Abstract
Colletotrichum gloeosporioides was evaluated for its capacity to produce extracellular lipase. A crude enzyme preparation obtained after 48 h of fermentation reached 742 U/L of lipolytic activity. Estimated molecular weight of proteins responsible for this activity was about 18 kDa as determined by SDS-PAGE and zymogram analysis. Enzyme preparation showed optimum pH at 10 and stability at optimum temperature (37°C) for 5 h. It showed tolerance to a wide range of salts (NH4+, Mg+2, Ca+2, Mn+2 and Sn+2) and to some solvents (methanol, ethanol, isopropanol, 1-butanol, acetonitrile n-heptane and n-hexane) in different concentrations. The crude enzyme preparation was applied in hydrolysis reactions on different substrates (waste cooking soybean oil, cocoa butter and palm kernel oil) reaching high yields (87.6; 80.1; 74.9%, respectively). The preparation was lyophilized and it was applied in the synthesis of pineapple flavor, by esterification with butanol and butyric acid. C. gloeosporioides lipolytic enzymes synthesized butyl butyrate with 70% yield, in experiments carried out for 24 h using 1:1 acid/alcohol molar ratio in n-heptane medium. The lyophilized preparation was also able to perform transesterification of alcohols and p-nitrophenyl palmitate in organic medium (n-hexane), showing better activity when propanol was used (5.4.10-3 U/kg.min). This study pointed the potential of alkaline lipolytic enzyme produced by C. gloeosporioides in biotechnological industry. Key words: Lipase, Colletotrichum gloeosporioides, hydrolysis, esterification, transesterification.
Highlights
Lipases are hydrolases (E.C. 3.1.1.3) widely distributed in nature
Half-life of the enzyme occurred after 5 h of incubation, with sharp decline after this period. These results show a special behavior of C. gloeosporioides lipase
The results showed that C. gloeosporioides lipase have broad hydrolytic activity, corroborating with literature for lipases from other sources (Chen et al, 2007; Balaji and Ebenezer, 2008)
Summary
Lipases are hydrolases (E.C. 3.1.1.3) widely distributed in nature. These enzymes, in association with cutinases and others esterases, play an important role in the biological cycling of lipids (Villeneuve et al, 2000). They are versatile biocatalysts that catalyze the breakdown of triglycerides with release of diacylglycerols, monoacylglycerols and glycerol They usually show good chemoselectivity, regioselectivity and enantioselectivity, acting over a wide range of temperatures (Joseph et al, 2008). Its catalytic employment covers different areas such as obtaining food and esters used as flavors, production of detergents, application in optically active drugs resolution, production of fine chemicals, agrochemicals, biopolymers, as well as in use as biosensors, in bioremediation, and, even, for cosmetics and perfumes production (Hasan et al, 2006; Joseph et al, 2008)
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
