TY - JOUR
AU1 - Thiagarajan, S.
AU2 - Jeya, M.
AU3 - Gunasekaran, P.
AB - A high molecular weight endoxylanase (XylF2) from the solid state culture of Aspergillus fumigatus MKU1 was purified to homogeneity by a combination of tube gel electrophoresis and electroelution methods. The purity was demonstrated by SDS-PAGE and the molecular mass of the XylF2 was found to be 66 kDa. The optimal pH and temperature for activity were 5.0 and 90 °C, respectively. The apparent K
m and V
max values of XylF2 with oat spelt xylan as substrate were 1.6 mg/ml and 3.25 mmol/min/mg protein respectively. The enzyme showed high activity towards oat spelt xylan while negligible activity was observed on carboxymethylcellulose. The activity of XylF2 was strongly inhibited by Hg2+, Ni2+, Zn2+, SDS and N-bromosuccinimide and stimulated by l-cysteine and iodoacetamide. The hydrolysis of oat spelt xylan by XylF2 released only xylo-oligosaccharides.
TI - Purification and characterization of a high molecular weight endoxylanase from the solid-state culture of an alkali-tolerant Aspergillus fumigatus MKU ...
JF - World Journal of Microbiology and Biotechnology
DO - 10.1007/s11274-005-9061-9
DA - 2005-11-25
UR - https://www.deepdyve.com/lp/springer-journals/purification-and-characterization-of-a-high-molecular-weight-90LT0nyPpw
SP - 487
EP - 492
VL - 22
IS - 5
DP - DeepDyve
ER -