Candida and Pseudomonas Lipase-Catalyzed Hydrolysis of Butteroil in the Absence of Organic Solvents

Candida rugosa lipase (CRL) and Pseudomonas fluorescein lipase (PFL) were used to hydrolyze a low-melting point butteroil fraction in the absence of orgaic solvents. CRL and PFL displayed pH activity optima of 6.7 and 7.8, and temperature-activity optima of 40–50°C and 35°C, respectively. Maximum activity for PFL was observed at 5% (v/v) water content. CRL showed higher specificity towards butyric acid relative to PFL after 3 hours of hydrolysis at 40°C (22.3 mol% vs 7.8 mol%, respectively). Both enzymes displayed, however, high specificities towards palmitic and oleic acids. CRL's inherent specificity towards butyric acid makes it an ideal choice for a biological catalyst to generate useful dairy flavor profiles.