@article { ISI:000232737900002, title = {Enzymatic hydrolysis of delignified bagasse polysaccharides}, journal = {Carbohydrate Polymers}, volume = {62}, number = {1}, year = {2005}, month = {OCT}, pages = {6-10}, publisher = {ELSEVIER SCI LTD}, type = {Article}, address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND}, abstract = {

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.

}, keywords = {bagasse polysaccharides, Cellulase, chemical treatment, Enzymatic hydrolysis, Penicillium janthinellum, Sugarcane bagasse, Xylanase}, issn = {0144-8617}, doi = {10.1016/j.carbpol.2005.07.010}, author = {Adsul, Mukund G. and Ghule, J. E. and Shaikh, H. and Singh, R. and Bastawade, Kulbhushan B. and Gokhale, D. V. and Varma, Anjanikumar} } @article { ISI:000237886100006, title = {Convenient chemoenzymatic synthesis of (1S,7aS)-1-hydroxy-5-oxo-4-(2 {\textquoteleft}-carboxyethyl)-7a-methyltetrahydro-indane - a key intermediate of steroids}, journal = {Journal of Molecular Catalysis B-Enzymatic}, volume = {40}, number = {1-2}, year = {2006}, month = {MAY}, pages = {38-43}, publisher = {ELSEVIER SCIENCE BV}, type = {Article}, address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS}, abstract = {

A porcine pancreatic lipase mediated enzymatic hydrolysis of (+/-)-1-acetoxy-5-oxo-4-(2 {\textquoteleft}-carbomethoxyethyl)-7a-methyltetrahydroindane (5b) furnished (1S,7aS)-1-acetoxy-5-oxo-4-(2 {\textquoteleft}-carbomethoxyethyl)-7a-methyltetrahydro-indane (9) and (1R,7aR)-1-hydroxy-5-oxo-4-(2 {\textquoteleft}-carbomethoxyethyl)-7a-methyltetrahydro-indane (8) with \> 99\% e.e. which on further chemical hydrolysis gave 1 and ent-1, key intermediates of steroids. (c) 2006 Elsevier B.V. All rights reserved.

}, keywords = {chemoenzymatic method, Enzymatic hydrolysis, steroids, terpenoids}, issn = {1381-1177}, doi = {10.1016/j.molcatb.2006.01.037}, author = {Kalkote, Uttam R. and Purude, A. N. and Puranik, Vedavati G. and Gurjar, M. K.} } @article { ISI:000270147700079, title = {Hydrolysis of cellulose derived from steam exploded bagasse by penicillium cellulases: comparison with commercial cellulase}, journal = {Bioresource Technology}, volume = {100}, number = {24}, year = {2009}, month = {DEC}, pages = {6679-6681}, publisher = {ELSEVIER SCI LTD}, address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND}, abstract = {

A complete cellulase from Penicillium pinophilum was evaluated for the hydrolysis of a-cellulose derived from steam exploded sugarcane bagasse and other cellulosic substrates. alpha-Cellulose at 1\% substrate concentration was completely hydrolyzed by Penicillium cellulase within 3 h wherein at 10\% the hydrolysis was 100\% within 24 h with an enzyme loading of 10 FPU/g. The hydrolysate yielded glucose as major end product as analyzed by HPLC. Under similar conditions, hydrolysis of Sigmacell (microcrystalline cellulose), CP-123 (pulverized cellulose powder) and ball milled Solka Floc were 42\%, 56\% and 52\%, respectively. Further the hydrolysis performance of Penicillium sp. cellulase is compared with Trichoderma reesei cellulase (Accellerase (TM) 1000) from Genencore. The kinetics of hydrolysis with respect to enzyme and substrate concentration will be presented. (C) 2009 Elsevier Ltd. All rights reserved.

}, keywords = {Accellerase (TM) 1000, Enzymatic hydrolysis, High beta-glucosidase, Penicillium cellulase, Sugarcane bagasse}, issn = {0960-8524}, doi = {10.1016/j.biortech.2009.07.060}, author = {Singh, Rajkumar and Varma, Anjanikumar and Laxman, Ryali Seeta and Rao, Mala} } @article { ISI:000294187400078, title = {Enhanced enzymatic hydrolysis of cellulose by partial modification of its chemical structure}, journal = {Carbohydrate Polymers}, volume = {86}, number = {2}, year = {2011}, month = {AUG}, pages = {962-968}, publisher = {ELSEVIER SCI LTD}, address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND}, abstract = {

A series of 2,3-dialdehyde celluloses with different degrees of oxidation were used for deriving corresponding dicarboxylate, dicarboxy, and Schiff{\textquoteright}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.

}, keywords = {2, 3-Dialdehyde celluloses, 3-Dibenzylimine cellulose, 3-Dibutylimine cellulose, 3-Dicarboxy celluloses, 3-Diethyimine cellulose, 3-Dihydrazone cellulose, 3-Dipropylimine cellulose, Cellulase, Enzymatic hydrolysis}, issn = {0144-8617}, doi = {10.1016/j.carbpol.2011.05.067}, author = {Shaikh, H. M. and Adsul, Mukund G. and Gokhale, D. V. and Varma, Anjanikumar} } @article { ISI:000312205000007, title = {Effect of alkali pretreatment on the structural properties and enzymatic hydrolysis of corn cob}, journal = {Applied Biochemistry and Biotechnology}, volume = {168}, number = {7}, year = {2012}, month = {DEC}, pages = {1806-1819}, publisher = {HUMANA PRESS INC}, address = {999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA}, abstract = {

An effective alkali pretreatment which affects the structural properties of cellulose (corn cob) has been studied. The pretreatment of corn cob was carried out with different combinations of alkali at varying temperatures. The most effective pretreatment of corn cob was achieved with 1 \% alkali at 50 A degrees C in 4 h. The crystallinity index (CrI) and specific surface area (SSA) of untreated corn cob was 39 \% and 0.52 m(2)/g wherein after alkali pretreatment CrI decreased to 15 \% and SSA increased to 3.32 m(2)/g. The fungal organism was identified as Penicillium pinophilum on the basis of ITS sequence. At 5 \% substrate concentration using a complete cellulase from Penicillium pinophilum the hydrolysis of untreated corn cob with 5, 10 and 20 FPU/g enzyme loadings were 11 \%, 13 \% and 16 \%, whereas after alkali treatment the hydrolysis increased to 78 \%, 90 \% and 100 \%, respectively. Further hydrolytic potential of commercial cellulases viz. Accellerase (TM) 1,000, Palkofeel-30 and Palkocel-40 were investigated under similar conditions.

}, keywords = {Corn cob, Crystallinity index, Enzymatic hydrolysis, Penicillium pinophilum, Specific surface area}, issn = {0273-2289}, doi = {10.1007/s12010-012-9898-y}, author = {Sahare, Padmavati and Singh, Rajkumar and Laxman, Ryali Seeta and Rao, Mala} }