Substrate profiling of marine-derived thermotolerant cysteine protease reveals unique cleavage preferences for industrial applications.

ABSTRACT: Due to their industrial importance, new proteases are constantly being sourced from the marine environment. However, their substrate specificities remain insufficiently studied, restricting the evaluation of their potential applications. Here, we applied multiplex substrate profiling by mass spectrometry (MSP-MS) to globupain, a marine thermotolerant clostripain-like protease and show that it has a novel substrate specificity. Globupain is an endopeptidase with a preference for cleavage of substrates on the C-terminal side of norleucine (Nle), Leu, Asn, Arg and Lys. While it can hydrolyze gelatin and collagen, its reaction rate is lower than that of papain, a commercial cysteine protease. The precise knowledge of substrate specificity of globupain led to the discovery that the calpain inhi

SUBMITTER: Royseth V 

PROVIDER: S-EPMC12280095 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature