02773nas a2200301 4500008004100000022001400041245006400055210006400119260009900183300000900282490000700291520177900298653002802077653001402105653002302119653002502142653002902167653002202196653001302218100002202231700001802253700001502271700001402286700003002300700002002330700002302350856009802373 2005 eng d a0144-861700aEnzymatic hydrolysis of delignified bagasse polysaccharides0 aEnzymatic hydrolysis of delignified bagasse polysaccharides aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcOCT a6-100 v623 a

Sugarcane bagasse, consisting of cellulose, xylan, and lignin, was chemically treated to generate bagasse samples with continuously decreasing content of lignin. These bagasse samples were hydrolyzed by cellulase and xylanase enzymes, produced earlier by Penicillium janthinellum NCIM 1171 in the same bagasse polysaccharides production medium. The hydrolysis was carried out by using different concentrations of the enzymes at two different temperatures, 30 and 50 degrees C, taking hydrolysis of Avicel as control. It was found that while the maximum hydrolysis for Avicel was 70% that of some of the bagasse polysaccharides was as high as 95%. The products of hydrolysis were glucose, xylose, and arabinose, as confirmed by high pressure ion chromatography (HPIC). It is interesting to note that arabinose, which constitutes about 10% of the weight of bagasse xylan, could also be released easily by the enzymes. Also, the initial rates of hydrolysis was found to be much higher for the bagasse polysaccharides, and in some cases about 90% of the hydrolysis occurred within 20 h. Amongst all bagasse samples, the sample with (Kappa no. 1.2, lignin content 0.18%) gave the highest degree of hydrolysis at 50 degrees C. Even the bagasse polysaccharide with Kappa no. 16.8 (lignin content 2.5%) underwent greater extent of hydrolysis than Avicel. Apparently, the delignified bagasse medium appears to be a facile medium for the combined hydrolytic action of the cellulase and xylanase enzymes. Considering that sugarcane bagasse is a waste biomass material available in abundance annually, this methodology can be used to value-add to this biomass to produce sugars, which can be fermented to produce biofuels like ethanol. (C) 2005 Elsevier Ltd. All rights reserved.

10abagasse polysaccharides10aCellulase10achemical treatment10aEnzymatic hydrolysis10aPenicillium janthinellum10aSugarcane bagasse10aXylanase1 aAdsul, Mukund, G.1 aGhule, J., E.1 aShaikh, H.1 aSingh, R.1 aBastawade, Kulbhushan, B.1 aGokhale, D., V.1 aVarma, Anjanikumar uhttps://library.ncl.res.in/content/enzymatic-hydrolysis-delignified-bagasse-polysaccharides-002506nas a2200301 4500008004100000022001400041245010600055210006900161260009900230300001000329490000700339520143700346653002101783653002101804653003201825653002101857653002201878653002401900653002001924100001401944700001401958700002101972700002001993700003002013700002002043700002302063856011802086 2005 eng d a0144-861700aLignin-carbohydrate complexes from sugarcane bagasse: preparation, purification, and characterization0 aLignincarbohydrate complexes from sugarcane bagasse preparation  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcOCT a57-660 v623 a

Lignin-carbohydrate complexes were isolated from sugarcane bagasse by a process, which yielded sulfur-free lignins. These could be made carbohydrate-free, if necessary, by treatment with xylanase enzyme. A study of the preparation, purification, and characterization of such lignin-carbohydrate complexes, comparison with commercial lignin samples (wood based as well as bagasse based) and some other lignin derivatives was made by using a variety of analytical tools such as FTIR, HPLC at three different UV-wavelengths, GPC, thermal analysis and elemental analysis. The use of such a diverse range of lignin-carbohydrate complex samples enabled us to predict the sensitivity of the various analytical techniques for characterization of complex polymers containing carbohydrate moieties. Evidence for lignin-carbohydrate complex was detectable by FTIR as well as HPLC studies. Thermal analysis studies showed the crucial effect of carbohydrate groups, the content of aliphatic chains, and the sulfur content of the lignins. Generalized structures of lignin-carbohydrate complexes obtained from various sources using different preparation methods and chemical modifications are presented. This will aid the applications development effort with advantageously using lignins containing low levels of carbohydrate moieties as reactive sites as well as biodegradability inducing sites. (C) 2005 Elsevier Ltd. All rights reserved.

