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

Casper Bøjer Rasmussen, Carsten Scavenius, Ida B Thøgersen, Seandean Lykke Harwood, Øivind Larsen, Gro Elin Kjaereng Bjerga, Peter Stougaard, Jan J Enghild, Mariane Schmidt Thøgersen*

*Corresponding author for this work

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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. AW02J18, and Subtilisin Carlsberg (SC). The results showed that P355 was the most heat-labile of these enzymes, closely followed by T0034. P355 and T0034 exhibited catalytic constants (k cat ) that were much higher than those of T0099 and SC. Thus, both P355 and T0034 demonstrate the characteristics of the stability-activity trade-off that has been widely observed in cold-adapted proteases.

Original languageEnglish
Article number1121857
JournalFrontiers in Microbiology
Number of pages15
Publication statusPublished - 2023


  • calcium
  • characterization
  • cold adaptation
  • intracellular subtilisin protease
  • maturation
  • Planococcus
  • protein chemistry


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