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-002971nas a2200241 4500008004100000022001400041245013500055210006900190260007300259300001200332490000700344520204800351653002602399653001302425653002702438653002502465653004102490100002102531700001602552700002002568700002302588856011802611 2007 eng d a0141-813000aMetal complexes of crosslinked chitosans. part II. an investigation of their hydrolysis to chitooligosaccharides using chitosanase0 aMetal complexes of crosslinked chitosans part II an investigatio aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcDEC a491-4960 v413 a

This paper investigates the behavior of crosslinked chitosans and metal-complexed crosslinked chitosans under similar hydrolytic conditions. Crosslinked chitosans with trimellitic anhydride, diisocyanatohexane, and dibromodecane as crosslinking agents under heterogenous reaction conditions were used as metal complexing agents by equilibrating them with metal salts such as ZnCl2, MnSO4, CuSO4, CdSO4, Pb(NO3)(2), and HgCl2. Crosslinked chitosan without metal complexation had the same hydrolytic behavior as uncrosslinked chitosan. However, when the crosslinked chitosans were complexed with metals, their rates of hydrolysis and extent of hydrolysis were significantly reduced. Thus, while for chitosan about 840 mu g/ml reducing sugar was produced in 4 h time, and 780 mu g/ml was produced for diisocyanatohexane crosslinked chitosan, only 400 mu g/ml and 320 [mu g/ml reducing sugars were produced for cadmium sulfate with crosslinked chitosan and diisocyanatohexane crosslinked chitosan, respectively. Similar results are obtained for other crosslinking agents. Studies on preincubation of the metal with the enzyme show that of the metals studied, Mn has no effect on preincubatioin with the enzyme, Hg, Cd, Pb, and Cu completely deactivates the enzyme, while Zn reduces the enzyme activity by about 43.3%. Preincubation of the metal salts with the chitosan shows that Hg and Cu completely deactivate the molecule from enzyme hydrolysis, Cd and Zn inactivate it to the extent of 56.8% and 43.3%, respectively, while Mn has no effect. Availability of the amino functions seems to be a key feature for the chitosanase to hydrolyze the chitosan polymer. This was also proved by the significant increase in the extent of hydrolysis for chitosan samples with 88% (final value 1120 mu g/ml reducing sugar) and 85% deacetylation (final value 840 mu g/ml reducing sugar). HPIC studies of the products show that a variety of oligomers are produced in the chitosanase enzyme hydrolytic reaction. (C) 2007 Elsevier B.V. All rights reserved.

10achitooligosaccharides10aChitosan10achitosanase hydrolysis10aCrosslinked chitosan10ametal-complexed crosslinked chitosan1 aTrimukhe, K., D.1 aBachate, S.1 aGokhale, D., V.1 aVarma, Anjanikumar uhttps://library.ncl.res.in/content/metal-complexes-crosslinked-chitosans-part-ii-investigation-their-hydrolysis-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-production01444nas a2200241 4500008004100000022001400041245013100055210006900186260007300255300001200328490000700340520057600347653001500923653001300938653001100951653001100962653001700973100002100990700002001011700002001031700002301051856012801074 2008 eng d a0141-813000aEnvironment friendly crosslinked chitosan as a matrix for selective adsorption and purification of lipase of aspergillus niger0 aEnvironment friendly crosslinked chitosan as a matrix for select aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcDEC a422-4250 v433 a

Chitosan and its derivatives have been used as affinity matrices for purification of lipase from Aspergillus niger NCIM 1207. Trimellitic anhydride (TMA)-crosslinked deacetylated chitin adsorbed lipase selectively, yielding approximately 5-fold purification of the crude lipase with 70% yield. Further 9-fold purification occurred on eluting through Sephacryl-100. These results suggest that chitosan derivatives can be used as inexpensive biopolymer matrices for the purification of lipases for industrial applications. (C) 2008 Elsevier B.V. All rights reserved.

