title: Transglycosylation catalyzed by a Penicillium chrysogenum exo-1,5-alpha-L-arabinanase.
abstract: Penicillium chrysogenum exo-arabinanase (Abnx), which releases arabinobiose from the nonreducing terminus of alpha-1,5-L-arabinan, was found to possess trans-arabinobiosylation activity on various acceptors, such as aliphatic alcohols, sugars, and sugar alcohols. Abnx was found to prefer primary hydroxyl groups in polyhydric alcohols as acceptors over primary hydroxyl groups in monohydric alcohols. Among the 21 different compounds tested, glycerol was the best acceptor for the enzyme. The transfer product of glycerol was identified as O-alpha-L-arabinosyl-(1-->5)-O-alpha-L-arabinosyl-(1-->1)-glycerol on the basis of the spectral data, fast atom bombardment-mass and 1H- and 13C-NMR. Unlike endo-arabinanases, Abnx catalyzed the hydrolysis of linear arabinan without inverting the anomeric configuration.
authors.affiliation: Laboratory of Fermentation Chemistry, Division of Applied Biochemistry, Graduate School of Agriculture and Biological Science, Osaka Prefecture University, Gakuen-cho 1-1, Sakai, Osaka 599-8531, Japan.
authors.forename: Tatsuji
authors.initials: T
authors.lastname: Sakamoto
authors.forename: Tomoyuki
authors.initials: T
authors.lastname: Fujita
authors.forename: Haruhiko
authors.initials: H
authors.lastname: Kawasaki
mesh_terms: D005656:Fungal Proteins / Q000378:metabolism*; D005990:Glycerol / Q000737:chemistry / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006031:Glycosylation; D006863:Hydrogen-Ion Concentration; D015394:Molecular Structure; D010408:Penicillium chrysogenum / Q000201:enzymology*; D011134:Polysaccharides / Q000378:metabolism; D013696:Temperature
chemical_list: D005656:Fungal Proteins; D011134:Polysaccharides; C030080:araban; D006026:Glycoside Hydrolases; C434938:exo-alpha-L-arabinanase; D005990:Glycerol