02277nas 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<p>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.</p>10aAlkalothermophilic Thermomonospora sp.10aBiotechnological applications10aPurification10aThermostable10aXyloglucanase1 aPol, Dipali1 aMenon, Vishnu1 aRao, Mala  uhttps://library.ncl.res.in/content/biochemical-characterization-novel-thermostable-xyloglucanase-alkalothermophilic-002491nas a2200253   4500008004100000022001400041245010500055210006900160260007900229300001200308490000800320520154900328653002101877653002101898653003301919653001701952653002001969100002101989700002702010700002602037700001402063700002802077856013202105       2012                        eng d  a0273-228900aProduction, purification, and characterization of a beta-glucosidase of penicillium funiculosum NCL10 aProduction purification and characterization of a betaglucosidas  a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcJUL  a959-9720 v1673 a<p>Penicillium funiculosum NCL1, a filamentous fungus, produced significantly higher levels of beta-glucosidase. The effect of initial pH, incubation temperature, and different carbon sources on extracellular beta-glucosidase production was studied in submerged fermentation. At 30 A degrees C with initial pH 5.0, enzyme production was increased by 48-fold upon induction with paper mill waste, as compared to commercial cellulose powder. In zymogram analysis, four isoforms of beta-glucosidases were observed with wheat bran whereas a minimum of one isoform was observed with other carbon sources. A major beta-glucosidase (Bgl3A) with the apparent molecular weight of similar to 120 kDa, induced by paper mill waste, was purified 19-fold to homogeneity, with a specific activity of 1,796 U/mg. Bgl3A was a monomeric glycoprotein with 29% of neutral carbohydrate content. It showed optimum activity at pH 4.0 and 5.0, optimum temperature at 60 A degrees C, and exhibited a half-life of 1 h at 60 A degrees C. K (m) of Bgl3A was found to be 0.057 mM with p-nitrophenyl beta-d-glucoside and V (max) was 1,920 U/mg. The purified enzyme exhibited glucose tolerance with a K (i) of 1.5 mM. Bgl3A readily hydrolyzed glucosides with beta-linkage. Bgl3A activity was enhanced (156%) by Zn2+ and was not affected by other metal cations and reagents. The supplementation of Bgl3A (5 U/mg) with Trichoderma reesei cellulase complex (5 FPU/mg) resulted in about 70% of enhanced glucose production, which emphasizes the industrial importance of Bgl3A.</p>10abeta-Glucosidase10aPaper mill waste10aPenicillium funiculosum NCL110aPurification10aThermostability1 aRamani, Gurusamy1 aMeera, Balasubramanian1 aVanitha, Chinnathambi1 aRao, Mala1 aGunasekaran, Paramasamy  uhttps://library.ncl.res.in/content/production-purification-and-characterization-beta-glucosidase-penicillium-funiculosum-ncl1-002494nas a2200229   4500008004100000022001400041245010100055210006900156260011000225300001200335490000700347520160200354653002701956653002801983653001802011653003302029653001702062100001602079700002502095700001402120856013002134       2012                        eng d  a0301-120800aPurification and biochemical characterization of endoglucanase from Penicillium pinophilum MS 200 aPurification and biochemical characterization of endoglucanase f  aDR K S KRISHNAN MARG, PUSA CAMPUS, NEW DELHI 110 012, INDIAbNATL INST SCIENCE COMMUNICATION-NISCAIRcJUN  a189-1940 v493 a<p>Cellulases find increasing prominence in sustainable production of fuel and feedstock from lignocellulosic biomass. The purification and biochemical characterization of individual components of cellulase complex is important to understand the mechanism of their action for the solubilization of crystalline cellulose. In this study, an extra-cellular endoglucanase isolated from culture filtrate of Penicillium pinophilum MS 20 was purified to homogeneity by ammonium sulphate precipitation, ion-exchange chromatography and gel filtration. The purified endoglucanase (specific activity 69 U/mg) was a monomeric protein with molecular mass of 42 kDa, as determined by SDS-PAGE. The endoglucanase was active over a broad range of pH (4-7) with maximum activity at pH 5 and showed optimum temperature of 50 degrees C. It retained 100% activity at 50 degrees C for 6 h and half- lives of 4 h and 3 h at 60 degrees C and 70 degrees C, respectively. The kinetic constants for the endoglucanase determined with carboxymethyl cellulose as substrate were V-max of 72.5 U/mg and apparent K-m of 4.8 mg/ml. The enzyme also showed moderate activity towards H3PO4 swollen cellulose and p-nitrophenyl beta-D-glucoside, but no activity towards filter paper, Avicel and oat spelt xylan. The activity was positively modulated by 47, 32 and 25% in the presence of Co2+, Zn2+ and Mg2+, respectively to the reaction mixture. The wide pH stability (4-7) and temperature stability up to 50 degrees C of endoglucanase makes the enzyme suitable for use in cellulose saccharification at moderate temperature and pH.</p>10aBiochemical properties10aCarboxymethyl cellulose10aEndoglucanase10aPenicillium pinophilum MS 2010aPurification1 aPol, Dipali1 aLaxman, Ryali, Seeta1 aRao, Mala  uhttps://library.ncl.res.in/content/purification-and-biochemical-characterization-endoglucanase-penicillium-pinophilum-ms-20-0