Characterization of a novel polyphenol-specific oligoxyloside transfer reaction by a family 11 xylanase from Bacillus sp. KT12.
A culture filtrate of Bacillus sp. KT12 was used to prepare polyphenyl beta-oligoxylosides from xylan and polyphenols in a one-step reaction. One oligoxyloside transfer enzyme was purified from multiple xylanolytic enzymes in the culture filtrate. N-terminal amino acid sequence determination classified the enzyme as a glycosyl hydrolase family 11 (endo-xylanase). The xylanolytic enzyme activities could be markedly altered; its hydrolytic activity was almost entirely inhibited at acidic pH, whereas near constant transxylosylation activity was observed at pH 4-11. Further, metal ions activated transxylosylation and almost completely inhibited hydrolysis. The enzyme specifically induced a beta-xylosyl transfer reaction to acceptor molecules, such as divalent and trivalent phenolic hydroxyl groups, and displayed no activity toward alcoholic compounds. The Bacillus sp. KT12 xylanolytic enzyme was a suitable enzyme for the synthesis of polyphenyl beta-oligoxylosides.
Chiku
Kazuhiro
K
Department of Advanced Bioresources Science, Graduate School of Science and Technology, Chiba University, Chiba, Japan. chiku06UD7204@graduate.chiba-u.jp
Uzawa
Jun
J
Seki
Hiroko
H
Amachi
Seigo
S
Fujii
Takaaki
T
Shinoyama
Hirofumi
H
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D005419:Flavonoids; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010636:Phenols; D059808:Polyphenols; D013696:Temperature; D043325:Xylan Endo-1,3-beta-Xylosidase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D005419:Flavonoids; D010636:Phenols; D059808:Polyphenols; D043325:Xylan Endo-1,3-beta-Xylosidase