02112nas a2200289   4500008004100000022001400041245009300055210006900148260009900217300001400316490000700330520111900337653002201456653001701478653001701495653001701512653001301529100002501542700002101567700002201588700001601610700001701626700002501643700002201668700001601690856011601706       2005                        eng d  a1359-511300aOptimization and scale up of production of alkaline protease from Conidiobolus coronatus0 aOptimization and scale up of production of alkaline protease fro  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcSEP  a3152-31580 v403 a<p>Alkaline protease secreted by Conidiobolus coronatus has been evaluated extensively in tanneries and finds application in pre-tanning operations in leather manufacture. It is important to produce the enzyme in inexpensive and optimized media on large scale for the process to be commercially viable. The present paper describes optimization of fermentation conditions in shake flasks and scale up of production to 100 L in fermentors. The production is complete in 2-3 days comparable to bacterial fermentations. The organism utilized several carbon sources such as starch, sucrose, lactose, glucose and fructose for production. Soyabean meal at an optimum concentration of 2-3% was found to be best inducer. Diammonium hydrogen phosphate, casamino acids and Hi-media peptone gave activities comparable to yeast extract. Preservation and stabilization studies showed that glycerol conferred considerable stabilization at room temperature while ammonium sulphate precipitated enzyme at 0.9 saturation was best with stability up to 2 years even at room temperature. (c) 2005 Elsevier Ltd. All rights reserved.</p>10aAlkaline Protease10aConidiobolus10aFermentation10aOptimization10ascale up1 aLaxman, Ryali, Seeta1 aSonawane, A., P.1 aMore, Shivaji, V.1 aRao, B., S.1 aRele, M., V.1 aJogdand, Vitthal, V.1 aDeshpande, V., V.1 aRao, M., B.  uhttps://library.ncl.res.in/content/optimization-and-scale-production-alkaline-protease-conidiobolus-coronatus-001407nas a2200205   4500008004100000022001400041245007000055210006900125260007400194300001400268490000700282520066700289653002300956653002200979653002201001653002501023100002401048700002501072856010401097       2008                        eng d  a0141-549200aHexavalent chromate reduction by immobilized streptomyces griseus0 aHexavalent chromate reduction by immobilized streptomyces griseu  aVAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDSbSPRINGERcJUN  a1005-10100 v303 a<p>Hexavalent chromium, which is a mutagen and carcinogen, was efficiently reduced by Streptomyces griseus. This activity was associated with the cell. Cr6+ reduction by free as well as immobilized cells was studied: cells in PVA- alginate had the highest ( 100%) Cr6+ removal efficiency in 24 h with reduction rates similar to free cells. Immobilized cells completely reduced 25 mg Cr6+ l(-1) in 24 h. PVA- alginate immobilized cells could be reused four times to completely reduce 25 mg Cr6+ l(-1) in 24 h each time. Chromate in a simulated effluent containing Cu2+, Mg2+, Mn2+ and Zn2+ was completely reduced by PVA- alginate immobilized cells within 9 h.</p>10aChromate reduction10aImmobilized cells10apolyvinyl alcohol10aStreptomyces griseus1 aPoopal, Ashwini, C.1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/hexavalent-chromate-reduction-immobilized-streptomyces-griseus-001723nas a2200217   4500008004100000022001400041245008800055210006900143260007400212300001000286490000700296520091600303653001901219653002301238653002201261653003101283653002501314100002401339700002501363856011701388       2009                        eng d  a0141-549200aChromate reduction by PVA-alginate immobilized streptomyces griseus in a bioreactor0 aChromate reduction by PVAalginate immobilized streptomyces grise  aVAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDSbSPRINGERcJAN  a71-760 v313 a<p>Microbial reduction of toxic Cr(6+) to the less toxic Cr(3+) is potentially a useful bioremediation process. Among the matrices tested for whole cell immobilization of an efficient chromate-reducing Streptomyces griseus strain, PVA-alginate was the most effective and was used for reduction of Cr(VI) in a bioreactor. Cr(6+) reduction efficiency decreased as Cr(6+) was increased from 2 to 12 mg l(-1) but increased with an increase in biomass concentration. However, increasing the flow rate from 2 to 8 ml h(-1) did not significantly affect Cr(6+) reduction. The reduction was faster in simulated effluent than in synthetic medium and complete removal of 8 mg Cr(6+) l(-1) from effluent and synthetic medium occurred in 2 and 12 h, respectively. Our results indicate that immobilized S. griseus cells could be applied for the large-scale bioremediation of chromate-containing effluents and wastewaters.