The structure and activity of fungal lipases in bile-salt solutions

• Published in: Biophysics (Oxford) 2016-03, Vol.61 (2), p.207-212
• Main Authors: Bogdanova, L. R., Bakirova, D. R., Valiullina, Yu. A., Idiyatullin, B. Z., Faizullin, D. A., Zueva, O. S., Zuev, Yu. F.
• Format: Article
• Language: English
• Subjects: Bile; Biological and Medical Physics; Biophysics; Candida rugosa; Enzymes; Fungi; Molecular Biophysics; Mucor; Physics; Physics and Astronomy; Rhizomucor miehei
• ISSN: 0006-3509; 1555-6654
• DOI: 10.1134/S0006350916020020

The changes in the structure and catalytic properties of fungal lipases ( Candida rugosa , Rhizomucor miehei , Mucor javanicus ) were investigated in micellar solutions of bile salts that differ in their hydrophilic–lypophilic balance and reaction medium properties. The methods of circular dichroism and tryptophan fluorescence were applied to estimate the changes in peptide structure within complexes with bile-salt micelles. Bile salts do not exert a significant influence on the structure of the enzymes under study: in the Rh. miehei and M. javanicus lipases the α-helix content was slightly decreased; an influence of the bile salts on the C. rugosa structure was not revealed. Despite negligible structural modifications in the enzymes, a considerable change in their catalytic properties, namely an abrupt decrease in catalytic effectiveness was observed in bile-salt solutions. Substrate–bile salt micelle complex formation was demonstrated by the NMR self-diffusion method. A model of the regulation of fungal lipase activity was proposed.