Effect of water content and temperature onCarica papayalipase catalyzed esterification and transesterification reactions (original) (raw)
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Characterization of the lipase from Carica papaya residues
Braz. J. Food. Technol. Preprint Serie, 2008
Lipases from vegetable sources have been the focus of intense and growing research. The use of enzymes from plants has the advantage of employing industrial waste products. Brazil is the world's largest papaya producer and the market for products derived from papaya is growing year after year. In this study, the authors carried out the characterization and partial purification of the lipase obtained from the seeds and skin of Carica papaya. The most active fractions were those obtained using the technique of precipitation with 50% of acetone (EBFL-50 acetone), and the technique of fractioned precipitation with ammonium sulphate 40-80% (EBFL-40-80 sulphate). The EBFL-50 acetone fraction presented an optimum pH at 9.5, with a second peak of activity at pH 4.5, and optimal temperature at 55 ºC. The fraction was stable at pH values between 8.5 and 10.0 and temperatures from 30 to 60 °C and from 90 to 100 °C. The EBFL-40-80 sulphate fraction had an optimum pH at 9.0, with a second peak at pH 6.0, and an optimum temperature at 55 °C, being stable at pH values between 6.0 and 9.0 and temperatures from 60 to 90 °C. The thermal stability of the EBFL-40-80 sulphate fraction changed to the range between 30 and 70 °C in the presence of the protease inhibitor phenylmethanosulfonyl fluorate (PMSF). The thermal stability of the fraction EBFL-50 acetone did not change in the presence of PMSF. The best esterification activity was observed in the presence of stearic acid after 48 h for the EBFL-50 acetone fraction.
Potravinarstvo Slovak Journal of Food Sciences, 2019
Most of industrial lipases are derived from microbial sources, following by a wide variety of plants. Among plant lipases, lipase from Carica papaya latex has been the focus of intense and growing research due to low cost, easy acceptance by consumers and its unique characteristics. This enzyme has been successfully applied for lipid modification and synthesis of some organic compounds. However, research for its molecular structure has been limited due to the difficulty to isolate the enzyme from the latex matrix. In this study, we suggested a modified approach using sodium lauroyl sarcosinate to solubilize the latex, then the protein was precipitated by ammonium sulphate. We also carried out the characterization of the lipase obtained from Carica papaya latex. The results showed that freeze-drying the fresh latex could improve significantly lipase activity of latex powder in comparison with sun-drying or oven-drying. The zwitterion sodium lauroyl sarcosinate could solubilize nearly...
Oléagineux, Corps gras, Lipides, 2003
L'activité lipasique du latex brut de la plante subtropicale de Babaco ( Carica pentagona est étudiée dans des réactions d'alcoolyse et d'estérification. Les résultats indiquent que le latex brut de Carica pentagona présente des propriétés biocatalytiques équivalentes au latex brut de Carica papaya dans des réactions de synthèse telles que l'alcoolyse de triacylglycérols et la réaction d'estérification (les rendements de réaction sont respectivement 72,3 % et 70,2 % après 3 h pour l'alcoolyse et 31,8 % et 33,8 % après 24 h pour la réaction d'estérification). Par contre, la papaïne brute commerciale donne des rendements de réaction beaucoup plus bas que les latex bruts des deux espèces de Carica (28,9 % en alcoolyse et 5,4 % en estérification).
