Purification and Characterisation of β-Amylase from Bacillus Subtilis Isolated from Fermented African Locust Bean (Parkia biglobosa) Seeds - Volume 3, No.4, October, 2014 - IJLBPR
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Purification and Characterisation of β-Amylase from Bacillus Subtilis Isolated from Fermented African Locust Bean (Parkia biglobosa) Seeds

Abu T F A1, Enujiugha V N1, Sanni D M2, and Bamidele O S2
1. Department of Food Science and Technology, Federal University of Technology, P.M.B 704, Akure, Ondo State, Nigeria
2. Department of Biochemistry, Federal University of Technology, P.M.B 704, Akure, Ondo State, Nigeria
Abstract—β-amylase was obtained from Bacillus subtilis isolated from fermented Parkia biglobosa seeds, purified and characterized. Purification was achieved using ion exchange DEAE column and gel filtration (Sephadex G-200) chromatography. Effects of temperature; pH and production time on β-amylase production were investigated. Also, physicochemical characteristics of the purified enzyme were investigated. The optimum production of β-amylase was at temperature, pH and time of 37°C, 7.0 and 24 h, respectively. The results showed that purified β-amylase had more enzymatic activity than crude samples from Bacillus subtilis whereby the activity of crude enzyme was 3.21 mM/min/mL while the purified enzyme had an improved activity of 21.46 mM/min/mL. Optimum temperature and pH values of the purified amylase were found to be 50°C and 5.0, respectively. pH stability of the enzyme ranged from 4.0- 9.0. At pH 5.0 and 7.0 it retained 70% and 60% of its activity after 5 h of incubation. Temperature stability ranged between 40°C and 70°C but most stable at 50°C retaining 64% of its activity after 1 h of incubation. The enzyme exhibited maximum activity on soluble starch and sucrose, among other carbohydrate substrates. EDTA, Cu2+ and Fe2+ inhibited its activity while Ca2+ and K+ enhanced it up to 30%. The Lineweaver-Burke plot of the purified β-amylase activity of B. subtilis indicates that the β-amylase enzyme has apparent Km and Vmax values for the hydrolysis of soluble starch of 17.74 mg mL-1 and 14.09U, respectively. The enzyme was purified 18.76 -fold and the molecular weight was 42.2 kDa. The study revealed that β-amylase from B. subtilis can be exploited for starch conversion biotechnologies. 

Index Terms—parkia biglobosa, bacillus subtilis, β-amylase, purification, characterization

Cite: Abu T F A, Enujiugha V N, Sanni D M, and Bamidele O S, "Purification and Characterisation of β-Amylase from Bacillus Subtilis Isolated from Fermented African Locust Bean (Parkia biglobosa) Seeds," International Journal of Life Sciences Biotechnology and Pharma Research, Vol. 3, No. 4, pp. 136-151, October 2014.
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