TY - JOUR
T1 - Characterization of the xylanolytic enzyme system of the extreme thermophilic anaerobic bacteria Thermotoga maritima, T. neapolitana, and T. thermarum
AU - Sunna, Anwar
AU - Puls, Jürgen
AU - Antranikian, Garabed
PY - 1997/11
Y1 - 1997/11
N2 - The extreme thermophilic anaerobic bacteria Thermotoga maritima, T. neapolitana, and T. thermarum when grown on xylan produce extremely thermoactive xylanases, β-xylosidases and α-arabinofuranosidases. Most of these enzymes are active over a broad temperature and pH range, namely between 40 and 110°C and pH 4 to 9. The xylanases are active towards soluble, as well as insoluble xylan. Unlike the enzyme system of T. maritima and T. thermarum, the xylanase activity of T. neapolitana is activated (up to 211%) in the presence of Ca2+, Mg2+, Co2+, and Mn2+. The xylanolytic enzyme system of T. thermarum is inactive towards cellulose. Xylan hydrolysis experiments indicate the presence of endoxylanases in the enzyme preparation of all strains investigated, with the main products being xylobiose, xylotriose, and larger xylooligosaccharides.
AB - The extreme thermophilic anaerobic bacteria Thermotoga maritima, T. neapolitana, and T. thermarum when grown on xylan produce extremely thermoactive xylanases, β-xylosidases and α-arabinofuranosidases. Most of these enzymes are active over a broad temperature and pH range, namely between 40 and 110°C and pH 4 to 9. The xylanases are active towards soluble, as well as insoluble xylan. Unlike the enzyme system of T. maritima and T. thermarum, the xylanase activity of T. neapolitana is activated (up to 211%) in the presence of Ca2+, Mg2+, Co2+, and Mn2+. The xylanolytic enzyme system of T. thermarum is inactive towards cellulose. Xylan hydrolysis experiments indicate the presence of endoxylanases in the enzyme preparation of all strains investigated, with the main products being xylobiose, xylotriose, and larger xylooligosaccharides.
UR - http://www.scopus.com/inward/record.url?scp=0031280411&partnerID=8YFLogxK
U2 - 10.1016/S0300-9629(97)00006-6
DO - 10.1016/S0300-9629(97)00006-6
M3 - Article
AN - SCOPUS:0031280411
SN - 0300-9629
VL - 118
SP - 453
EP - 461
JO - Comparative Biochemistry and Physiology - A Physiology
JF - Comparative Biochemistry and Physiology - A Physiology
IS - 3
ER -