Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis

• Main Authors: Salleh, Abu Bakar, Abdul Razak, Che Nyonya, Abd Samad, Mohd Yusoff, Ampon, Kamaruzaman, Wan Yunus, Wan Md. Zin, Basri, Mahiran
• Format: Article
• Language: English
• Published: Penerbit Universiti Kebangsaan Malaysia 1996
• Online Access: http://psasir.upm.edu.my/id/eprint/22573/1/Partial%20purification%20and%20characterization%20of%20lipases%20from%20thermophilic%20Rhizopus%20rhizopodiformis.pdf; http://psasir.upm.edu.my/id/eprint/22573/; http://www.ukm.my/jsm/english_journals/vol25num4_1996/vol25num4_96page131-141.html

Lipase from a newly isolated strain of Rhizopus rhizopodifonnis was partially purified and characterized. By acetone fractionation, the enzyme was purified to about 2.8 fold, with 62.5% recovery and with specific activity of 3.2 U/mg. By gel filtration through Sephadex G-100, the enzyme was further purified to 9.7 fold and had a specific activity of 11.1 U/mg. By polyacrylamide gel electrophoresis, five protein bands were observed after acetone fractionation, white two protein bands were observed after the preparation was passed through Sephadex G-100. It has a pH optimum at 6.0 and a temperature optimum at 45°C. The enzyme is most stable at pH 7.0 and temperature of 50°C. The enzyme has a preference for short chain triglycerides and can also hydrolyse some methyl esters. The lipase is specific for 1,3 positions.