02062nas a2200265   4500008004100000022001400041245021000055210006900265260009500334300001200429490000800441520103600449653000601485653003701491653003301528653001301561653001101574653000901585653000901594653002401603653000901627100002101636700001401657856012501671       2006                        eng d  a0006-291X00aConformation and microenvironment of the active site of a low molecular weight 1,4-beta-D-glucan glucanohydrolase from an alkalothermophilic thermomonospora sp.: involvement of lysine and cysteine residues0 aConformation and microenvironment of the active site of a low mo  a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcAUG  a428-4320 v3473 a<p>Conformation and microenvironment at the active site of 1,4-beta-D-glucan glucanohydrolase was probed with fluorescent chemo-affinity labeling using o-phthalaldehyde. OPTA has been known to form a fluorescent isoindole derivative by cross-linking the proximal thiol and amino groups of cysteine and lysine. Modification of lysine of the enzyme by TNBS and of cysteine residue by PHMB abolished the ability of the enzyme to form an isoindole derivative with OPTA. Kinetic analysis of the TNBS and PHMB-modified enzyme suggested the presence of essential lysine and cysteine residues, respectively, at the active site of the enzyme. The substrate protection of the enzyme with carboxymethylcellulose (CMC) confirmed the involvement of lysine and cysteine residues in the active site of the enzyme. Multiple sequence alignment of peptides obtained by tryptic digestion of the enzyme showed cysteine is one of the conserved amino acids corroborating the chemical modification studies. (c) 2006 Elsevier Inc. All rights reserved.</p>10a110a4-beta-D-glucan glucanohydrolase10aactive site microenvironment10aCysteine10alysine10aOPTA10aPHMB10aThermomonospora sp.10aTNBS1 aJagtap, Sharmili1 aRao, Mala  uhttps://library.ncl.res.in/content/conformation-and-microenvironment-active-site-low-molecular-weight-14-beta-d-glucan-002381nas a2200265   4500008004100000022001400041245014900055210006900204260009900273300001000372490000700382520140800389653000601797653000801803653003301811653002301844653001201867653001501879653001401894653002501908100001901933700001801952700001401970856013101984       2013                        eng d  a0964-830500aApproach towards biocatalytic valorisation of barley beta-glucan for bioethanol production using 1,3-1,4 beta-glucanase and thermotolerant yeast0 aApproach towards biocatalytic valorisation of barley betaglucan   aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcAUG  a81-860 v823 a<p>The exploitation of renewable resource containing polymers other than cellulose and hemicellulose are critically important for the feasibility of biofuel production. The potential of 1,3-1,4 glucan 4-gluconohydrolyase mediated saccharification of barley beta-glucan (BG) was investigated for ethanol production using thermotolerant Saccharomyces sp. A maximum hydrolysis of 71% was obtained in 24 h using in-house produced 1,3-1,4 beta-glucanase from an alkalothermophilic Thermomonospora sp. whereas the hydrolysis was 100% with Accellerase (TM) 1000. The synergistic effect of beta-glucosidase and 1,3-1,4 beta-glucanase was demonstrated by the exogenous addition of beta-glucosidase to Thermomonospora 1,3-1,4 beta-glucanase which resulted in complete hydrolysis of BG. The hydrolysates of BG obtained using Accellerase or a cocktail of Thermomonospora 1,3-1,4 beta-glucanase and beta-glucosidase when fermented with free cells of Saccharomyces at 40 degrees C produced an ethanol yield of 0.44 g g(-1) and 0.46 g g(-1) respectively and when fermented with immobilized cells produced a yield of 0.49 g g(-1). The Ca-alginate immobilized yeast cells were reused nine times at 40 degrees C with 100% fermentation efficiency. The economics of barley-to-fuel ethanol program will ameliorate if in addition to barley starch, beta-glucan is also utilized. (c) 2013 Elsevier Ltd. All rights reserved.</p>10a110a3-110a4 Glucan 4-gluconohydrolyase10aBarley beta-glucan10aEthanol10aHydrolysis10aSynergism10aThermotolerant yeast1 aDivate, Rupesh1 aMenon, Vishnu1 aRao, Mala  uhttps://library.ncl.res.in/content/approach-towards-biocatalytic-valorisation-barley-beta-glucan-bioethanol-production-using-0