01996nas a2200241   4500008004100000022001400041245019800055210006900253260009500322300001200417490000800429520105500437653001401492653000801506653000901514653002301523653002401546653001001570653001301580100002101593700001101614856012901625       2005                        eng d  a0006-291X00aPurification and properties of a low molecular weight 1,4-beta-D-glucan glucohydrolase having one active site for carboxymethyl cellulose and xylan from an alkalothermophilic Thermomonospora sp0 aPurification and properties of a low molecular weight 14betaDglu  a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcAPR  a111-1160 v3293 a<p>A low molecular weight 1,4-beta-D-glucan glucohydrolase from an extracellular culture filtrate of Thermomonospora sp. was purified to homogeneity. The molecular weight of the purified enzyme was 14.2 kDa by MALDI-TOF analysis and is in agreement with SDS-PAGE and gel filtration chromatography. The purified enzyme exhibited both endocarboxymethyl cellulase and endoxylanase activities. A kinetic method was employed to study the active site of the enzyme that hydrolyzes both carboxymethyl cellulose and xylan. The experimental data coincide well with the theoretical values calculated for the case of a single active site. Conformation and microenvironment at the active site was probed with fluorescent chemo-affinity labeling using o-phthalaidehyde as the chemical initiator. Formation of isoindole derivative resulted in complete inactivation of the enzyme to hydrolyze both xylan and CMC as judged by fluorescence studies corroborating a single active site for the hydrolysis of xylan and CMC. (C) 2005 Elsevier Inc. All rights reserved.</p>10aCellulase10aCMC10aOPTA10asingle active site10aThermomonospora sp.10axylan10aXylanase1 aJagtap, Sharmili1 aRao, M  uhttps://library.ncl.res.in/content/purification-and-properties-low-molecular-weight-14-beta-d-glucan-glucohydrolase-having-0