A Novel Cold-adapted Endoglucanase (M6A) from Microbacterium kitamiense S12 Isolated from Qinghai-Tibetan Plateau
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The gene M6A coding a novel cold-adapt endoglucanase was cloned from Microbacterium kitamiense Sa12 isolated from a wasteland in Saga, Qinghai-Tibetan Plateau. The deduced protein sequence encoded a 411-residue polypeptide sharing similar identities with glycosyl hydrolase family 6 enzymes. The recombinant M6A displayed maximum hydrolysis activity of 1.51 U/mg toward soluble cellulose substrate, CMC at 35°C and pH 5.0, and the Km and Vmax value were 2.12 mg/mL and 15.33 µmol/min*mg, respectively. Interestingly, M6A exhibited significant activity even at ice cold condition, showing 30–40% relative activity at 0–5°C, and had good tolerance to Li+, K+, NH4+, Rb+, Ca2+, Mg2+ Zn2+, Mn2+, and Ni2+, expect divalent cation Cu2+ led to 30% residual activity. These properties might make M6A to be a promising candidate used in the psychrophilic industrial process and/ or the volatile and thermosensitive manufacturing process.
Keywordsendoglucanase Microbacterium kitamiense cold-adapt protein modeling
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This study was supported by grants from the Key Laboratory of Biotic Environment and Ecology Safety in Anhui Province, Innovation Team of Scientific Research Platform in Anhui Universities and Provincial Key Project of Natural Science Research for Colleges and Universities of Anhui Province of China (KJ2017A321).
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