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- W2160091357 abstract "Three extracellular �. -mannosidases (EC 3.2.1.24) were purified from the digestive fluid of oil palm weevil larvae, Rhynchophorus palmarum (L.) and characterized in order to explore their potential for biotechnological application. Three steps procedure includ- ing size exclusion, anion exchange and hydrophobic interaction chromatography were used. The enzymes named RplM1, RplM2 and RplM3 had native molecular weights of approximately 125, 72 and 111 kDa, respectively and functioned as dimeric (RplM1) and monomeric (RplM2 and RplM3) structures. The three �. -mannosidases displayed acidic and mesophilic activities by using para-nitrophenyl-�. -D-Mannopyranoside as substrate. Apparent KM values were found to be 0.13, 0.22 and 0.16 mM for RplM1, RplM2 and RplM3, respectively. Ba 2+ , Ca 2+ , Mg 2+ , Zn 2+ and ethylene diamine tetra acetic acid (EDTA) had no effect on the three enzyme activities whereas detergents and reducing agents were inhibitors. RplM1, RplM2 and RplM3 were more sensitive to swainsonine and cleaved �. -1,2; �. -1,3 and �. -1,6 linked mannobioses. These characteristics prompted us to categorize them as catabolic �. -mannosidases. Thus, they would help in the larval oil palm weevil nutrition allowing digestion by the removal of mannose residues in the beetle's diet. Also, these enzymes could find potential application in biological, biochemical and pharma- ceutical area." @default.
- W2160091357 created "2016-06-24" @default.
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- W2160091357 date "2009-01-01" @default.
- W2160091357 modified "2023-10-18" @default.
- W2160091357 title "Biochemical properties of extracellular α-mannosidases from the digestive fluid of Rhynchophorus palmarum larvae." @default.
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