Kinetic analysis of extracellular proteolytic activity displayed by a locally isolated Rhizopus oryzae

Abstract

<span style="font-size:11.0pt;line-height:115%; font-family:" calibri","sans-serif";mso-ascii-theme-font:minor-latin;mso-fareast-font-family:="" "times="" new="" roman";mso-fareast-theme-font:minor-fareast;mso-hansi-theme-font:="" minor-latin;mso-bidi-font-family:"times="" roman";mso-ansi-language:en-us;="" mso-fareast-language:en-us;mso-bidi-language:ar-sa"="">The kinetic behaviour of an industrially important thermostable extracellular proteolytic enzyme produced by a locally isolated species, Rhizopus oryzae (RO) in shake flask culture, has been studied. Michaelis constant (<i>K</i>_m) and maximum reaction velocity (<i>V</i>_max) for this enzyme have been evaluated at different temperatures and substrate conditions. The inhibition coefficient (<i>K</i>_i) in presence of metal ions has also been estimated. An empirical correlation for the reaction velocity (<i>V</i>) has been developed as a function of temperature, <i>p</i>H substrate and enzyme concentrations.</span>