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- W1996295066 abstract "An α-L-arabinofuranosidase gene of Aspergillus oryzae was expressed in Pichia pastoris. The re-combinant enzyme released L-arabinose from arabinose-containing polysaccharides such as lupin pectic galactan, corn hull arabinoxylan, sugar beet arabinan, and potato pectic galactan. The enzyme displayed an optimum activity at 45°C and pH 4.0. The enzyme was slowly inactivated above pH 6.0 and below pH 3.0, and was stable at temperatures up to 40°C. On the other hand, a putative endo-arabinanase gene of Strep-tomyces coelicolor was cloned and expressed in Escherichia coli. The recombinant enzyme hydrolyzed linear arabinans and produced α-1,5-arabinooligosaccharides. The enzyme displayed an optimum activity at 45°C and pH 6.0. The enzyme was slowly inactivated above pH 10.0 and below pH 4.0, and it was stable at temperatures up to 35°C. Synergisms between the α-L-arabinofuranosidase and the endo-arabinanase for the degradation of arabinan and debranched arabinan were observed. The hydrolysis was most efficient when α-L-arabinofuranosidase and endo-arabinanase were in a ratio of 95 : 5." @default.
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- W1996295066 date "2006-01-01" @default.
- W1996295066 modified "2023-10-16" @default.
- W1996295066 title "Synergy Between an .ALPHA.-L-Arabinofuranosidase from Aspergillus oryzae and an Endo-Arabinanase from Streptomyces coelicolor for Degradation of Arabinan" @default.
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- W1996295066 doi "https://doi.org/10.3136/fstr.12.43" @default.
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