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- W350678604 abstract "Purified Aspergillus ficuum endoinulinase (Afi-Endo) previously produced by a recombinant Saccharomyces cerevisiae was heterogeneous in its molecular weight, ranging from 84 to 130 kDa. When an N-linked endoglycosylase, Endo H, was treated to the heterogeneous Afi-Endo, the recombinant enzyme showed a single band of 66 kDa on SDS-PAGE, suggesting that the recombinant enzyme is hyperglycosylated. Hyperglycosylated enzyme had higher optimal temperature and thermal stability than Afi-Endo produced from A. ficuum. Specific activities of hyperglycosylated and deglycosylated Afi-Endo were equal. These results indicate that hyperglycosylation increases optimal temperature and thermal stability of Afi-Endo, but does not affect specific activity. Hyperglycosylated Afi-Endo has more advantages than Afi-Endo produced from A. fucuum for industrial applications." @default.
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- W350678604 date "2003-01-01" @default.
- W350678604 modified "2023-09-28" @default.
- W350678604 title "Hyperglycosylation of Aspergillus ficuum Endoinulinase Increases the Optimal Temperature and Thermal Stability" @default.
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