Abstract
Eight industrial lipases were tested for cutinase activity on apple (Malus pumila cv. Golden Delicious) cutin and compared with cutinase from the fungus Fusarium solani f. sp pisi. The analysis of released cutin monomers was performed by normal‐phase h.p.l.c with an evaporative light‐scattering detector. Calibration curves of cutin monomers were established for quantification of cutinolytic activity of the industrial lipases. The pH optimum for cutinase activity of the lipase preparations was approx. 8.0. A high concentration of detergent was necessary for expression of cutinase activity. The most active lipase was found to be Amano PS‐800, which was capable of hydrolysing 16% of apple cutin.
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