AJPS  Vol.4 No.10 , October 2013
Chemical Analysis of Carica papaya L. Crude Latex
Abstract: Crude latex of Carica papaya L. has been known to offer a lot of benefits and potentials especially in the agricultural industry and human health. This study focuses on the latex coming from its fruits of Papaya CX variety. Seven to eight longitudinal incisions were made in order to allow latex to appear and drain in the collecting devices. 439.5 g dried latex was stored in plastic containers and freezed. Results showed that dried latex contained higher amount of crude protein (57.24 ± 0.69%), followed by moisture (17.76 ± 0.09%), ash (7.00 ± 0.01%), crude fat (5.21 ± 0.13%) and crude fiber (0.67 ± 0.09%) based on the complete proximate analysis. In the enzyme analysis, papain had protease activity of 2655 units·g-1 at pH 5.5 and 285 units·g-1 at pH 9.0. These results provided evidence that papain as a protease enzyme is found in the crude latex of papaya which is a major constituent in various proteolytic activities. Crude latex from C. papaya L. can be utilized to address the issues in agricultural farms to accelerate production and reduce environmental hazards.
Cite this paper: J. Macalood, H. Vicente, R. Boniao, J. Gorospe and E. Roa, "Chemical Analysis of Carica papaya L. Crude Latex," American Journal of Plant Sciences, Vol. 4 No. 10, 2013, pp. 1941-1948. doi: 10.4236/ajps.2013.410240.

[1]   A. Agrawal and K. Konno, “Latex: A Model for Understanding Mechanisms, Ecology, and Evolution of Plant Defense against Herbivory,” Annual Review of Ecology, Evolution, and Systematics, Vol. 40, No. 15, 2009, pp. 311-331.

[2]   R. L. Harrison and B. C. Bonning, “Proteases as Insecticidal Agents,” Toxins, Vol. 2, No. 5, 2010, pp. 935-953.

[3]   J. R. Kimmel and E. L. Smith, “Crystalline Papain, Part I. Preparation, Specificity, and Activation,” The Journal of Biological Chemistry, Vol. 207, No. 2, 1954, pp. 515-531.

[4]   M. C. Arribere, A. A. Cortadi, M. A. Gattuso, M. P. Bettiol and N. S. Priolo, “Comparison of Asclepiadaceae Latex Proteases and Characterization of Morrenia brachystephana Griseb. Cysteine Peptidases,” Phytochemical Analysis, Vol. 9, No. 6, 1998, pp. 267-273.<267::AID-PCA427>3.0.CO;2-4

[5]   K. R. Lynn and N. A. Clevette-Radford, “Biochemical Properties of Latices from the Euphorbiaceae,” Phytochemistry, Vol. 26, No. 4, 1987, pp. 939-944.

[6]   R. Giordani, A. Moulin and R. Verger, “Tributyroylglycerol Hydrolase Activity in Carica papaya and Other Lattices,” Phytochemistry, Vol. 30, No. 4, 1991, pp. 1069-1072.

[7]   N. Gandhi and N. Mukherjee, “Specificity of Papaya Lipase in Esterification with Respect to the Chemical Structure of Substrates,” Journal of Agricultural and Food Chemistry, Vol. 48, No. 2, 2000, pp. 566-570.

[8]   F. Fiorillo, C. Palocci, S. Simonetta and G. Pasqua, “Latex Lipase of Euphorbia charcias L.: An Aspecific Acylhydrolase with Several Isoforms,” Plant Science, Vol. 172, No. 4, 2007, pp. 722-727.

[9]   S. Zerhouni, A. Amrani, M. Nijs, N. Smolders and M. Azarkan, “Purification and Characterization of Papaya Glutamine Cyclotransferase, a Plant Enzyme Highly Resistant to Chemical, Acid and Thermal de Naturation,” Biochimica et Biophysica Acta, Vol. 1387, No. 1-2, 1998, pp. 275-290.

[10]   M. Azarkan, R. Wintjens, Y. Looze and D. Baeyens-Volant, “Detection of Three Wound-Induced Proteins in Papaya Latex,” Phytochemistry, Vol. 65, No. 5, 2004, pp. 525-534.

[11]   J. W. Purseglove, “Edible Fruits and Nuts, in Tropical Crops, ‘Dicotyledons’,” Longman Publishers, London, 1968.

[12]   J. Janick, “Horticultural Science,” 4th Edition, W.H. Freeman Company Publisher, New York, 1988, pp. 82-83.