</p>10aBioremediation10aChromate reduction10aImmobilized cells10aPolyvinyl alcohol-alginate10aStreptomyces griseus1 aPoopal, Ashwini, C.1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/chromate-reduction-pva-alginate-immobilized-streptomyces-griseus-bioreactor-001877nas a2200241   4500008004100000022001400041245012800055210006900183260009900252300001400351490000800365520092800373653002601301653002501327653002601352653002601378653002201404100002001426700002301446700002501469700001401494856012701508       2009                        eng d  a0960-852400aHydrolysis of cellulose derived from steam exploded bagasse by penicillium cellulases: comparison with commercial cellulase0 aHydrolysis of cellulose derived from steam exploded bagasse by p  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcDEC  a6679-66810 v1003 a<p>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.</p>10aAccellerase (TM) 100010aEnzymatic hydrolysis10aHigh beta-glucosidase10aPenicillium cellulase10aSugarcane bagasse1 aSingh, Rajkumar1 aVarma, Anjanikumar1 aLaxman, Ryali, Seeta1 aRao, Mala  uhttps://library.ncl.res.in/content/hydrolysis-cellulose-derived-steam-exploded-bagasse-penicillium-cellulases-comparison-001925nas a2200205   4500008004100000022001400041245007200055210006900127260007300196300001200269490000800281520119200289653001701481653002301498653002401521653002501545100002401570700002501594856010001619       2009                        eng d  a0304-389400aStudies on biological reduction of chromate by Streptomyces griseus0 aStudies on biological reduction of chromate by Streptomyces gris  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcSEP  a539-5450 v1693 a<p>Chromium is a toxic heavy metal used in various industries and leads to environmental pollution due to improper handling. The most toxic form of chromium Cr(VI) can be converted to less toxic Cr(III) by reduction. Among the actinomycetes tested for chromate reduction, thirteen strains reduced Cr(VI) to Cr(III), of which one strain of Streptomyces griseus (NCIM 2020) was most efficient showing complete reduction within 24h. The organism was able to use a number of carbon sources as electron donors. Sulphate, nitrate, chloride and carbonate had no effect on chromate reduction during growth while cations such as Cd, Ni, Co and Cu were inhibitory to varying degrees. Chromate reduction was associated with the bacterial cells and sonication was the best method of cell breakage to release the enzyme. The enzyme was constitutive and did not require presence of chromate during growth for expression of activity. Chromate reduction with cell free extract (CFE) was observed without added NADH. However, addition of NAD(P)H resulted in 2-3-fold increase in activity. Chromate reductase showed optimum activity at 28 degrees C and pH 7 (C) 2009 Elsevier B.V. All rights reserved.</p>10aBioreduction10aChromate reductase10aHexavalent chromium10aStreptomyces griseus1 aPoopal, Ashwini, C.1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/studies-biological-reduction-chromate-streptomyces-griseus-001601nas a2200205   4500008004100000022001400041245008700055210006900142260008000211300001400291490000700305520083500312653002201147653002701169653001901196653001901215100001801234700002501252856011801277       2011                        eng d  a1582-959600aImmobilization of conidiobolus coronatus alkaline protease on waste fungal biomass0 aImmobilization of conidiobolus coronatus alkaline protease on wa  a71 MANGERON BLVD, IASI, 700050, ROMANIAbGH ASACHI TECHNICAL UNIV IASIcNOV  a1727-17320 v103 a<p>Alkaline protease from Conidiobolus coronatus which is optimally active at pH 10 and 40 degrees C finds application in leather and detergent industries as well as for recovery of silver from waste photographic films. The protease was immobilized in Ca-alginate, polyacrylamide gel and alkali treated waste fungal biomass (ATWFB). ATWFB was found to be most suitable among the matrices tested. Glutaraldehyde marginally increased the binding to ATWFB. Binding of protease to ATWFB seems to be through adsorption as confirmed by FTIR spectra. Though temperature optima of free and immobilized proteases were identical, optimum pH of the immobilized enzyme shifted to 11 from 10. Temperature stability of the protease increased after immobilization. Immobilized protease could be reused 3 times with marginal loss in activity.