Morris, Laura S. and Marchesi, Julian Roberto ![]() |
Abstract
Proteases are a fundamental function in many organisms and thus many ecosystems and yet they are rarely obtained in functional metagenomic screens. Here, we have isolated an active protease gene (M1-2; 613 amino acids) which resided in a 38.4 kb fosmid clone that showed a classical protease-positive phenotype. It was classified as a zinc-dependent metalloprotease, with the closest annotated sequence as a neutral protease from Collimonas fungivorans (62 % similarity and 72 % homology). Further characterisation showed that its optimum temperature and pH were 42 °C and 8.0, respectively. Activity was inhibited by EDTA, but inhibition started to be reversed by excess Zn2+. A putative signal peptide was identified bioinformatically and this may be why this protease was successfully isolated using a functional metagenomic screen. Bioinformatic analysis shows that this does not represent a novel protease, but simply expands the current sequence space of known proteases.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Biosciences Systems Immunity Research Institute (SIURI) |
Subjects: | Q Science > QR Microbiology |
Publisher: | Springer Verlag |
ISSN: | 0343-8651 |
Last Modified: | 28 Oct 2022 08:34 |
URI: | https://orca.cardiff.ac.uk/id/eprint/71284 |
Citation Data
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