ArticleExtremophiles : life under extreme conditions2011
Expression and characterization of a novel mesophilic protease from metagenomic library derived from Antarctic coastal sediment.
Article in Extremophiles : life under extreme conditions, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Enzymes for production of whey protein hydrolysates and other value-added products.Applied microbiology and biotechnology · 2024Review
- Characterization of novel proteases identified by metagenomic analysis from dairy stabilization ponds.Applied microbiology and biotechnology · 2023Article
- Two-step functional screen on multiple proteinaceous substrates reveals temperature-robust proteases with a broad-substrate range.Applied microbiology and biotechnology · 2021Article
- Current functional metagenomic approaches only expand the existing protease sequence space, but does not presently add any novelty to it.Current microbiology · 2015Article
- Identification and characterization of novel cellulolytic and hemicellulolytic genes and enzymes derived from German grassland soil metagenomes.Biotechnology letters · 2012Article
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Authors and funding
3 authors.
Funding
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Abstract
A metagenomic cosmid library was constructed, in which the insert DNA was derived from the coastal sediment near Antarctic China Zhongshan Station. One clone (ACPRO001) expressing protease activity was isolated from the library using milk agar plates. Sequencing of the clone revealed a novel protease gene. The amino acid sequence comparison and phylogenetic analysis indicated that it could be classified as a subtilisin-like serine protease, though the highly conserved residue Asp was replaced by Ala. The ACPRO001 protease gene was expressed in pET-His and purified for characterization. The optimal temperature and pH for the activity of the ACPRO001 protease were 60°C and pH 9.0, respectively. The enzyme retained about 73% of residual activity after 2 h incubation at 50°C in the presence of Ca(2+). The presence of Ca(2+) increased the thermostability of ACPRO001 protease obviously. The enzymatic activity was inhibited by 1 mM phenylmethyl sulfonylfluoride (PMSF) and hydrochloride 4-(2-aminoethyl)-benzenesulfonyl fluoride (AEBSF), indicating that it was a serine protease.
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