TY - JOUR
T1 - A bifunctional endoglucanase/endoxylanase from Cellulomonas flavigena with potential use in industrial processes at different pH
AU - Pérez-Avalos, Odilia
AU - Sánchez-Herrera, Leticia M.
AU - Salgado, Luis M.
AU - Ponce-Noyola, Teresa
N1 - Funding Information:
This work was supported by Consejo Nacional de Ciencia y Tecnología-México (45678-Z). The authors thank the W. M. Keck Biomedical Mass Spectrometry Laboratory UVHS for sequencing the protein and Martha Mercado-Morales for technical assistance.
PY - 2008/7
Y1 - 2008/7
N2 - Cellulomonas flavigena CDBB-531 was found to secrete a bifunctional cellulase/xylanase with a molecular mass of 49 kDa and pI 4.3. This enzyme was active on Remazol brilliant blue-carboxymethylcellulose (RBB-CMC) and Remazol brilliant blue-xylan (RBB-X). Based on thin-layer chromatographic analysis of the degradation products, the cellulase activity produced glucose, cellobiose, cellotriose, and cellotetraose from CMC as the substrate. When xylan from birchwood was used, end products were xylose, arabinose, and xylobiose. The bifunctional enzyme showed a pH optimum of 6 for cellulase activity and 9 for xylanase activity, which pointed out that this enzyme had separate sites for each activity. In both cases, the apparent optimum temperature was 50°C. The predicted amino acid sequence of purified protein showed similarity with the catalytic domain of several glycosyl hydrolases of family 10.
AB - Cellulomonas flavigena CDBB-531 was found to secrete a bifunctional cellulase/xylanase with a molecular mass of 49 kDa and pI 4.3. This enzyme was active on Remazol brilliant blue-carboxymethylcellulose (RBB-CMC) and Remazol brilliant blue-xylan (RBB-X). Based on thin-layer chromatographic analysis of the degradation products, the cellulase activity produced glucose, cellobiose, cellotriose, and cellotetraose from CMC as the substrate. When xylan from birchwood was used, end products were xylose, arabinose, and xylobiose. The bifunctional enzyme showed a pH optimum of 6 for cellulase activity and 9 for xylanase activity, which pointed out that this enzyme had separate sites for each activity. In both cases, the apparent optimum temperature was 50°C. The predicted amino acid sequence of purified protein showed similarity with the catalytic domain of several glycosyl hydrolases of family 10.
UR - http://www.scopus.com/inward/record.url?scp=44049094301&partnerID=8YFLogxK
U2 - 10.1007/s00284-008-9149-1
DO - 10.1007/s00284-008-9149-1
M3 - Artículo
SN - 0343-8651
VL - 57
SP - 39
EP - 44
JO - Current Microbiology
JF - Current Microbiology
IS - 1
ER -