[13]   P. Jaiswal, P. Kumar, V. K. Singh and D. K. Singh, “Carica papaya Linn: A Potential Source for Various Health Problems,” Journal of Pharmacy Research, Vol. 3, No. 5, 2010, pp. 998-1003.

[14]   A. El Moussaoui, M. Nijs, C. Paul, R. Wintjens, J. Vincentelli, M. Azarkan and Y. Looze, “Revisiting the Enzymes Stored in the Laticifers of Carica papaya in the Context of Their Possible Participation in the Plant Defense Mechanism,” Cell and Molecular Life Science, Vol. 58, No. 4, 2001, pp. 556-570.

[15]   N. Barouh, S. Abdelkafi, B. Fouquet, M. Michel Pina, F. Frantz Scheirlinckx, F. Carriére and P. Villeneuve, “Neutral Lipid Characterization of Non-Water-Soluble Fractions of Carica Papaya Latex,” Journal of the American Oil Chemists’ Society, Vol. 87, No. 9, 2010, pp 987-995.

[16]   N. O. Chukwuemeka and A. B. Anthonia, “Antifungal Effects of Pawpaw Seed Extracts and Papain on Post Harvest Carica papaya L. Fruit Rot,” African Journal of Agricultural Research, Vol. 5, No. 12, 2010, pp. 1531-1535.

[17]   K. Konno, C. Hirayama, M. Nakamura, K. Tateishi, Y. Tamura, M. Hattori and K. Konno, “Papain Protects Papaya Trees from Herbivorous Insects: Role of Cysteine Proteases in Latex,” Plant Journal, Vol. 37, No. 3, 2004, pp. 370-378.

[18]   S. Nitsawang, R. H. Kaulb and P. Kanasawud, “Purification of Papain from Carica papaya Latex: Aqueous Two-Phase Extraction versus Two-Step Salt Precipitation,” Enzyme and Microbial Technology, Vol. 39, No. 5, 2006, pp. 1103-1107.

[19]   R. Kamalkumar, R. Amutha, S. Muthulaksmi, P. Mareeswari and W. Baby Rani, “Screening of Dioecious Papaya Hybrids for Papain Yield and Enzyme Activit,” Research Journal Agriculture and Biological Sciences, Vol. 3, No. 5, 2007, pp. 447-449.

[20]   O. A. Adu, K. A. Akingboye and A. Akinfemi, “Potency of Pawpaw (Carica papaya) Latex as an Anthelmintic in Poultry Production,” Botany Research Internaional, Vol. 2, No. 3, 2009, pp. 139-142.

[21]   D. Narinesingh and R. Mohammed-Maraj, “Solar Drying Characteristics of Papaya (Carica Papaya) Latex,” Journal of the Science of Food and Agriculture, Vol. 46, No. 2, 1989, pp. 175-186.

[22]   Y. C. Sim, S. G. Lee, D. C. Lee, B. Y. Kang, K. M. Park, J. Y. Lee, M. S. Kim, I. S. Chang and J. S. Rhee, “Stabilization of Papain and Lysozyme for Application to Cosmetic Products,” Biotechnology Letters, Vol. 22, No. 2, 2000, pp. 137-140.

[23]   A. Puig, I. Gil and O. Sánchez, “Evaluation of Drying Techniques Measuring Proteolytic Activity of Papain Obtained from Unripe Fruit and Skin Juice, Universidad de los Andes,” Carrera 1E No. 19 A 40, Bogotá, Colombia, 2008.

[24]   C. Liggieri, W. Obregò, S. Trejo and N. Priolo, “Biochemical Analysis of a Papain-Like Protease Isolated from the Latex of Asclepias curassavica L.,” Acta Biochimica et Biophysica Sinica, Vol. 41, No. 2, 2009, pp. 154-162.

[25]   R. D. Vierstra, “Proteolysis in Plants: Mechanisms and Functions,” Plant Molecular Biology, Vol. 32, No. 1-2, 1996, pp. 275-302.

[26]   A. Bell, “Biochemical Mechanisms of Disease Resistance,” Annual Review of Plant Biology, Vol. 32, No. 3, 1981, pp. 21-81.

[27]   T. Boller, “Roles of Proteolytic in Interactions of Plant with Other Organisms,” In: M. J. Dalling, Ed., Plant Proteolytic Enzymes, CRC Press, Boca Raton, 1986, pp. 67-96.

[28]   E. N. Baker and J. Drenth, “The Cysteine Proteinases Structure and Mechanism,” In: F. Journal and A. Mc Pherson, Eds., Biological Macromolecules and Assemblies, Willey & Sons, New York, 1987, pp. 559-572.

