02244nas a2200265 4500008004100000022001400041245012200055210006900177260008100246300001000327490000700337520126400344653002601608653002601634653002701660653003001687653001101717100001801728700001801746700001801764700003001782700002601812700002001838856012001858 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. uhttp://library.ncl.res.in/content/production-lactic-acid-and-fructose-media-cane-sugar-using-mutant-lactobacillus-002655nas a2200253 4500008004100000022001400041245014200055210006900197260009900266300001400365490000700379520163400386653002402020653004402044653001702088653002402105653002402129100001702153700002602170700002002196700003002216700002602246856012902272 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 uhttp://library.ncl.res.in/content/purification-characterization-and-substrate-specificity-thermostable-alpha-galactosidase-001624nas a2200205 4500008004100000022001400041245008800055210006900143260009900212300001400311490000800325520083300333653001801166653002201184653002701206100001901233700003001252700002001282856011601302 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. uhttp://library.ncl.res.in/content/purification-and-characterization-acidic-lipase-aspergillus-niger-ncim-1207-0