T. Nishimura et al., PURIFICATION AND SOME PROPERTIES OF ALPHA-AMYLASE FROM BACILLUS-SUBTILIS X-23 THAT GLUCOSYLATES PHENOLIC-COMPOUNDS SUCH AS HYDROQUINONE, Journal of fermentation and bioengineering, 78(1), 1994, pp. 31-36
Six hundred strains of soil microorganisms were screened for the produ
ction of hydroquinone glucosylating enzyme (HGE). One of these strains
, Bacillus subtilis strain X-23, produced an enzyme that glucosylated
hydroquinone in the culture filtrate. The HGE was successively purifie
d by ammonium sulfate fractionation, and Q-Sepharose, Phenyl-Toyopearl
, and Superose 12 column chromatographies. The molecular weight was es
timated as 65 kDa by SDS-polyacrylamide gel electrophoresis, and 54 kD
a by gel filtration. Based on an analysis of the hydrolytic products f
rom soluble starch, HGE was considered to be a kind of alpha-amylase.
The structure of the hydroquinone glucoside produced by HGE was identi
fied as 4-hydroxyphenyl-O-alpha-D-glucopyranoside by alpha- and beta-g
lucosidase treatments, and H-1-NMR and C-13-NMR.