ArticleThe protein journal2026
Cloning, Expression, Purification and Biochemical Characterization of Novel Thermostable Subtilisin-like Serine Protease from Thermococcus onnurineus NA1.
Article in The protein journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The persistent rise in demand for biocatalysts in industries has prompted the exploration of novel enzymes. Proteases are very important class of enzymes with many industrial applications. However, majority of the reported proteases are from mesophiles and exhibit low stability under harsh conditions limiting their potential applications. This study presents the expression and characterization of a novel thermostable recombinant subtilisin-like serine protease derived from Thermococcus onnurineus NA1. The subtilisin serine protease gene was successfully cloned and expressed in E. coli BL21. The recombinant protease was purified by affinity chromatography and has an estimated molecular mass of 29 kDa following SDS-PAGE analysis. It exhibited an optimal activity at a pH of 10 and temperature of 90 °C. The recombinant subtilisin-like serine protease maintained 96% of its activity at 100 °C. Additionally, Na
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