ArticleExtremophiles : life under extreme conditions2015
A pectate lyase from a deep subseafloor Georgenia muralis with unusual molecular characteristics.
Article in Extremophiles : life under extreme conditions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed, 8 citations in OpenAlex.
- A high-molecular-weight, alkaline, and thermostable β-1,4-xylanase of a subseafloor Microcella alkaliphila.Extremophiles : life under extreme conditions · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
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Abstract
A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the presence of SDS. The purified enzyme (Pel-S2) had a molecular mass of ~51 kDa by SDS-PAGE and ~75 kDa by gel filtration. In contrast, without heat treatment, the purified enzyme in SDS sample buffer was found to consist of 23- and 23.5-kDa polypeptides by SDS-PAGE. The enzyme was gradually inactivated by heat treatment with and without SDS in parallel with a shift of polypeptides molecular masses from 23 and 23.5 to 51 kDa on SDS-PAGE. Pel-S2 degraded pectate optimally at pH 10 in a glycine buffer and temperature of 50 °C. The enzyme showed relatively broad substrate specificity toward pectic acid and pectin.
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