</p>10aAlkaline Protease10aConidiobolus coronatus10afungal biomass10aImmobilization1 aShankar, Shiv1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/immobilization-conidiobolus-coronatus-alkaline-protease-waste-fungal-biomass-001855nas a2200217   4500008004100000022001400041245009400055210006900149260009900218300001200317490000700329520104200336653002201378653002401400653001701424653002201441100001801463700001401481700002501495856011701520       2011                        eng d  a1359-511300aPurification and characterization of an alkaline protease by a new strain of Beauveria sp0 aPurification and characterization of an alkaline protease by a n  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcFEB  a579-5850 v463 a<p>A fungal culture isolated from animal dung was identified as a new strain of Beauveria sp MTCC 5184 based on 18S rDNA and ITS nucleotide sequence homology. The fungal isolate secretes alkaline protease active at pH 9 and 50 degrees C. The alkaline protease from Beauveria sp (BAP) was purified to homogeneity with 10.2-folds increase in specific activity and 38.6% recovery. The molecular mass and isoelectric point of the protease were found to be 29 kDa and 9.3, respectively. The N-terminal sequence of the BAP showed only partial homology with subtilisin like proteases from other fungi. The enzyme was stable up to 40 degrees C and pH 3-11. The protease was inhibited by Cd(2+), Hg(2+) and Mn(2+). The activity was totally lost in the presence of 1 mM PMSF suggesting it to be a serine protease. The protease showed maximum activity with casein followed by haemoglobin and BSA. The purified protease is able to separate the endothelial cells and can be used in animal cell culture. (C) 2010 Elsevier Ltd. All rights reserved.</p>10aAlkaline Protease10aAnimal cell culture10aBeauveria sp10aSequence homology1 aShankar, Shiv1 aRao, Mala1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/purification-and-characterization-alkaline-protease-new-strain-beauveria-sp-001950nas a2200241   4500008004100000022001400041245010000055210006900155260007900224300001400303490000800317520106300325653001301388653002401401653002501425653002701450653002601477100002201503700002001525700002501545700001401570856012401584       2012                        eng d  a0273-228900aEffect of alkali pretreatment on the structural properties and enzymatic hydrolysis of corn cob0 aEffect of alkali pretreatment on the structural properties and e  a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcDEC  a1806-18190 v1683 a<p>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.</p>10aCorn cob10aCrystallinity index10aEnzymatic hydrolysis10aPenicillium pinophilum10aSpecific surface area1 aSahare, Padmavati1 aSingh, Rajkumar1 aLaxman, Ryali, Seeta1 aRao, Mala  uhttps://library.ncl.res.in/content/effect-alkali-pretreatment-structural-properties-and-enzymatic-hydrolysis-corn-cob-002494nas a2200229   4500008004100000022001400041245010100055210006900156260011000225300001200335490000700347520160200354653002701956653002801983653001802011653003302029653001702062100001602079700002502095700001402120856013002134       2012                        eng d  a0301-120800aPurification and biochemical characterization of endoglucanase from Penicillium pinophilum MS 200 aPurification and biochemical characterization of endoglucanase f  aDR K S KRISHNAN MARG, PUSA CAMPUS, NEW DELHI 110 012, INDIAbNATL INST SCIENCE COMMUNICATION-NISCAIRcJUN  a189-1940 v493 a<p>Cellulases find increasing prominence in sustainable production of fuel and feedstock from lignocellulosic biomass. The purification and biochemical characterization of individual components of cellulase complex is important to understand the mechanism of their action for the solubilization of crystalline cellulose. In this study, an extra-cellular endoglucanase isolated from culture filtrate of Penicillium pinophilum MS 20 was purified to homogeneity by ammonium sulphate precipitation, ion-exchange chromatography and gel filtration. The purified endoglucanase (specific activity 69 U/mg) was a monomeric protein with molecular mass of 42 kDa, as determined by SDS-PAGE. The endoglucanase was active over a broad range of pH (4-7) with maximum activity at pH 5 and showed optimum temperature of 50 degrees C. It retained 100% activity at 50 degrees C for 6 h and half- lives of 