Der Pharma Chemica
Journal for Medicinal Chemistry, Pharmaceutical Chemistry, Pharmaceutical Sciences and Computational Chemistry

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Purification and kinetics of Pectinase production from Paenibacillus lactis NRC1 locally isolated from Egyptian mangrove habitat

Author(s): Manal, S Selim, Sahar, S Mohamed, Manal, G Mahmoud, Mohsen, M Asker, and Osama, H El Sayed

Biotechnology is the use of microorganism to perform special industrial process, Therefore The aims of our study were to screen the bacteria that able to produce pectinase enzyme from locally marine by isolation technique. Pectinolytic activity, confirmed by the clear zones on the pectin medium plates. The highest pectinase was identified as Paenibacillus lactis NRC1 which produce 3.20 U/ml after 2 days of incubation at pH 7, 40°C, 5 g/L pectin and yeast extract 1 g/L. The purification fold of the enzyme was 98.718 with final recovery 3.844% using different chromatographic steps. The molecular weight of the purified pectinase determined by SDS-PAGE was 45 kD. The ideal pH was 7 and the enzyme safe up to 40 ºC for 60 min. The Km and Vmax was 0.772 and 7.936 respectively.


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