02593nas 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-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-001731nas a2200229   4500008004100000022001400041245013800055210006900193260000800262300000900270490000700279520093700286653002201223653001401245653001401259653000901273653001601282100002101298700002001319700003101339856013101370       2017                        eng d  a1544-047800aSilk degumming and utilization of silk sericin by hydrolysis using alkaline protease from beauveria Sp. (MTCC 5184): a green approach0 aSilk degumming and utilization of silk sericin by hydrolysis usi  cJUL  a1-110 v153 aConventionally, degumming is carried out at 90°C--110°C temperature by boiling the raw silk with Marseilles soap and sodium bicarbonate which eventually requires a lot of water and energy. In this study, degumming of Chinese bivoltine raw silk fibres with alkaline protease produced by Beauveria sp. (MTCC 5184) is studied. Complete degumming was obtained in 45 min with 75 units of enzyme per gram of silk. Degumming was found to be optimal at 50°C and pH 9.0. Scanning electron micrographs showed that the sericin deposits were removed and the obtained fibres were clean, separated, had smooth feel with shine as compared to untreated fibres. Sericin isolated from silk cocoon (by-product which goes waste) was hydrolyzed with the same alkaline protease obtained from Beauveria sp. to get small molecular weight peptides. These peptides can be utilized further for cosmetic, pharmaceutical, and various industrial applications.10aAlkaline Protease10abivoltine10adegumming10aSilk10aweight loss1 aMore, Snehal, V.1 aChavan, Sakalya1 aPrabhune, Asmita, Ashutosh  uhttps://library.ncl.res.in/content/silk-degumming-and-utilization-silk-sericin-hydrolysis-using-alkaline-protease-beauveria-sp