10abiodegradability10ahardwood lignins10alignin-carbohydrate complex10asoftwood lignins10aSugarcane bagasse10asulfur-free lignins10axylanase enzyme1 aSingh, R.1 aSingh, S.1 aTrimukhe, K., D.1 aPandare, K., V.1 aBastawade, Kulbhushan, B.1 aGokhale, D., V.1 aVarma, Anjanikumar uhttps://library.ncl.res.in/content/lignin-carbohydrate-complexes-sugarcane-bagasse-preparation-purification-and-002245nas a2200265 4500008004100000022001400041245012200055210006900177260008100246300001000327490000700337520126400344653002601608653002601634653002701660653003001687653001101717100001801728700001801746700001801764700003001782700002601812700002001838856012101858 2006 eng d a0266-825400aProduction of lactic acid and fructose from media with cane sugar using mutant of Lactobacillus delbrueckii NCIM 23650 aProduction of lactic acid and fructose from media with cane suga a9600 GARSINGTON RD, OXFORD OX4 2DQ, OXON, ENGLANDbBLACKWELL PUBLISHINGcJUL a53-570 v433 a

Aims: To examine the potential of Lactobacillus delbrueckii mutant, Uc-3 to produce lactic acid and fructose from sucrose-based media. Methods and Results: The mutant of L. delbrueckii NCIM 2365 was cultivated in shake flask containing hydrolysed cane sugar (sucrose)-based medium. The lactic acid yield and volumetric productivity with hydrolysed cane concentration up to 200 g l(-1) were in the range of 92-97% of the theoretical value and between 2.7 and 3.8 g l(-1) h(-1), respectively. The fructose fraction of the syrup produced was more than 95% when the total initial sugar concentration in the medium was higher (150-200 g l(-1)). There are no unwanted byproducts detected in the fermentation broth. Conclusions: We demonstrated that L. delbrueckii mutant Uc-3 was able to utilize glucose preferentially to produce lactic acid and fructose from hydrolysed cane sugar in batch fermentation process. Significance and Impact of the Study: These findings will be useful in the production of lactic acid and high fructose syrups using media with high concentrations of sucrose-based raw materials. This approach can lead to modification of the traditional fermentation processes to obtain value-added byproducts, attaining better process economics.

10afructose accumulation10ahydrolyzed cane sugar10alactic acid production10aLactobacillus delbrueckii10aMutant1 aPatil, S., S.1 aKadam, S., R.1 aPatil, S., S.1 aBastawade, Kulbhushan, B.1 aKhire, Jayant, Malhar1 aGokhale, D., V. uhttps://library.ncl.res.in/content/production-lactic-acid-and-fructose-media-cane-sugar-using-mutant-lactobacillus-002656nas a2200253 4500008004100000022001400041245014200055210006900197260009900266300001400365490000700379520163400386653002402020653004402044653001702088653002402105653002402129100001702153700002602170700002002196700003002216700002602246856013002272 2006 eng d a1359-511300aPurification, characterization and substrate specificity of thermostable alpha-galactosidase from Bacillus stearothermophilus (NCIM-5146)0 aPurification characterization and substrate specificity of therm aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcJUN a1311-13170 v413 a

An extracellular thermostable alpha-galactosidase from Bacillus stearothermophilus (NCIM-5146) has been purified to homogeneity by chromatographic step, using Phenyl Sepharose CL-4B column. The specific activity of the enzyme was increased approximately 389-fold, from 1.03 U/mg protein to 400 U/mg protein. The molecular mass of the purified enzyme as determined by SDS-PAGE and gel filtration was 79.9 and 165.9 kDa, respectively, suggesting dimeric nature. The purified alpha-galactosidase is a non-glycosylated protein with a pI of 4.9. The pH and temperature optima for the purified enzyme are 6.5-7.0 and 65 degrees C, respectively. The alpha-galactosidase is stable over a broad pH range (3-9) and its half-life of inactivation (t(1/2)) at 70 degrees C is 30 min. The partial N-terminal sequence of alpha-galactosidase showed remarkable homology (80% similarity) with earlier reported alpha-galactosidase from B. stearothermophilus NUB 3621. The secondary structure of the enzyme determined by circular dichroism (CD) spectroscopy exhibited alpha/beta class of protein and showed temperature induced conformational forms below and above the transition temperature. The purified enzyme showed biphasic Arrhenius plot with break point at 55 degrees C for pNPG and 50 degrees C for melibiose, raffinose and stachyose. The enzyme hydrolyzes alpha-1-3, alpha-1-4, and alpha-1-6 galactosidic linkages and not the beta-galactosidic linkages. Synthetic substrates pNPG and oNPG had lower K-m and higher K-cat as compare to natural substrates, melibiose, raffinose, and stachyose. (c) 2006 Elsevier Ltd. All rights reserved.