4 h and 3 h at 60 degrees C and 70 degrees C, respectively. The kinetic constants for the endoglucanase determined with carboxymethyl cellulose as substrate were V-max of 72.5 U/mg and apparent K-m of 4.8 mg/ml. The enzyme also showed moderate activity towards H3PO4 swollen cellulose and p-nitrophenyl beta-D-glucoside, but no activity towards filter paper, Avicel and oat spelt xylan. The activity was positively modulated by 47, 32 and 25% in the presence of Co2+, Zn2+ and Mg2+, respectively to the reaction mixture. The wide pH stability (4-7) and temperature stability up to 50 degrees C of endoglucanase makes the enzyme suitable for use in cellulose saccharification at moderate temperature and pH.</p>10aBiochemical properties10aCarboxymethyl cellulose10aEndoglucanase10aPenicillium pinophilum MS 2010aPurification1 aPol, Dipali1 aLaxman, Ryali, Seeta1 aRao, Mala  uhttps://library.ncl.res.in/content/purification-and-biochemical-characterization-endoglucanase-penicillium-pinophilum-ms-20-001543nas a2200253   4500008004100000022001400041245005700055210005700112260008600169300001100255490000700266520074800273653002201021653001401043653001401057653001401071653000901085653001601094100002201110700002701132700001901159700002501178856008601203       2013                        eng d  a1544-047800aEnzymatic degumming of silk with microbial proteases0 aEnzymatic degumming of silk with microbial proteases  a325 CHESTNUT ST, SUITE 800, PHILADELPHIA, PA 19106 USAbTAYLOR & FRANCIS INCcJAN  a98-1110 v103 a<p>Degumming of Chinese bivoltine silk with alkaline proteases from various microbial sources was investigated and compared with commercial enzymes. Among the proteases tested, two fungal and two actinomycete proteases were promising, which showed weight loss similar to conventional method (19.58% to 21.78%). Conidiobolus brefeldianus and BOA-2 proteases were best enzymes, which showed weight loss similar to conventional method with low enzyme concentrations and in shorter time. No significant differences were found in tensile strength or elongation at break by enzymatic degumming indicating that there was no damage to the fiber. Scanning electron micrographs showed the sericin deposits were removed and the fibers were separated.</p>10aAlkaline Protease10abivoltine10adegumming10amicrobial10aSilk10aweight loss1 aMore, Shivaji, V.1 aKhandelwal, Harish, B.1 aJoseph, M., A.1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/enzymatic-degumming-silk-microbial-proteases-002593nas a2200277   4500008004100000022001400041245009900055210006900154260005700223300001200280490000700292520162200299653001401921653002601935653003101961653002001992653001402012653002502026653002802051100002102079700002102100700001802121700002502139700002502164856012602189       2014                        eng d  a0175-757100aSubtilase from Beauveria sp.: conformational and functional investigation of unusual stability0 aSubtilase from Beauveria sp conformational and functional invest  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcSEP  a393-4030 v433 a<p>Retention of total activity of the subtilisin-like serine protease from Beauveria sp. MTCC 5184 (Bprot) in the vicinity of (1) 3 M GdnHCl for 12 h, (2) 50 % methanol and dimethyl sulfoxide each for 24 h, and (3) proteolytic enzymes (trypsin, chymotrypsin, and proteinase K) for 48 h led to expect the enzyme to be a kinetically stable protein. Also, the structure of the protein was stable at pH 2.0. Biophysical characterization and conformational transitions were monitored using steady-state and time-resolved fluorescence, FTIR, and CD spectroscopy. Single tryptophan in the protein exists as two conformers, in hydrophobic and polar environment. The secondary structure of Bprot was stable in 3 M GdnHCl as seen in far-UV CD spectra. The active fraction of Bprot obtained from size-exclusion chromatography in the presence of GdnHCl (1.0-3.0 M) eluted at reduced retention time. The peak area of inactive or denatured protein with the same retention time as that of native protein increased with increasing concentration of denaturant (1.0-4.0 M GdnHCl). However, the kinetics of GdnHCl-induced unfolding as studied from intrinsic fluorescence revealed k (unf) of native protein to be 5.407 x 10(-5) s(-1) and a half-life of 3.56 h. The enzyme is thermodynamically stable in spite of being resistant to the denaturant, which could be due to the effect of GdnHCl imparting rigidity to the active fraction and simultaneously unfolding the partially unfolded protein that exists in equilibrium with the folded active protein. Thermal and pH denaturation of Bprot exhibited interesting structural transitions.