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• W2015657190 abstract "Chitin deacetylase catalyzes hydrolysis of the acetamido groups of N-acetylglucosamine of chitin in fungal cell walls. Here a chitin deacetylase secreted by Rhizopus circinans was purified to homogeneity and partially characterized. The enzyme exhibits an apparent molecular weight of ∼75 kDa. At 37 °C it shows optimal activity at pH 5.5–6. Its pH stability and thermal stability are good. Mn2+ and Mg2+ slightly enhance the activity of the enzyme and Cu2+ strongly inhibits it. An R. circinans cDNA library was constructed and screened with a homologous probe synthesized by RT-PCR or with synthetic primers derived from the N-terminal amino-acid sequence of the native purified chitin deacetylase. Three chitin deacetylase cDNAs (RC, D2, and I3/2) were isolated from the cDNA library and sequenced. These cDNAs exhibit features characteristic of chitin deacetylase sequences: the presence of a polysaccharide deacetylase domain, a metal-binding triad, the conserved catalytic residues, and high homology with various chitin deacetylase genes. The cDNAs were cloned in a Pichia pastoris expression system and produced as polyhistidine-tagged proteins. Only one recombinant enzyme (called RC) was active under the tested conditions. It was purified to homogeneity in a single step and further characterized. The protein showed an apparent molecular mass of ∼75 kDa and, like the native enzyme, showed optimal activity at pH 5.5–6 at 37 °C. It was strongly inhibited by Cu2+. The isolation of several chitin deacetylase cDNAs from the same microorganism is discussed." @default.
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• W2015657190 date "2008-05-01" @default.
• W2015657190 modified "2023-10-16" @default.
• W2015657190 title "Characterization and cloning of chitin deacetylases from Rhizopus circinans" @default.
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• W2015657190 doi "https://doi.org/10.1016/j.pep.2008.01.013" @default.
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