Biocatalytic properties of lipase in crude latex from babaco fruit (Carica pentagona)
2001
Biocatalytic activities in proteolysis, lipolysis and interesterification reactions were studied for crude latex from the subtropical plant Carica pentagona. The results reveal that crude Carica pentagona latex exhibits equivalent proteolytic activities (5.73 units mg-1) and lipolytic activities (1.01 units mg-1) compared to the well-known Carica papaya, the commercially source for papain (4.57 units mg-1 and 0.90 units mg-1 respectively). Therefore,
Biotechnology and Bioengineering, 2002
Adsorption and desorption isotherms of two commercial enzyme preparations of papain and bromelain were determined with a Dynamic Vapor System. The Guggenheim-Anderson-deBoer (GAB) modeling of the obtained sorption isotherms allowed the de®nition of different levels of hydration of those samples. Afterward, these enzyme preparations were used as biocatalysts in water and solvent-free esteri®cation and alcoholysis reactions. The evolution of the obtained fatty acid ester level as a function of the initial hydration level of the biocatalyst, i.e., thermodynamic water activity (a w ) and water content, was studied. The results show an important correlation between the initial hydration level of the biocatalyst and its catalytic activity during the lipasecatalyzed synthesis reactions. Thus, the Carica papaya lipase (crude papain preparation) catalytic activity is highly dependent on the biocatalyst hydration state. The optimized synthesis reaction yield is obtained when the a w value of the enzyme preparation is stabilized at 0.22, which corresponds to 2% water content. This optimal level of hydration occurs on the linear part of the biocatalyst's sorption isotherm, where the water molecules can form a mono-or multiple layer with the protein network. The synthesis reaction yield decreases when the a w of the preparation is higher than 0.22, because the excess water molecules modify the system equilibrium leading to the reverse and competitive reaction, i.e., hydrolysis. These results show also that an optimal storage condition for the highly hydrophilic crude papain preparation is a relative humidity strictly lower than 70% to avoid an irreversible structural transition leading to a useless biocatalyst. Concerning the bromelain preparation, no effect of the hydration level on the catalytic activity during esteri®cation reactions was observed. This biocatalyst has too weak a catalytic activity which makes it dif®cult to observe any differences. Furthermore, the bromelain preparation is far more hydrophobic as it adsorbs only 18 g of water per 100 g of dry material at a w around 0.90. No deliquescence of this enzymatic preparation is oserved at this a w value.
Carica papaya lipase (CPL): An emerging and versatile biocatalyst
Biotechnology Advances, 2006
In recent years, the Carica papaya lipase (CPL) is attracting more and more interest. This hydrolase, being tightly bonded to the water-insoluble fraction of crude papain, is thus considered as a "naturally immobilized" biocatalyst. To date, several CPL applications have already been described: (i) fats and oils modification, derived from the sn-3 selectivity of CPL as well as from its preference for short-chain fatty acids; (ii) esterification and inter-esterification reactions in organic media, accepting a wide range of acids and alcohols as substrates; (iii) more recently, the asymmetric resolution of different non-steroidal antiinflammatory drugs (NSAIDs), 2-(chlorophenoxy)propionic acids, and non-natural amino acids. Taking into account the novelty and the current interest of the topic, this review aims to highlight the origin, features, and applications of the C. papaya lipase, with the objective to prompt research groups to further investigate the spectra of applications that this emerging and versatile CPL could have in the future.
Investigation of crude latex from various Carica papaya varietices for lipid bioconversions
Journal of the American Oil Chemists' Society, 2000
The protein contents in crude latices from various varieties of papaya (Carica papaya) and their catalytic activities in proteolysis, lipolysis, and interesterification reactions were studied with regard to the variety, the geographic location of cultures, and the frequency of fruit tapping. Biocatalytic activities of these raw materials were compared to several commercially available crude and purified preparations of papain. These investigations were carried out in order to have a better physicochemical characterization of these raw materials, to select the adequate papaya latex for protein or lipid bioconversions, and to valorize them on an industrial scale. For the purified preparations of papain, only proteolytic activity was obtained. All crude papaya latices exhibit proteolytic, lipolytic, and interesterification activities, and no relationship between the proteolytic and lipolytic activities was observed. The high multiple correlation coefficient (R) on the order of R = 0.93-0.99, obtained from the regression analysis for the lipolytic and interesterification activities for all crude papaya latices investigated suggested that there was a correlation between these enzyme activities. However, for the same lipase preparation, the interesterification activity differed substantially depending on the type of interesterification reaction.