[29]   M. Rao, A. Tanksale, M. Ghatge and V. Deshpande, “Molecular and Biotechnological Aspects of Microbial Proteases, Microbiol,” Molecular Biology Reviews, Vol. 62, No. 3, 1998, pp. 597-635.

[30]   D. A. Campbell and A. K. Szardenings, “Functional Profiling the Proteome with Affinity Labels,” Current Opinion in Chemical Biology, Vol. 7, No. 2, 2003, pp. 296-303.

[31]   R. Alvan der Hogrn and J. D. G. Jones, “The Plant Proteolytic Machinery and Its Role in Defence,” Current Opinion, Plant Biology, Vol. 7, No. 4, 2004, pp. 400-407.

[32]   M. Grudkowska and B. Zagdanska, “Multifunctional Role of Plant Cysteine Proteinases,” Acta Bichimica Polonica, Vol. 51, No. 3, 2004, pp. 609-624.

[33]   K. Brocklehurst, B. S. Baines and M. P. Kierstan, “Papain and Other Constituintes of Carica papaya L. Top,” Enzyme and Fermentation Biotechnology, Vol. 5, No. 5, 1981, pp. 262-235.

[34]   H. A. Chapman, R. J. Riese and G. P. Shi, “Emerging Roles for Cysteine Proteases in Human Biology,” Annual Review of Physiology, Vol. 59, No. 5, 1997, pp. 63-88.

[35]   E. Amri and F. Mamboya, “Papain, a Plant Enzyme of Biological Importance: A Review,” American Journal of Biochemistry and Biotechnology, Vol. 8, No. 2, 2012, pp. 99-104.

[36]   B. S. Baines and K. Brocklehurst, “A Necessary Modification to the Preparation of Papain from Any High-Quality Latex of Carica papaya and Evidence for the Structural Integrity of the Enzyme Produced by Traditional Methods,” Biochemical Journal, Vol. 177, No. 2, 1979, pp. 541-548.

[37]   F. Edwin and M. V. Jagannadham, “Single Disulfide Bond Reduced Papain Exists in a Compact Intermediate State,” Biochemica et Biophysica Acta, Vol. 1479, No. 1-2, 2002, pp. 69-82.

[38]   H. Tsuge, T. Nishimura, Y. Tada, T. Asao and D. Turk, “Inhibition Mechanism of Cathepsin L-Specific Inhibitors Based on the Crystal Structure of Papa Papain-CLIK148 Complex,” Biochemical and Biophysical Research Communications, Vol. 266, No. 2, 1999, pp. 411-416.

[39]   F. Edwin and M. V. Jagannadham, “Single Disulfide Bond Reduced Papain Exists in a Compact Intermediate State,” Biochimica et Biophysica Acta, Vol. 1479, No. 1-2, 2000, pp. 69-82.

[40]   Anonymous, “The Wealth of India. Raw Materials Vol. III: Ca-Ci,” Publications and Information Directorate, CSIR, New Delhi, 1992.

[41]   E. M. Frankel, “Studies on Enzyme Action. XV. Factors Influencing the Proteolytic Activity of Papain,” The Journal of Biological Chemistry, Vol. 31, No. , 1917, pp. 201-215.

[42]   M. Roxas, “The Role of Enzyme Supplementation in Digestive Disorders,” Alternative Medicine Review, Vol. 13, No. 4, 2008, pp. 307-314.

[43]   L. W. Cohen, V. M. Coghlan and L. C. Dihel, “Cloning and Sequencing of Papain-Encoding cDNA,” Gene, Vol. 48, No. 2-3, 1986, pp. 219-227.

[44]   S. Ghosh, “Physicochemical and Conformational Studies of Papain/Sodium Dodecyl Sulfate System in Aqueous Medium,” Colloids and Surfaces A: Physicochemical and Engineering Aspects, Vol. 264, No. 1-3, 2005, pp. 6-16.

[45]   E. D. Stevenson and C. A. Storer, “Papain in Organic Solvents: Determination of Conditions Suitable for Biocatalysis and the Effect on Substrate Specificity and Inhibition,” Biotechnology and Bioengineering, Vol. 37, No. 6, 1991, pp. 519-527.

[46]   A. K. Maiti, S. S. Ahlawat, D. P. Sharma and N. Khanna, “Application of Natural Tenderizers I Meat—A Review,” Agricultural Review, Vol. 29, No. 3, 2008, pp. 226-230.

[47]   M. Frankel, R. Maimin and B. Shapiro, “Hydrolytic Properties of Carica papaya Latex and La Tex Preparations,” Biochemical Journal, Vol. 31, No. 11, 1937, pp. 1926-1933.