Purification and Properties of Lipoprotein Lipase from Rhizopus japonicus

抄録

Lipoprotein lipase (LPL) and lipase activities from Rhizopus japonicus KY 521 were separated into two peaks by Sephadex G-100 gel filtration. Peak I (LPL) with higher LPL activity than lipase activity was further purified by chromatography on hydroxylapatite, gel filtration on Sephadex G-150 and isoelectric focusing. The purified enzyme had LPL activity and lipase activity in a ratio of 1.5:1. The two activities showed similar catalytic properties; they could hydrolyzed tricaprin most rapidly among triglycerides tested, had an optimum pH around 8.3 and were stable in the pH range of 5 to 7 and up to 50°C with treatment for 15 min. However, the LPL activity of the purified enzyme was strongly inhibited by NaCl and protamine, whereas lipase activity was enhanced by them.