Author/Authors :
-، - نويسنده Plant Biomass Utilization Research Unit, Department of Botany, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand.
Institute of Biochemistry, University of Balochistan, Quetta, 87300, Pakistan Ali, Imran , -، - نويسنده Food Engineering and Bioprocess Technology, School of Environment, Resources and Development, Asian Institute of Technology, Klong Luang, Pathumthani, 12120, THAILAND Akbar, Ali , -، - نويسنده Institute of Biochemistry, University of Balochistan, Quetta, 87300, PAKISTAN Anwar, Muhammad , -، - نويسنده Plant Biomass Utilization Research Unit, Department of Botany, Faculty of Science, Chulalongkorn University, Bangkok, 10330, THAILAND Yanwisetpakdee, Benjawan , -، - نويسنده Plant Biomass Utilization Research Unit, Department of Botany, Faculty of Science, Chulalongkorn University, Bangkok, 10330, THAILAND Prasongsuk, Sehanat , -، - نويسنده Plant Biomass Utilization Research Unit, Department of Botany, Faculty of Science, Chulalongkorn University, Bangkok, 10330, THAILAND Lotrakul, Pongtharin , -، - نويسنده Plant Biomass Utilization Research Unit, Department of Botany, Faculty of Science, Chulalongkorn University, Bangkok, 10330, THAILAND Punnapayak, Hunsa
Abstract :
Background: a-Amylases (EC 3.2.1.1) are covering approximately 25% of total enzyme market and are frequently used in food, pharmaceutical and detergent industries.Objectives: The first ever detailed characterization of amylase from any halophilic Engyodontium album is presented. Materials and Methods: An extracellular α-amylase was studied from halophilic E. album TISTR 3645. The enzyme was extracted and purified by column chromatography. SDS-PAGE was performed to find the molecular weight of the enzyme. The effects of pH, temperature and salinity on the isolated enzyme were determined. The effects of various additives on enzyme were studied.Results: The molecular weight of the amylase was 50 kDa. The enzyme specific activity was 132.17 U.mg-1 with Vmax and Km values of 15.36 U.mg-1 and 6.28 mg.ml-1, respectively. The optimum enzyme activities were found at pH 9.0, 60ºC and 30% (w/v) NaCl. BaCl2, CaCl2, HgCl2 and MgCl2 improved amylase activity. b-mercaptoethanol, EDTA, FeCl2 and ZnCl2 decreased enzyme activity. Conclusions: Polyextremophilic characteristics of a-amylase from halophilic E. album TISTR 3645 were revealed during the characterization studies, demonstrating promising features, making it a useful candidate for various industries.
