S. Yosida et al., PURIFICATION, PROPERTIES, AND N-TERMINAL AMINO-ACID-SEQUENCES OF GUARGUM-DEGRADING ENZYME FROM BACILLUS-CIRCULANS K-1, Bioscience, biotechnology, and biochemistry, 61(2), 1997, pp. 251-255
A guar gum-degrading enzyme of the newly isolated Bacillus circulans K
-1 was purified to an electrophoretically homogeneous state, The molec
ular weight of the purified enzyme was 62,000 by SDS-PAGE, The purifie
d enzyme was separated into at least six isozymes by isoelectric focus
ing and the pI of these isozymes were 5.4, 5.5, 5.6, 5.8, 6.0, and 6.2
, respectively, The N-terminal amino acid sequences of the typical thr
ee of these proteins were all the same, s-Leu-Leu-Asp-Ala-Thr-Gly-Gln-
Pro-Phe-Val-Met-Arg. The enzyme was most active at pH 6.9 and at 64 de
grees C, The enzyme was activated slightly by Al3+ and inhibited stron
gly by Sn2+ and Zn2+, N-bromosuccinimide, 2-mercaptoethanol, and ethyl
enediamine-tetraacetic acid.