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ABSTRACT:
SUBMITTER: Itoh T
PROVIDER: S-EPMC6796002 | biostudies-literature | 2019 Oct
REPOSITORIES: biostudies-literature
Itoh Takafumi T Nakagawa Emi E Yoda Moe M Nakaichi Akari A Hibi Takao T Kimoto Hisashi H
Scientific reports 20191016 1
A novel alginate lyase, PsAly, with a molecular mass of 33 kDa and whose amino acid sequence shares no significant similarity to other known proteins, was biochemically and structurally characterised from Paenibacillus sp. str. FPU-7. The maximum PsAly activity was obtained at 65 °C, with an optimum pH of pH 7-7.5. The activity was enhanced by divalent cations, such as Mg<sup>2+</sup>, Mn<sup>2+</sup>, or Co<sup>2+</sup>, and inhibited by a metal chelator, ethylenediaminetetraacetic acid. The re ...[more]