</p>10aBeauveria10aChemical denaturation10aConformational transitions10aSerine protease10aSubtilase10aThermal denaturation10aThermodynamic stability1 aDalal, Sayli, A.1 aMore, Snehal, V.1 aShankar, Shiv1 aLaxman, Ryali, Seeta1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/subtilase-beauveria-sp-conformational-and-functional-investigation-unusual-stability-002792nas a2200337   4500008004100000022001400041245011000055210006900165260007100234300001200305490000600317520166100323653001301984653002501997653001502022653001502037653002102052100001702073700002002090700002002110700002002130700002202150700002102172700002102193700002202214700001902236700002702255700001702282700002502299856013002324       2014                        eng d  a2168-048500aUptake of Azo dyes into silk glands for production of colored silk cocoons using a green feeding approach0 aUptake of Azo dyes into silk glands for production of colored si  a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcFEB  a312-3170 v23 a<p>Dyeing of textile fabrics is considered to be one of the most polluting industries today, and there is a need to develop green processes that can reduce this pollution. A promising technology that can potentially cleanup the dyeing of silk fibers that are widely used for textile applications would involve the generation of intrinsically colored silk cocoons. This can be achieved by feeding of Bombyx mori silkworm larvae with a modified feed of mulberry leaves containing a sprayed dye solution. This process significantly reduces the need for treating toxic dye effluents that are generated in traditional dyeing processes. In this report, we have evaluated a set of seven different azo dyes that are used in the textile industry for dyeing to produce intrinsically dyed silk. The dyes used in the study had similar chemical structures with systematically varying partition coefficients. The results suggest that while some dyes produced intrinsically colored silk other did not. Careful evaluation of the physical properties of these related azo dyes suggest that the balance of hydrophobic and hydrophilic character is necessary for diffusion of the dye from the alimentary canal of the silkworm larva into the hemolymph and later into the silk glands. The partition coefficient of the dye also determines the preferential association of the dye with either sericin or fibroin protein in the silkworm gland and finally into the cocoon. These insights are extremely important in development of novel dye molecules that can be successfully fed to Bombyx mori silkworm larvae for producing intrinsically colored silk of various colors and shades.</p>10aAzo dyes10aBiochemical pathways10aColor silk10aDye uptake10a`' Green `' silk1 aNisal, Anuya1 aTrivedy, Kanika1 aMohammad, Hasan1 aPanneri, Suyana1 aGupta, Sayam, Sen1 aLele, Ashish, K.1 aManchala, Ramesh1 aKumar, Nirmal, S.1 aGadgil, Mugdha1 aKhandelwal, Harish, B.1 aMore, Snehal1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/uptake-azo-dyes-silk-glands-production-colored-silk-cocoons-using-green-feeding-approach-002082nas a2200217   4500008004100000022001400041245012000055210006900175260007900244300001200323490000800335520125300343653001601596653002201612653001701634653002001651653002301671100001801694700002501712856012701737       2015                        eng d  a0273-228900aBiophysicochemical characterization of an alkaline protease from beauveria sp. MTCC 5184 with multiple applications0 aBiophysicochemical characterization of an alkaline protease from  a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcJAN  a589-6020 v1753 a<p>This study illustrates the biophysicochemical properties of an alkaline protease, BAP (Beauveria sp. alkaline protease) from Beauveria sp. MTCC 5184. This protease exhibited maximum activity at 50 degrees C, pH 9.0, and stability in a broad pH range, in the presence of organic solvents, denaturants, as well as detergents. Wash performance studies revealed that BAP was able to remove blood clots/stains from blood-soaked cloth. Peptide mass fingerprinting results demonstrated partial homology of BAP with subtilisin-like proteinase. BAP showed catalytic activity against natural as well as synthetic substrates. Active site characterization of BAP confirmed the involvement of serine, tryptophan, and aspartic acid in catalytic activity. Detailed kinetic and thermodynamic studies of BAP demonstrated that the activation energy (Ea) for casein hydrolysis was 82.55 kJ/M, the specificity constant (Kcat/K-m), and the values of Delta G (change in Gibbs free energy) decreased with increase in temperature, whereas Delta H (change in enthalapy) and Delta S (change in entropy) were constant. The results of the present study indicate that BAP has potential for applications as detergent additive, in peptide synthesis, and in basic research.