Parameter’s optimization and kinetics study of α-amylase enzyme of Bacillus sp. MB6 isolated from vegetable waste |
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| Institution: | 1. School of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur, Chhattisgarh, India;2. Department of Botany, Govt. DB Girls PG College, Raipur, Chhattisgarh, India;1. Laboratoire de Génie microbiologie et applications, Université Constantine 1, Campus ChaâbatErssas, 25000 Constantine, Algeria;2. Laboratory of Applied Biology and Health, Faculty of Natural Sciences and Life, University Constantine 1, Ain El Bey street, 25000 Constantine, Algeria;1. Key Laboratory of Agricultural Environmental Microbiology, Ministry of Agriculture, College of Life Science, Nanjing Agricultural University, Nanjing, 210095, China;2. Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, 210014, China;3. State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, 211800, China;4. Key Laboratory of Plant Immunity, Nanjing Agricultural University, Nanjing, 210095, China;1. School of Studies in Biotechnology, Pt. Ravishankar Shukla University, Raipur 492010, CG, India;2. Department of Botany, Govt. College, Bichhua, Chhindwara 480111, MP, India |
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| Abstract: | α-Amylase, a very critical enzyme for hydrolysis of starch into simple sugar and it has various applications in industrial settings. This study reports the identification of Bacillus sp. MB6 which produces increased amount of enzyme from less required resources. To optimize the yield of enzyme, we used various combinations of parameters. The most optimized conditions for production of amylase enzyme from the bacterium Bacillus sp. MB6 are pH of 6, temperature of 37 °C, and incubation period of 48 h. Condition of enzymatic activity were also examined and the results show that pH of 6, a temperature of 55 °C, and a reaction time of 30 min are the best available conditions for its activity. Purification of enzyme by 1.63 fold enhanced the specific activity of enzyme based upon its activity analysis as compared with unpurified enzyme. Enzyme kinetics studies show the Michaelis constant (Km) to be 5.45 mg/ml and maximum velocity of the reaction (Vmax) to be 24.15 mg/ml/min. In conclusion, we report enzyme production and purification methodology that exhibit better yield of alpha-amylase for commercial applications. |
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| Keywords: | Enzymatic activity α-Amylase |
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