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-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-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-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