10aAdsorption10aChitosan10aLipase10aMatrix10aPurification1 aTrimukhe, K., D.1 aMahadik, N., D.1 aGokhale, D., V.1 aVarma, Anjanikumar uhttps://library.ncl.res.in/content/environment-friendly-crosslinked-chitosan-matrix-selective-adsorption-and-purification-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-1207-001560nas a2200241 4500008004100000022001400041245007600055210006900131260007400200300001200274490000700286520071800293653002701011653002901038653002501067653001101092653002501103100001801128700002001146700002601166700002001192856010601212 2010 eng d a0141-549200aStrain improvement of lactobacillus lactis for d-lactic acid production0 aStrain improvement of lactobacillus lactis for dlactic acid prod aVAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDSbSPRINGERcAPR a517-5200 v323 a

Three mutants, isolated by repeated UV mutagenesis of Lactobacillus lactis NCIM 2368, produced increased d-lactic acid concentrations. These mutants were compared with the wild type using 100 g hydrolyzed cane sugar/l in the fermentation medium. One mutant, RM2-24, produced 81 g lactic acid/l which was over three times that of the wild type. The highest d-lactic acid (110 g/l) in batch fermentation was obtained with 150 g cane sugar/l with a 73% lactic acid yield. The mutant utilizes cellobiose efficiently, converting it into d-lactic acid suggesting the presence of cellobiase. Thus, this strain could be used to obtain d-lactic acid from cellulosic materials that are pre-hydrolyzed with cellulase.

10aCellobiose utilization10aD-Lactic acid production10aLactobacillus lactis10aMutant10aSucrose (cane sugar)1 aJoshi, D., S.1 aSinghvi, M., S.1 aKhire, Jayant, Malhar1 aGokhale, D., V. uhttps://library.ncl.res.in/content/strain-improvement-lactobacillus-lactis-d-lactic-acid-production-001852nas a2200217 4500008004100000022001400041245014800055210006900203260009900272300001400371490000800385520094100393653003701334653001901371653002901390653002701419100002001446700002201466700002001488856012601508 2011 eng d a0960-852400aComparative production of cellulases by mutants of penicillium janthinellum NCIM 1171 and its application in hydrolysis of avicel and cellulose0 aComparative production of cellulases by mutants of penicillium j aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcJUN a6569-65720 v1023 a

Mutants of Penicillium janthinellum NCIM 1171 were evaluated for cellulase production using both submerged fermentation (SmF) and solid state fermentation (SSF). Mutant EU2D-21 gave highest yields of cellulases in both SmF and SSF. Hydrolysis of Avicel and cellulose were compared using SmF and SSF derived enzyme preparations obtained from EU2D-21. Surprisingly, the use of SSF derived preparation gave less hydrolysis compared to SmF derived enzymes. This may be due to inactivation of beta-glucosidase at 50 degrees C in SSF derived enzyme preparations. SmF derived enzyme preparations contained both thermostable and thermosensitive beta-glucosidases where as SSF derived enzyme preparations contained predominantly thermosensitive beta-glucosidase. This is the first report on less thermostability of SSF derived p-glucosidase which is the main reason for getting less hydrolysis. (C) 2011 Elsevier Ltd. All rights reserved.

10abeta-Glucosidase thermostability10aMutant EU2D-2110aSolid state fermentation10aSubmerged fermentation1 aSinghvi, M., S.1 aAdsul, Mukund, G.1 aGokhale, D., V. uhttps://library.ncl.res.in/content/comparative-production-cellulases-mutants-penicillium-janthinellum-ncim-1171-and-its-002036nas a2200241 4500008004100000022001400041245009900055210006900154260009900223300001400322490000800336520113800344653002401482653002401506653001201530653001601542653002501558100002201583700002001605700002801625700002001653856012101673 2011 eng d a0960-852400aDevelopment of biocatalysts for production of commodity chemicals from lignocellulosic biomass0 aDevelopment of biocatalysts for production of commodity chemical aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcMAR a4304-43120 v1023 a

Lignocellulosic biomass is recognized as potential sustainable source for production of power, biofuels and variety of commodity chemicals which would potentially add economic value to biomass. Recalcitrance nature of biomass is largely responsible for the high cost of its conversion. Therefore, it is necessary to introduce some cost effective pretreatment processes to make the biomass polysaccharides easily amenable to enzymatic attack to release mixed fermentable sugars. Advancement in systemic biology can provide new tools for the development of such biocatalysts for sustainable production of commodity chemicals from biomass. Integration of functional genomics and system biology approaches may generate efficient microbial systems with new metabolic routes for production of commodity chemicals. This paper provides an overview of the challenges that are faced by the processes converting lignocellulosic biomass to commodity chemicals. The critical factors involved in engineering new microbial biocatalysts are also discussed with more emphasis on commodity chemicals. (C) 2011 Elsevier Ltd. All rights reserved.

