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A novel glyA gene from the marine bacterium Alcanivorax sp. was cloned and expressed in Escherichia coli BL21(DE3). The recombinant glyA encodes a polypeptide of 418 amino acids, which was designated as AdSHMT that shows the highest identity (70%) with a SHMT from Shewanella algae. The purified enzyme showed
a single band at about 45 kDa by SDS-PAGE analysis. It was found that AdSHMT exhibited the maximal activity at 50 ◦ C and pH 7.0. The K m , V max , and K cat values of AdSHMT against dl-threo-3-phenylserine were calculated to be 0.097 mol/L, 3.255 ?mol/min/mg and 2.451/s, respectively. More importantly, RP-HPLC detection showed that the AdSHMT achieved an 88.37% molecular conversion rate in catalyzing glycine to l-serine, with the final concentration of l-serine being 353.15 mM in the reaction at 35 ◦ C and 22nd hour when the initial concentration of the substrate (glycine) was 0.399 M. The molecular conversion rate of the AdSHMT from the Alcanivorax sp. was 1.26-fold that of the EcSHMT from the E. coli,which is currently applied in industrial production. Therefore, AdSHMT has the potential for industrial applications due to its high enzymatic conversion rate. |
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到新单位后，换了新的研究方向，没有团队，持续积累2区以上论文，能申请到面上吗
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