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	Provedor de dados BABT (1) BJM (1) Autor Bisht,Deepali (1) Darmwal,Nandan Singh (1) Irfan,Muhammad (1) Mushtaq,Zareena (1) Nadeem,Muhammad (1) Naz,Mammona (1) Syed,Quratulain (1) Yadav,Santosh Kumar (1) Mais... Palavra-chave Detergent stability (2) Alkaline lipase (1) Characterization (1) Kinetics (1) Mutant (1) Organic-solvent (1) P-nitrophenyl palmitate Pseudomonas (1) Protease (1) Purification (1) Rhizopus oryzae (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2015 (1) 2013 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae BABT Mushtaq,Zareena; Irfan,Muhammad; Nadeem,Muhammad; Naz,Mammona; Syed,Quratulain. In this study, extracellular alkaline protease was produced from Rhizopus oryzae in submerged fermentation using dairy waste (whey) as a substrate. Fermentation kinetics was studied and various parameters were optimized. The strain produced maximum protease at initial medium pH of 6.0 medium depth of 26 mm, inoculum size of 2% at incubation temperature of 35ºC for 168 h of fermentation. Alkaline protease was purified to homogeneity by ammonium sulphate fractionation followed by sephadex G-100 chromatography. The molecular mass of alkaline protease was 69 kDa determined by 10% SDS-PAGE. The optimum pH and temperature of alkaline protease was 9.0 and 40ºC, respectively. Metal profile of the enzyme showed that the enzyme was non-metallic in nature. The Km ,... Tipo: Info:eu-repo/semantics/article Palavras-chave: Kinetics; Purification; Characterization; Protease; Detergent stability; Rhizopus oryzae. Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000200175 An oxidant and organic solvent tolerant alkaline lipase by P. aeruginosa mutant: downstream processing and biochemical characterization BJM Bisht,Deepali; Yadav,Santosh Kumar; Darmwal,Nandan Singh. An extracellular alkaline lipase from Pseudomonas aeruginosa mutant has been purified to homogeneity using acetone precipitation followed by anion exchange and gel filtration chromatography and resulted in 27-fold purification with 19.6% final recovery. SDS-PAGE study suggested that the purified lipase has an apparent molecular mass of 67 kDa. The optimum temperature and pH for the purified lipase were 45°C and 8.0, respectively. The enzyme showed considerable stability in pH range of 7.0-11.0 and temperature range 35-55 °C. The metal ions Ca2+, Mg2+ and Na+ tend to increase the enzyme activity, whereas, Fe2+ and Mn2+ ions resulted in discreet decrease in the activity. Divalent cations Ca+2 and Mg+2 seemed to protect the enzyme against thermal denaturation... Tipo: Info:eu-repo/semantics/article Palavras-chave: Alkaline lipase; Detergent stability; Mutant; Organic-solvent; P-nitrophenyl palmitate Pseudomonas. Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822013000400040 Registros recuperados: 2 Primeira ... 1 ... Última

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