Production,purification and characterization of an endopolygalacturonase from Mucor rouxii NRRL 1894 |
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| Institution: | 1. Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Paraná, Cx. P. 19046 Centro Politécnico, Curitiba 81531-980, Paraná, Brazil;2. Departamento de Química, Universidade Federal do Paraná, Cx. P. 19081 Centro Politécnico, Curitiba 81531-980, Paraná, Brazil;1. Environmental Science and Engineering, CSIR—Central Leather Research Institute (CLRI), Adyar, Chennai 600020, India;2. Environment & Sustainability, CSIR—Institute of Minerals and Materials Technology, Bhubaneswar, Odisha, India;3. Department of Microbiology, Jaya College of arts and science, Thiruninravur, Chennai, India;1. School of Food Science and Engineering, South China University of Technology, Guangzhou, 510641, China;2. Guangdong Yantang Dairy Co.,Ltd., Guangzhou, 510507, China;1. Environmental & Material Chemistry Laboratory, Department of Chemistry, University of Agriculture, Faisalabad 38040, Pakistan;2. Department of Chemistry, Government College Women University, Faisalabad, Pakistan;3. Industrial Biotechnology Laboratory, Department of Biochemistry, University of Agriculture, Faisalabad 38040, Pakistan |
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| Abstract: | An extracellular polygalacturonase (PGase) from Mucor rouxii NRRL 1894 was purified to homogeneity by two chromatographic steps using CM-Sepharose and Superdex 75. The purified enzyme was a monomer with a molecular weight of 43100 Da and a pI of 6. The PGase was optimally active at 35 °C and at pH 4.5. It was stable up to 30 °C and stability of PGase decrease rapidly above 60 °C. The extent of hydrolysis of different pectins was decreased with increasing of degrees of esterification. Except Mn2+, all the examined metal cations showed inhibitory effects on the enzyme activity. The apparent Km and Vmax values for hydrolyze of polygalacturonic acid (PGA) were 1.88 mg/ml and 0.045 μmol/ml/min, respectively. The enzyme released a series of oligogalacturonates from polygalacturonic acid indicating that it had an endo-action. Its N-terminal sequence showed homologies with the endopolygalacturonase from the psychrophilic fungus Mucor flavus. |
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