Biochemical characterization of the novel endo-β-mannanase AtMan5-2 from Arabidopsis thaliana.
作者： Yang Wang , Shoaib Azhar , Rosaria Gandini , Christina Divne , Ines Ezcurra
DOI: 10.1016/J.PLANTSCI.2015.10.002
关键词: Mannan 、 Glycoside hydrolase family 5 、 Arabidopsis 、 Biochemistry 、 Glycoside hydrolase 、 Galactoglucomannan 、 Biology 、 Beta-mannosidase 、 Mannose 、 Pichia pastoris
摘要: Plant mannanases are enzymes that carry out fundamentally important functions in cell wall metabolism during plant growth and development by digesting manno-polysaccharides. In this work, the Arabidopsis mannanase 5-2 (AtMan5-2) from a previously uncharacterized subclade of glycoside hydrolase family 5 subfamily 7 (GH5_7) has been heterologously produced Pichia pastoris. Purified recombinant AtMan5-2 is glycosylated protein with an apparent molecular mass 50kDa, pH optimum 5.5-6.0 temperature 25°C. The enzyme exhibits high substrate affinity catalytic efficiency on mannan substrates main chains containing both glucose mannose units such as konjac glucomannan spruce galactoglucomannan. Product analysis manno-oligosaccharide hydrolysis shows requires at least six substrate-binding subsites. No transglycosylation activity for was detected present study. Our results demonstrate diversification function among members GH5_7 subfamily.
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