10aalpha-galactosidase10aBacillus stearothermophilus (NCIM-5146)10aPurification10aSecondary structure10athermostable enzyme1 aGote, M., M.1 aKhan, Mohammad, Islam1 aGokhale, D., V.1 aBastawade, Kulbhushan, B.1 aKhire, Jayant, Malhar uhttps://library.ncl.res.in/content/purification-characterization-and-substrate-specificity-thermostable-alpha-galactosidase-002016nas a2200229 4500008004100000022001400041245009600055210006900151260009900220300001400319490000700333520110200340653004001442653002301482653003301505653002901538100002201567700003001589700002301619700002001642856012401662 2007 eng d a0960-852400aStrain improvement of penicillium janthinellum ncim 1171 for increased cellulase production0 aStrain improvement of penicillium janthinellum ncim 1171 for inc aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcMAY a1467-14730 v983 a

The strain of Penicilhuinjanthinellunt NOM 1171 was subjected to mutation involving treatment of Ethyl Methyl Sulfonate (EMS) for 24 h followed by UV-irradiation for 3 min. Successive mutants showed enhanced cellulase production (EMS-UV-8), clearance zone on Avicel containing plate (SM2) and rapid growth on Walseth cellulose agar plates containing 0.2% 2-deoxy-D-glucose (SM3). These mutants were transferred to Walseth cellulose plates containing higher concentration (1.5%) of 2-deoxy-D-glucose (SM4) in which only five mutants showed clearance zone on SM4. All these mutants showed approximately two-fold increase in activity of both FPase and CMCase in shake flask culture when grown on basal medium containing CP-123 (1%) and wheat bran (2.5%). The enzyme preparations from these mutants were used to hydrolyze Avicel. Higher hydrolysis yields of Avicel were obtained with enzyme preparations of EU1. This is the first report on the isolation and selection of mutants based on hydrolysis of Avicel, which is the most crystalline substrate. (c) 2006 Elsevier Ltd. All rights reserved.

10a2-deoxy-D-glucose resistant mutants10acellulase activity10aEMS and ultraviolet mutation10aPenicillium janthinellum1 aAdsul, Mukund, G.1 aBastawade, Kulbhushan, B.1 aVarma, Anjanikumar1 aGokhale, D., V. uhttps://library.ncl.res.in/content/strain-improvement-penicillium-janthinellum-ncim-1171-increased-cellulase-production01984nas a2200205 4500008004100000022001400041245011900055210006900174260009900243300001400342490000800356520113000364653002801494653002601522653002501548100002201573700003001595700002601625856012701651 2009 eng d a0960-852400aBiochemical characterization of two xylanases from yeast Pseudozyma hubeiensis producing only xylooligosaccharides0 aBiochemical characterization of two xylanases from yeast Pseudoz aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcDEC a6488-64950 v1003 a

Two distinct xylanases from Pseudozyma hubeiensis NCIM 3574 were purified to homogeneity. The molecular masses of two native xylanases were 33.3 kDa (PhX33) and 20.1 kDa (PhX20). PhX33 is predominant with alpha-helix and PhX20 contained predominantly beta-sheets. Xylanase, PhX33, possesses three tryptophan and one carboxyl residues at the active site. The active site of PhX20 comprises one residue each of tryptophan, carboxyl and histidine. Carboxyl residue is mainly involved in catalysis and tryptophane residues are solely involved in substrate binding. Histidine residue present at the active site of PhX20 appeared to have a role in substrate binding. Both the xylanases produced only xylooligosaccharides (XOS) with degree of polymerization (DP) 3-7 without formation of xylose and xylobiose. These XOS could be used in functional foods or as prebiotics. Lc ms-ms ion search of cryptic digestion of these xylanases revealed that there is no significant homology of peptides with known fungal xylanase sequences which indicate that these xylanases appear to be new. (c) 2009 Elsevier Ltd. All rights reserved.

10aCellulase-free xylanase10aPseudozyma hubeiensis10aXylooligosaccharides1 aAdsul, Mukund, G.1 aBastawade, Kulbhushan, B.1 aGokhale, Digambar, V. uhttps://library.ncl.res.in/content/biochemical-characterization-two-xylanases-yeast-pseudozyma-hubeiensis-producing-only-001625nas a2200205 4500008004100000022001400041245008800055210006900143260009900212300001400311490000800325520083300333653001801166653002201184653002701206100001901233700003001252700002001282856011701302 2009 eng d a0960-852400aPurification and characterization of acidic lipase from aspergillus niger NCIM 12070 aPurification and characterization of acidic lipase from aspergil aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcFEB a1486-14900 v1003 a

An extracellular lipase from Aspergillus niger NCIM 1207 has been purified to homogeneity using ammonium sulfate precipitation followed by phenyl sepharose and Sephacryl-100 gel chromatography. This protocol resulted in 149 fold purification with 54% final recovery. The purified enzyme showed a prominent single band on SDS-PAGE. The purified enzyme is a monomeric protein of 32.2 kDa molecular weight and exhibits optimal activity at 50 degrees C. One interesting feature of this enzyme is its highly acidic pH optimum. The isoelectric point (pl) of lipase was 8.5. The purified lipase appears to be unique since it cleaved triolein at only 3-position releasing 1,2-diolein. Chemical modification studies revealed that His, Ser, Carboxylate and Trp are involved in catalysis. (c) 2008 Elsevier Ltd. All rights reserved.

