At low concentration, i.e., (0.03% w/v) Triton X-100 and SLS increased the activity of glucoamylase, while in higher concentration it inhibited activities of both the enzymes. In low amount (1 mM) almost all metal ions except Mn, such as Ca 2+, Co 2+, Cu 2+, Fe 3+, Mg 2+, Zn 2+ and Hg 2+ enhanced glucoamylase activity whereas protease activity was inhibited by all the ions except Zn 2+. K m and V max of glucoamylase and protease were 9.8 mg/ml, 56.2 mg/ml/min and 1.08 mg/ml, 8.8 mg/ml/min, respectively. Half life of glucoamylase was 210, 120, 60 and 35 min at 50, 60, 70 and 80 ☌, respectively, which was 150, 120, 65 and 15 min at 40, 50, 60 and 70 ☌, respectively, for acid protease. Optimum activities of amylase and protease were obtained at pH 4 and 5, respectively, whereas 70 and 55 ☌ had been found as most suitable temperature for highest activities of amylase and protease, respectively. Both the enzymes were found stable in wide range of pH (3–9) and temperature (25–70 ☌).
The aim of this study was to characterize the glucoamylase and acid protease produced in a single bioreactor by Aspergillus awamori: nakazawa MTCC 6652.