10aBiomass utilization10aCommodity chemicals10aEthanol10aLactic acid10aMicrobial cellulases1 aAdsul, Mukund, G.1 aSinghvi, M., S.1 aGaikaiwari, Shalaka, A.1 aGokhale, D., V. uhttps://library.ncl.res.in/content/development-biocatalysts-production-commodity-chemicals-lignocellulosic-biomass-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-002192nas a2200301 4500008004100000022001400041245009700055210006900152260009900221300001200320490000700332520109700339653000601436653002801442653003001470653002901500653002701529653002801556653002801584653003001612653001401642653002501656100001901681700002201700700002001722700002301742856012501765 2011 eng d a0144-861700aEnhanced enzymatic hydrolysis of cellulose by partial modification of its chemical structure0 aEnhanced enzymatic hydrolysis of cellulose by partial modificati aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcAUG a962-9680 v863 a

A series of 2,3-dialdehyde celluloses with different degrees of oxidation were used for deriving corresponding dicarboxylate, dicarboxy, and Schiff's base cellulose derivatives. The dialdehyde cellulose was hydrolyzed by cellulase to a lower extent than the starting cellulose, except at high levels of aldehyde content (above 50%). For dicarboxylate and dicarboxy celluloses, the highest level of oxidized NaDCC and DCC hydrolysed up to 70 and 60% respectively which was 3-4 times more than cellulose. The 2,3-dioxime cellulose derivative hydrolyzes only up to 16.3% for the highest level of oxidized dioxime. In the case of 2,3-diethylimine cellulose, all derivatives hydrolyse faster than the native cellulose. Up to 75% hydrolysis was observed for 2,3-diethyimine cellulose-50, 2,3-dipropylimine and 2,3-dibutylimine cellulose. The 2,3-dibenzylimine cellulose hydrolyses a little slower than the alkylimine derivatives. The 2,3-dihydrazone cellulose derivatives with all level of oxidation showed resistance towards enzymatic hydrolysis. (C) 2011 Elsevier Ltd. All rights reserved.

10a210a3-Dialdehyde celluloses10a3-Dibenzylimine cellulose10a3-Dibutylimine cellulose10a3-Dicarboxy celluloses10a3-Diethyimine cellulose10a3-Dihydrazone cellulose10a3-Dipropylimine cellulose10aCellulase10aEnzymatic hydrolysis1 aShaikh, H., M.1 aAdsul, Mukund, G.1 aGokhale, D., V.1 aVarma, Anjanikumar uhttps://library.ncl.res.in/content/enhanced-enzymatic-hydrolysis-cellulose-partial-modification-its-chemical-structure-002321nas a2200241 4500008004100000022001400041245005900055210005800114260000800172300001400180490000800194520161100202653001801813653001801831653001801849653001301867653002501880653002001905100002001925700002101945700002001966856009301986 2019 eng d a1364-507200aPolylactic acid: synthesis and biomedical applications0 aPolylactic acid synthesis and biomedical applications cDEC a1612-16260 v1273 a

Social and economic development has driven considerable scientific and engineering efforts on the discovery, development and utilization of polymers. Polylactic acid (PLA) is one of the most promising biopolymers as it can be produced from nontoxic renewable feedstock. PLA has emerged as an important polymeric material for biomedical applications on account of its properties such as biocompatibility, biodegradability, mechanical strength and process ability. Lactic acid (LA) can be obtained by fermentation of sugars derived from renewable resources such as corn and sugarcane. PLA is thus an eco-friendly nontoxic polymer with features that permit use in the human body. Although PLA has a wide spectrum of applications, there are certain limitations such as slow degradation rate, hydrophobicity and low impact toughness associated with its use. Blending PLA with other polymers offers convenient options to improve associated properties or to generate novel PLA polymers/blends for target applications. A variety of PLA blends have been explored for various biomedical applications such as drug delivery, implants, sutures and tissue engineering. PLA and their copolymers are becoming widely used in tissue engineering for function restoration of impaired tissues due to their excellent biocompatibility and mechanical properties. The relationship between PLA material properties, manufacturing processes and development of products with desirable characteristics is described in this article. LA production, PLA synthesis and their applications in the biomedical field are also discussed.

10aBiocompatible10abiodegradable10adrug delivery10aimplants10al- and d-lactic acid10apolylactic acid1 aSinghvi, M., S.1 aZinjarde, S., S.1 aGokhale, D., V. uhttps://library.ncl.res.in/content/polylactic-acid-synthesis-and-biomedical-applications