enzymatic conversion rate.

Authors+Show Affiliations

State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23632047

Citation

Jiang, Wei, et al. "A Serine Hydroxymethyltransferase From Marine Bacterium Shewanella Algae: Isolation, Purification, Characterization and L-serine Production." Microbiological Research, vol. 168, no. 8, 2013, pp. 477-84.
Jiang W, Xia B, Liu Z. A serine hydroxymethyltransferase from marine bacterium Shewanella algae: Isolation, purification, characterization and l-serine production. Microbiol Res. 2013;168(8):477-84.
Jiang, W., Xia, B., & Liu, Z. (2013). A serine hydroxymethyltransferase from marine bacterium Shewanella algae: Isolation, purification, characterization and l-serine production. Microbiological Research, 168(8), 477-84. https://doi.org/10.1016/j.micres.2013.04.002
Jiang W, Xia B, Liu Z. A Serine Hydroxymethyltransferase From Marine Bacterium Shewanella Algae: Isolation, Purification, Characterization and L-serine Production. Microbiol Res. 2013 Oct 1;168(8):477-84. PubMed PMID: 23632047.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A serine hydroxymethyltransferase from marine bacterium Shewanella algae: Isolation, purification, characterization and l-serine production. AU - Jiang,Wei, AU - Xia,Bingzhao, AU - Liu,Ziduo, Y1 - 2013/04/28/ PY - 2013/03/22/received PY - 2013/04/02/revised PY - 2013/04/02/accepted PY - 2013/5/2/entrez PY - 2013/5/2/pubmed PY - 2014/2/18/medline KW - Characterization KW - RP-HPLC KW - SHMT KW - TAIL-PCR KW - l-Serine enzymatic production SP - 477 EP - 84 JF - Microbiological research JO - Microbiol. Res. VL - 168 IS - 8 N2 - Currently, l-serine is mainly produced by enzymatic conversion, in which serine hydroxymethyltransferase (SHMT) is the key enzyme, suggesting the importance of searching for a SHMT with high activity. Shewanella algae, a methanol-utilizing marine bacterium showing high SHMT activity, was selected based on screening bacterial strains and comparison of the activities of SHMTs. A glyA was isolated from the S. algae through thermal asymmetric interlaced PCR (TAIL-PCR) and it encoded a 417 amino acid polypeptide. The SaSHMT, encoded by the glyA, showed the optimal activity at 50°C and pH 7.0, and retained over 45% of its maximal activity after incubation at 40°C for 3h. The enzyme showed better stability under alkaline environment (pH 6.5-9.0) than Hyphomicrobium methylovorum GM2's SHMT (pH 6.0-7.5). The SaSHMT can produce 77.76mM of l-serine by enzymatic conversion, with the molecular conversion rate in catalyzing glycine to l-serine being 1.41-fold higher than that of Escherichia coli. Therefore, the SaSHMT has the potential for industrial applications due to its tolerance of alkaline environment and a relatively high enzymatic conversion rate. SN - 1618-0623 UR - https://www.unboundmedicine.com/medline/citation/23632047/A_serine_hydroxymethyltransferase_from_marine_bacterium_Shewanella_algae:_Isolation_purification_characterization_and_l_serine_production_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0944-5013(13)00045-1 DB - PRIME DP - Unbound Medicine ER -