10aAcidic lipase10aAspergillus niger10aPositional specificity1 aMhetras, Nutan1 aBastawade, Kulbhushan, B.1 aGokhale, D., V. uhttps://library.ncl.res.in/content/purification-and-characterization-acidic-lipase-aspergillus-niger-ncim-1207-002073nas a2200265 4500008004100000022001400041245011900055210006900174260009900243300001600342490000800358520106000366653002201426653002301448653002501471653002301496653002201519100002601541700002201567700003001589700001901619700002301638700002001661856012601681 2011 eng d a0960-852400aDifferential induction, purification and characterization of cold active lipase from Yarrowia lipolytica NCIM 36390 aDifferential induction purification and characterization of cold aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcNOV a10663-106700 v1023 a

The production, purification and characterization of cold active lipases by Yarrowia lipolytica NCIM 3639 is described. The study presents a new finding of production of cell bound and extracellular lipase activities depending upon the substrate used for growth. The strain produced cell bound and extracellular lipase activity when grown on olive oil and Tween 80, respectively. The organism grew profusely at 20 degrees C and at initial pH of 5.5, producing maximum extracellular lipase. The purified lipase has a molecular mass of 400 kDa having 20 subunits forming a multimeric native protein. Further the enzyme displayed an optimum pH of 5.0 and optimum temperature of 25 degrees C. Peptide mass finger printing reveled that some peptides showed homologues sequence (42%) to Yarrowia lipolytica LIP8p. The studies on hydrolysis of racemic lavandulyl acetate revealed that extracellular and cell bound lipases show preference over the opposite antipodes of irregular monoterpene, lavandulyl acetate. (C) 2011 Elsevier Ltd. All rights reserved.

10aCell bound lipase10aCold active lipase10aExtracellular lipase10aLavandulyl acetate10aOligomeric lipase1 aYadav, K., N. Sathish1 aAdsul, Mukund, G.1 aBastawade, Kulbhushan, B.1 aJadhav, D., D.1 aThulasiram, H., V.1 aGokhale, D., V. uhttps://library.ncl.res.in/content/differential-induction-purification-and-characterization-cold-active-lipase-yarrowia-002402nas a2200205 4500008004100000022001400041245011800055210006900173260010200242300001400344490000600358520153300364653003201897653003201929653003101961100001901992700003002011700002602041856012902067 2011 eng d a1930-212600aHyper-production of beta-glucosidase and beta-xylosidase by aspergillus niger NCIM 1207 In Xylan-Containing Media0 aHyperproduction of betaglucosidase and betaxylosidase by aspergi aCAMPUS BOX 8005, RALEIGH, NC 27695-8005 USAbNORTH CAROLINA STATE UNIV DEPT WOOD & PAPER SCIcJAN a2066-20760 v63 a

Aspergillus niger NCIM 1207 produced significantly high levels of beta-glucosidase and beta-xylosidase activities in submerged fermentation. Cellulose induced only beta-glucosidase, while xylan induced both beta-glucosidase and beta-xylosidase activities. Both the enzymes of this strain were found to undergo catabolite repression in the presence of high concentrations of glucose and glycerol. The sudden drop in pH of the fermentation medium below 3.5 caused the inactivation of enzymes when the fungus was grown in glycerol-containing media at lower temperatures. The growth of the organism at 36 degrees C led to an increase in pH of the fermentation above 6.0 that affected beta-xylosidase activity significantly. Highest levels of beta-glucosidase ((19 IU mL(-1) or 633 IU g(-1) of substrate) and beta-xylosidase (18.7 IU/mL(-1) or 620 IU g(-1) of substrate) activities were detected when A. niger was grown at 30 degrees C for first five days followed by further incubation at 36 degrees C. Such a process of growing the organism at lower temperatures (growth phase) followed by producing the enzymes at higher temperatures (production phase) in case of fungal systems has not been reported so far. The zymogram staining of the beta-glucosidase demonstrated that A. niger produced only single species of beta-glucosidase. We feel that A. niger NCIM 1207 is a potential candidate to produce both beta-glucosidase and beta-xylosidase in high amounts that can be used to supplement commercial cellulase preparations.

10aAspergillus niger NCIM 120710abeta-glucosidase production10abeta-xylosidase production1 aKhisti, Ujwala1 aBastawade, Kulbhushan, B.1 aGokhale, Digambar, V. uhttps://library.ncl.res.in/content/hyper-production-beta-glucosidase-and-beta-xylosidase-aspergillus-niger-ncim-1207-xylan-0