</p>10aActive site10aAlkaline Protease10aBeauveria sp10aOrganic solvent10aSubstrate kinetics1 aShankar, Shiv1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/biophysicochemical-characterization-alkaline-protease-beauveria-sp-mtcc-5184-multiple-001983nas a2200253   4500008004100000022001400041245008300055210006900138260005700207300001200264490000700276520111600283653002201399653003001421653001401451653001901465653002401484653001601508100002701524700002101551700001801572700002501590856011401615       2015                        eng d  a1618-954X00aEco-friendly enzymatic dehairing of skins and hides by C-brefeldianus protease0 aEcofriendly enzymatic dehairing of skins and hides by Cbrefeldia  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcFEB  a393-4050 v173 a<p>Alkaline protease from Conidiobolus brefeldianus was efficient in unhairing various types of skins and hides. The crude protease preparation was active toward keratin-azure, elastin-orcin, azocasein, and azocoll, but did not show true collagenase activity. In addition, the crude enzyme exhibited other enzyme activities such as chondroitinase, laminarase, and chitinase. Complete hair removal of skin/hide by the protease achieved in 16-18 h. The dehaired pelt showed smooth and white appearance due to hair removal along with epidermal layer. In addition, the grain was clean and without damage in enzymatically dehaired pelts. The microscopic observation of the cross-section of dehaired goat skin and cow hide showed absence of epidermis, hair shaft with empty follicles. Enzymatic dehairing resulted in complete and uniform fiber opening in the dermis and corium region. Physical properties viz. tensile strength, elongation, and tear strength of dyed crust of enzymatically and conventionally dehaired pelts were comparable. Results were also validated on large scale with goat skins and cow hides.</p>10aAlkaline Protease10aConidiobolus brefeldianus10aCow hides10aDehaired pelts10aEnzymatic dehairing10aSheep skins1 aKhandelwal, Harish, B.1 aMore, Snehal, V.1 aKalal, K., M.1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/eco-friendly-enzymatic-dehairing-skins-and-hides-c-brefeldianus-protease-001907nas a2200253   4500008004100000022001400041245008900055210006900144260009200213300001200305490000600317520099800323653002201321653002101343653001701364653002301381653002101404100001801425700002501443700002401468700001801492700002501510856011801535       2015                        eng d  a2158-584900aGreen synthesis of silver nanoribbons from waste X-ray films using alkaline protease0 aGreen synthesis of silver nanoribbons from waste Xray films usin  a26650 THE OLD RD, STE 208, VALENCIA, CA 91381-0751 USAbAMER SCIENTIFIC PUBLISHERScAPR  a165-1700 v53 a<p>This work illustrates a facile approach to synthesize silver nanoribbons from waste X-ray films using alkaline protease from Beauveria sp. MTCC 5184 (BAP). The green synthesized nanoribbons have been characterized by UV-Vis spectroscopy, TEM, and FTIR. The UV-visible spectra gave maximum absorbance at 400 nm. TEM micrograph showed well-dispersed silver nanoribbons with an average length of 200-400 nm. FTIR result demonstrated the respective bands of the silver nanoribbons and proteins. XRD data revealed crystalline nature of silver nanoribbons dominated with (111) facets. In vitro antibacterial activity in terms of minimum inhibitory concentrations (MIC) and minimum bactericidal concentration (MBC) showed 8/16 mu g/mL (MIC/MBC) against Staphylococcus aureus ATCC 29213 and 4/8 mu g/mL (MIC/MBC) against Escherichia coli ATCC 25922. The green synthesized silver nanoribbons showed excellent biocompatibility up to 40 mu g/mL concentrations on mouse fibroblast cell line (L929).</p>10aAlkaline Protease10aCharacterization10aCytotoxicity10aSilver Nanoribbons10aWaste X-ray Film1 aShankar, Shiv1 aPrasad, R., G. S. V.1 aSelvakannan, P., R.1 aJaiswal, Lily1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/green-synthesis-silver-nanoribbons-waste-x-ray-films-using-alkaline-protease-0