Abstract
An extracellular beta amylase was induced in cultures of Bacillus subtilis isolated from the kolanut weevil, Balanogastris kolae grown in liquid medium that contained kolanut starch as sole carbon source. The enzyme was partially purified 1.28-fold by acid treatment with ice cold 1.0N HCl and 6.4-fold by gel filtration with Sephadex G-150. The beta amylase had a molecular weight of 39.4 kDa .The enzyme had its optimal activity at pH 5.0 and exhibited maximal activity at temperature of 50oC. The activity of the enzyme was enhanced by Na+, Ca2+ and ethylene diaminetetraacetic acid (EDTA), while Hg2+ ,Mg2+ and Fe2+ acted as inhibitors of its activity. The beta amylase had an apparent Michaelis constant Km of 5.0 mg/ml and maximum velocity (Vmax) of 50 U/mg proteins.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.