Effect of nonionic detergents on the activity of a thermostable lipase from Bacillus stearothermophilus MC7

• Published in: Journal of molecular catalysis. B, Enzymatic Enzymatic, 2007-11, Vol.49 (1), p.88-91
• Main Authors: Guncheva, M., Zhiryakova, D., Radchenkova, N., Kambourova, M.
• Format: Article
• Language: English
• Subjects: Activation; Bacillus stearothermophilus; Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Freeze-drying; Fundamental and applied biological sciences. Psychology; Methods. Procedures. Technologies; Nonionic detergents; Thermophilic lipase
• ISSN: 1381-1177; 1873-3158
• DOI: 10.1016/j.molcatb.2007.08.010

The influence of nonionic surfactants on the activity of a novel thermostable lipase from Bacillus stearothermophilus MC7 was investigated with a view to its potential for synthesis of structured lipids. A large number of modifiers within a broad concentration range were applied. The activity of the enzyme was measured at a relatively high reaction temperature. Highest degree of activation was observed when PEG 6000 was applied (up to 2.3-fold increase). Modification essentially changed the performance of the lyophilised preparations—they keep up to 80% of the activity of the native enzyme in the presence of a detergent against 30% in its absence. The effect of sorbitan esters (spans) and polyoxyethylene derivatives of sorbitan esters (tweens) on lipase MC7 was estimated, their HLB value varying within the interval 2.1–16.7. Tweens were strong inhibitors at higher concentrations. For all spans, excepting span 60, an increase of enzyme activity with concentration was observed. All studied additives slow down the process of thermal denaturation. Lipase preparations preserve more than 60% of their activity after 30-min incubation at 75 °C in the presence of tween 60 or PEG 4000.