Abstract
Herein, we investigate a glucoamylase from newly isolated Aspergillus niger. The enzyme was purified, using fractionation, followed by anion-exchange chromatography and then characterised. The molecular mass of the enzyme was estimated to be ∼62,000Da, using SDS–PAGE and 57151Da, based on mass spectrometry results. The pI of the protein, and optimum pH/temperature of enzyme activity were 4.4, 5 and 70°C, respectively and the kinetic parameters (Km, Vmax and kcat) were determined to be 0.33 (mgml−1), 0.095 (Uμg−1min−1) and 158.3 (s−1) for soluble starch, respectively. The glucoamylase nature of the enzyme was also confirmed using TLC and a specific substrate. Metal ions Fe3+, Al3+ and Hg2+ had the highest inhibitory effect, while Ag2+, Ca2+, Zn2+, Mg2+ and Cd2+ and EDTA showed no significant effect on the enzyme activity. In addition, thermal stability of the enzyme increased in the presence of starch and calcium ion. Based on the results, the purified glucoamylase appeared to be a newly isolated enzyme.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: 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.
