β-D-xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43

被引:27
作者
Jordan, Douglas B.
Li, Xin-Liang
Dunlap, Christopher A.
Whitehead, Terence R.
Cotta, Michael A.
机构
[1] USDA ARS, Natl Ctr Agr Utilizat Res, Fermentat Biotechnol Res Unit, Peoria, IL 61604 USA
[2] USDA ARS, Natl Ctr Agr Utilizat Res, Crop Bioprotect Res Unit, Peoria, IL 60604 USA
关键词
fuel ethanol; glycohydrolase; hemicellulose; protein stability; saccharification; arabinofuranosidase; inhibitors; catalysis;
D O I
10.1007/s12010-007-9042-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
beta-D-Xylosidase from the ruminal. anaerobic bacterium, Selenomonas ruminantium (SXA), catalyzes hydrolysis of beta-1,4-xylooligosacharides and has potential utility in saccharification processes. The enzyme, heterologously produced in Escherichia coli and purified to homogeneity, has an isoelectric point of approx 4.4, an intact N terminus, and a Stokes radius that defines a homotetramer. SXA denatures between pH 4.0 and 4.3 at 25 degrees C and between 50 and 60 degrees C at pH 5.3. Following heat or acid treatment, partially inactivated SXA exhibits lower k(cat) values, but similar K-m values as untreated SXA. D-Glucose and D-xylose protect SXA from inactivation at high temperature and low pH.
引用
收藏
页码:93 / 104
页数:12
相关论文
共 16 条
[1]   UTILIZATION OF XYLOOLIGOSACCHARIDES BY SELECTED RUMINAL BACTERIA [J].
COTTA, MA .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1993, 59 (11) :3557-3563
[2]   Xylooligosaccharide utilization by the ruminal anaerobic bacterium Selenomonas ruminantium [J].
Cotta, MA ;
Whitehead, TR .
CURRENT MICROBIOLOGY, 1998, 36 (04) :183-189
[3]   Calculation of hydrodynamic properties of globular proteins from their atomic-level structure [J].
de la Torre, JG ;
Huertas, ML ;
Carrasco, B .
BIOPHYSICAL JOURNAL, 2000, 78 (02) :719-730
[4]   CALCULATION OF PROTEIN EXTINCTION COEFFICIENTS FROM AMINO-ACID SEQUENCE DATA [J].
GILL, SC ;
VONHIPPEL, PH .
ANALYTICAL BIOCHEMISTRY, 1989, 182 (02) :319-326
[5]   SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling [J].
Guex, N ;
Peitsch, MC .
ELECTROPHORESIS, 1997, 18 (15) :2714-2723
[6]   The beta-D-xylosidase of Trichoderma reesei is a multifunctional beta-D-xylan xylohydrolase [J].
Herrmann, MC ;
Vrsanska, M ;
Jurickova, M ;
Hirsch, J ;
Biely, P ;
Kubicek, CP .
BIOCHEMICAL JOURNAL, 1997, 321 :375-381
[7]   KINETICS OF ALPHA-CHYMOTRYPSIN-CATALYZED HYDROLYSIS OF P-NITROPHENYL ACETATE [J].
KEZDY, FJ ;
BENDER, ML .
BIOCHEMISTRY, 1962, 1 (06) :1097-&
[8]  
MARSHALL PJ, 1983, BIOCHEM J, V215, P67, DOI 10.1042/bj2150067
[9]   Cellvibrio japonicus α-L-arabinanase 43A has a novel five-blade β-propeller fold [J].
Nurizzo, D ;
Turkenburg, JP ;
Charnock, SJ ;
Roberts, SM ;
Dodson, EJ ;
McKie, VA ;
Taylor, EJ ;
Gilbert, HJ ;
Davies, GJ .
NATURE STRUCTURAL BIOLOGY, 2002, 9 (09) :665-668
[10]   Hemicellulose bioconversion [J].
Saha, BC .
JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY, 2003, 30 (05) :279-291