A serine hydroxymethyltransferase from marine bacterium Shewanella algae: Isolation, purification, characterization and l

Add time:08/10/2019    Source:sciencedirect.com

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 3 h. 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 77.76 mM 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.

We also recommend Trading Suppliers and Manufacturers of L-Serine hydrochloride (cas 16428-75-4). Pls Click Website Link as below: cas 16428-75-4 suppliers

Prev:Experimental and theoretical study on the interactions between dopamine hydrochloride and nicotinamide
Next:Trigonelline hydrochloride: A promising inhibitor for type I collagen fibrillation)