Characterization of membrane-bound lipase from a thermophilic Rhizopus oryzae isolated from palm oil mill effluent

• Main Authors: Abdul Razak, Che Nyonya, Musani, Rosiah, Basri, Mahiran, Salleh, Abu Bakar
• Format: Article
• Language: English; English
• Published: AOCS Press 1999
• Online Access: http://psasir.upm.edu.my/id/eprint/22569/1/Characterization%20of%20membrane-bound%20lipase%20from%20a%20thermophilic%20Rhizopus%20oryzae%20isolated%20from%20palm%20oil%20mill%20effluent.pdf; http://psasir.upm.edu.my/id/eprint/22569/7/J%20Americ%20Oil%20Chem%20Soc%20-%201999%20-%20Razak%20-%20Characterization%20of%20membrane%E2%80%90bound%20lipase%20from%20a%20thermophilic%20Rhizopus%20oryzae.pdf; http://psasir.upm.edu.my/id/eprint/22569/; http://link.springer.com/article/10.1007%2Fs11746-999-0214-0

The characteristics of the membrane-bound lipase from a thermophilic Rhizopus oryzae were studied. The pH and temperature optima for lipase activity were at 7.0 and 37°C, respectively. The enzyme was stable and acidic conditions, retaining more than 80% of its initial activity at pH 4.0 after 30 min incubation. It was stable up to 50°C with 70% of initial activity retained after 3 h incubation. The enzyme is 1,3 specific and exhibits substrate preference. Monoacid triglyceride substrates were hydrolyzed better than methyl esters, polyoxysorbitan and sorbitan substrates.