Production Purification Characterization and Applications of Cutinase from Pseudomonas Cepacia Nrrl
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Cutinase has some vital properties of lipase and esterase. Because of its unique nature, it has potential of being an industrially important enzyme. Some of the useful applications of cutinase include hydrolysis of fats and oils, esterification and transesterification reactions. It is used in the food industry for synthesis of flavors, petrochemical industry for synthesis of biodiesel and preparation of some house-hold detergents. At low water activities, transesterification of fats and oils or stereo selective esterification of alcohols can be achieved using cutinase. This enzyme is mainly produced by phytopathogenic fungi, but there are several bacteria, which are known to produce cutinase. In this study, fifteen different microorganisms grown on medium containing Tween 80 or olive oil or cutin, were screened for their possible cutinase producing potential. Cutin, the essential substrate for the production of cutinase, was prepared from tomatoes and characterized. Among fifteen microorganisms, Pseudomonas cepacia NRRL B 2320, Pseudomonas fluorescens NRRL B 3178 and Pseudomonas geniculata NRRL B 1606 were capable of growing on the medium containing cutin as a sole source of carbon and their culture filtrates showed enzyme activity towards p-nitrophenyl butyrate (p-NPB). Cutinase activity was further confirmed by cutinase specific substrate, p-nitrophenyl (16 methyl sulphone ester) hexadecanoate (p-NMSH), where, P. cepacia NRRL B 2320 had shown highest activity of 40 U mg-1 and 41.2 D10-2 U mg-1 towards p-NPB and p-NMSH, respectively. Hence, further studies had been carried out using P. cepacia NRRL B 2320. However, further attempts have been made to replace cutin with different oils, cutin monomer and other carbon sources for the production of cutinase..
Supervisor: V.V. Dasu
BIOSCIENCES AND BIOENGINEERING