02367nas a2200241 4500008004100000022001400041245016600055210006900221260007300290300001200363490000800375520144300383653001201826653002201838653001501860653002701875653002501902653001801927100001801945700001801963700001401981856013001995 2010 eng d a0168-165600aEnzymatic hydrolysis and ethanol production using xyloglucanase and debaromyces hansenii from tamarind kernel powder: galactoxyloglucan predominant hemicellulose0 aEnzymatic hydrolysis and ethanol production using xyloglucanase  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcAUG a233-2390 v1483 a

The hydrolysis and ethanol production from tamarind kernel powder (TKP), a rich source of galactoxyloglucan (GXG) was investigated for the first time using xyloglucanase and thermotolerant Debaromyces hansenii. The acid hydrolysis of TKP with 2N H(2)SO(4) at 120 degrees C for 30 min yielded an overall saccharification of 94% based on the total available carbohydrate content and further fermentation at 40 degrees C with thermotolerant D hansenii produced an ethanol yield of 0.35 g/g. A maximum hydrolysis of 55 and 78% for GXG was obtained in 48 h at 50 degrees C using Thermomonospora xyloglucanase (TXy) and accellerase (TM) 1000, respectively. The synergistic effect of beta-galactosidase and xyloglucanase was demonstrated by the exogenous addition of beta-galactosidase to TXy which improved the overall hydrolysis of GXG by 30%. The rate of hydrolysis of GXG with TXy and accellerase was increased by 15-20% in the presence of chemical surfactants (tween 80 and toluene) or protein additive (BSA). The fermentation of enzymatic hydrolysates of GXG by TXy and accellerase with free cells at 40 degrees C produced an ethanol yield of 0.39 and 0.41 g/g whereas with immobilized cells produced 0.45 and 0.43 g/g, respectively, with a theoretical conversion efficiencies of 78-88%. The immobilized yeast cells were reused six times at 40 degrees C with 100% fermentation efficiency. (C) 2010 Elsevier B.V. All rights reserved.

10aEthanol10aGalactoxyloglucan10aHydrolysis10aTamarind kernel powder10aThermotolerant yeast10aXyloglucanase1 aMenon, Vishnu1 aPrakash, Gyan1 aRao, Mala uhttps://library.ncl.res.in/content/enzymatic-hydrolysis-and-ethanol-production-using-xyloglucanase-and-debaromyces-hansenii-002277nas a2200229 4500008004100000022001400041245011800055210006900173260010700242300001200349490000700361520138000368653004301748653003401791653001701825653001701842653001801859100001601877700001801893700001401911856012201925 2012 eng d a1431-065100aBiochemical characterization of a novel thermostable xyloglucanase from an alkalothermophilic thermomonospora sp.0 aBiochemical characterization of a novel thermostable xyloglucana aCHIYODA FIRST BLDG EAST, 3-8-1 NISHI-KANDA, CHIYODA-KU, TOKYO, 101-0065, JAPANbSPRINGER JAPAN KKcJAN a135-1460 v163 a

Xyloglucanase from an extracellular culture filtrate of alkalothermophilic Thermomonospora sp. was purified to homogeneity with a molecular weight of 144 kDa as determined by SDS-PAGE and exhibited specificity towards xyloglucan with apparent K (m) of 1.67 mg/ml. The enzyme was active at a broad range of pH (5-8) and temperatures (40-80A degrees C). The optimum pH and temperature were 7 and 70A degrees C, respectively. The enzyme retained 100% activity at 50A degrees C for 60 h with half-lives of 14 h, 6 h and 7 min at 60, 70 and 80A degrees C, respectively. The kinetics of thermal denaturation revealed that the inactivation at 80A degrees C is due to unfolding of the enzyme as evidenced by the distinct red shift in the wavelength maximum of the fluorescence profile. Xyloglucanase activity was positively modulated in the presence of Zn2+, K+, cysteine, beta-mercaptoethanol and polyols. Thermostability was enhanced in the presence of additives (polyols and glycine) at 80A degrees C. A hydrolysis of 55% for galactoxyloglucan (GXG) from tamarind kernel powder (TKP) was obtained in 12 h at 60A degrees C and 6 h at 70A degrees C using thermostable xyloglucanases, favouring a reduction in process time and enzyme dosage. The enzyme was stable in the presence of commercial detergents (Ariel), indicating its potential as an additive to laundry detergents.

10aAlkalothermophilic Thermomonospora sp.10aBiotechnological applications10aPurification10aThermostable10aXyloglucanase1 aPol, Dipali1 aMenon, Vishnu1 aRao, Mala uhttps://library.ncl.res.in/content/biochemical-characterization-novel-thermostable-xyloglucanase-alkalothermophilic-001772nas a2200217 4500008004100000022001400041245014500055210006900200260009900269300001200368490000800380520088800388653002201276653002701298653002101325653002701346653001801373100001801391700001401409856013101423 2012 eng d a0960-852400aInhibition of xyloglucanase from an alkalothermophilic thermomonospora sp by a peptidic aspartic protease inhibitor from Penicillium sp VM240 aInhibition of xyloglucanase from an alkalothermophilic thermomon aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcNOV a390-3990 v1233 a

A bifunctional inhibitor from Penicilliurn sp VM24 causing inactivation of xyloglucanase from Thermomonospora sp and an aspartic protease from Aspergillus saitoi was identified. Steady state kinetics studies of xyloglucanase and the inhibitor revealed an irreversible, non-competitive, two-step inhibition mechanism with IC50 and K-i; values of 780 and 500 nM respectively. The interaction of o-phthalaldehyde (OPTA)-labeled xyloglucanase with the inhibitor revealed that the inhibitor binds to the active site of the enzyme. Far- and near-UV spectrophotometric analysis suggests that the conformational changes induced in xyloglucanase by the inhibitor may be due to irreversible denaturation of enzyme. The bifunctional inhibitor may have potential as a biocontrol agent for the protection of plants against phytopathogenic fungi. (C) 2012 Elsevier Ltd. All rights reserved.

10aAspartic protease10aBifunctional inhibitor10aBiocontrol agent10aInactivation mechanism10aXyloglucanase1 aMenon, Vishnu1 aRao, Mala uhttps://library.ncl.res.in/content/inhibition-xyloglucanase-alkalothermophilic-thermomonospora-sp-peptidic-aspartic-protease-0