Data/hora: 01/06/2024 08:04:16

Provedor de dados: | 52
País: | Brazil
Título: | Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae
Autores: | Mushtaq,Zareena; Irfan,Muhammad; Nadeem,Muhammad; Naz,Mammona; Syed,Quratulain.
Data: | 2015-04-01
Ano: | 2015
Palavras-chave: | Kinetics; Purification; Characterization; Protease; Detergent stability; Rhizopus oryzae.
Resumo: | 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 , Kcat , Vmax and Kcat/Km values of purified protease were 7.0 mg/mL, 3.8 x102S-1, 54.30 µmol/min and 54.28 s-1mg -1.mL respectively, using casein as substrate. The purified alkaline protease had stability with commercial detergents.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000200175
Editor: | Instituto de Tecnologia do Paraná - Tecpar
Relação: | 10.1590/S1516-8913201400071
Formato: | text/html
Fonte: | Brazilian Archives of Biology and Technology  v.58 n.2 2015
Fonte: | info:eu-repo/semantics/openAccess