Characterization of a novel cold-adapted intracellular serine protease from the extremophile Planococcus halocryophilus Or1.

ABSTRACT: The enzymes of microorganisms that live in cold environments must be able to function at ambient temperatures. Cold-adapted enzymes generally have less ordered structures that convey a higher catalytic rate, but at the cost of lower thermodynamic stability. In this study, we characterized P355, a novel intracellular subtilisin protease (ISP) derived from the genome of Planococcus halocryophilus Or1, which is a bacterium metabolically active down to -25°C. P355's stability and activity at varying pH values, temperatures, and salt concentrations, as well as its temperature-dependent kinetics, were determined and compared to an uncharacterized thermophilic ISP (T0099) from Parageobacillus thermoglucosidasius, a previously characterized ISP (T0034) from Planococcus sp. AW0

SUBMITTER: Rasmussen CB 

PROVIDER: S-EPMC9995970 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature