02350nas a2200193 4500008004100000022001400041245010100055210006900156260011000225300001400335490000700349520156800356100001901924700001701943700002201960700002301982700002602005856012502031 2010 eng d a1463-926200aD-(-)-Lactic acid production from cellobiose and cellulose by Lactobacillus lactis mutant RM2-240 aDLactic acid production from cellobiose and cellulose by Lactoba aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcMAY a1106-11090 v123 a

Lactobacillus lactis mutant RM2-24 utilizes cellobiose efficiently, converting it into D-(-)-lactic acid. Cellobiose-degrading enzyme activities were determined for whole cells, cell extracts and disrupted cells. Aryl-beta-glucosidase activity was detected in whole cells and disrupted cells, suggesting that these activities are confined to the cells. The mutant produced 80 g l(-1) of lactic acid from 100 g l(-1) of cellobiose with 1.66 g l(-1) h(-1) productivity. Production of D-lactic acid from different cellulose samples was also studied. The cellulose samples at high concentration (10%) were hydrolyzed by cellulase enzyme preparation (10 FPU g(-1) cellulose) derived from Penicillium janthinellum mutant EU1 generated in our own laboratory. We obtained a maximum 72% hydrolysis, yielding glucose and cellobiose as the main end products. Lactic acid was produced from these cellulose samples by simultaneous sacchari. cation and fermentation (SSF) in a media containing a cellulase enzyme preparation derived from Penicillium janthinellum mutant EU1 and cellobiose utilizing Lactobacillus lactis mutant RM2-24. A maximum lactic acid concentration of 73 g l(-1) was produced from a concentration of 100 g l(-1) of bagasse-derived cellulose, the highest productivity and yield being 1.52 g l(-1) h(-1) and 0.73 g g(-1), respectively. Considering that bagasse is a waste material available in abundance, we propose to use this biomass to produce cellulose and then sugars, which can be fermented to valuable products such as ethanol and lactic acid.

1 aSinghvi, Mamta1 aJoshi, Dipti1 aAdsul, Mukund, G.1 aVarma, Anjanikumar1 aGokhale, Digambar, V. uhttp://library.ncl.res.in/content/d-lactic-acid-production-cellobiose-and-cellulose-lactobacillus-lactis-mutant-rm2-24-002035nas a2200241 4500008004100000022001400041245009900055210006900154260009900223300001400322490000800336520113800344653002401482653002401506653001201530653001601542653002501558100002201583700002001605700002801625700002001653856012001673 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. uhttp://library.ncl.res.in/content/development-biocatalysts-production-commodity-chemicals-lignocellulosic-biomass-002072nas a2200265 4500008004100000022001400041245011900055210006900174260009900243300001600342490000800358520106000366653002201426653002301448653002501471653002301496653002201519100002601541700002201567700003001589700001901619700002301638700002001661856012501681 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. uhttp://library.ncl.res.in/content/differential-induction-purification-and-characterization-cold-active-lipase-yarrowia-0