Application of Bromelain Extract for Muscle Foods Tenderization

Sunantha Ketnawa, Saroat Rawdkuen

.
Food Technology Program, School of Agro-Industry, Mae Fah Luang University, Muang, Chiang Rai, Thailand..

DOI: 10.4236/fns.2011.25055                

Abstract

This study investigates the tenderizing effects of bromelain extract (BE) obtained from the top phase of an aqueous two-phase system comprising of 18% PEG 6000–17% MgSO₄ in muscle foods. Uniform-sized chunks of beef, chicken, and squid were marinated with different concentrations of BE (0, 3, 7%, and 20%, w/w) for 1 h at room temperature. The physico-chemical and quality characteristics of the marinated samples were determined. Decreases in pH and moisture content were observed in the samples BE treated, but the TCA-soluble peptides content significantly increased (p < 0.05). Water holding capacity and cooking yields were observed in all of the tested samples, especially when the concentration of BE increased. In addition, a reduction of meat firmness and toughness were also observed in all of the samples when compared to the control (p < 0.05). Electrophoretic patterns also revealed extensive proteolysis and a reduction in number and intensity of the protein bands in all of the treated samples. At the microstructural level, tissue fibers were broken, cell membranes were more strongly degraded, the connections between the sarcolemma and the myofibrils were disappeared, and the generation of numerous gaps could be clearly observed when 20% (w/w) BE was added. The results show that the bromelain extract derived from the two-phase extraction of a pineapple peel could be used as an effective meat tenderizer.

Keywords

Bromelain, Pineapple Peel, Aqueous Two Phase System, Muscle Food, Meat Tenderization

Conflicts of Interest

The authors declare no conflicts of interest.

References

[1]	C. M. Kemp, P. L. Sensky, R. G. Bardsley, P. J. Buttery and T. Parr, “Tenderness: an Enzymatic View,” Meat Science, Vol. 84, No. 2, 2010, pp. 248-256. doi:10.1016/j.meatsci.2009.06.008
[2]	Q. H. Chen, G. Q. He, Y. C. Jiao and H. Ni, “Effects of Elastase from a Bacillus Strain on the Tenderization of Beef Meat,” Food Chemistry, Vol. 98, No. 4, 2006, pp. 624-629. doi:10.1016/j.foodchem.2005.06.043
[3]	J. A. Melendo, J. A. Beltrin and P. Roncales, “Tenderization of Squid (Loligo Vulgaris and Illex Coindetii) with Bromelain and Bovine Spleen Lysosomal-enriched Extract,” Food Research International, Vol. 30, No. 5, 1997, pp. 335-341. doi:10.1016/S0963-9969(97)00057-4
[4]	I. N. A. Ashie, T. L. Sorensen and P. M. Nielsen, “Effects of Papain and a Microbial Enzyme on Meat Proteins and Beef Tenderness,” Journal of Food Science, Vol. 67, No. 6, 2002, pp. 2138-2142. doi:10.1111/j.1365-2621.2002.tb09516.x
[5]	M. Wada, T. Suzuki, Y. Yaguti and T. Hasegawa, “The Effect of Pressure Treatments with Kiwi Fruit Protease on Adult Cattle Semitendinosus Muscle,” Food Chemistry, Vol. 78, No. 2, 2002, pp. 167-171. doi:10.1016/S0308-8146(01)00395-8
[6]	B. M. Naveena, S. K. Mendiratta and A. S. R. Anjaneyulu, “Tenderization of Buffalo Meat Using Plant Proteases from Cucumis Trigonus Roxb (Kachri) and Zingiber Officinale Roscoe (Ginger Rhizome),” Meat Science, Vol. 68, No. 3, 2004, pp. 363-369. doi:10.1016/j.meatsci.2004.04.004
[7]	V. D. Pawar, B. D. Mule and G. M. Machewad, “Effect of Marination with Ginger Rhizome Extract on Properties of Raw and Cooked Chevon,” Journal of Muscle Foods, Vol. 18, No. 4, 2007, pp. 349-369. doi:10.1111/j.1745-4573.2007.00091.x
[8]	Z. Pietrasik, J. L. Aalhus, L. L. Gibson and P. J. Shand, “Influence of Blade Tenderization, Moisture Enhancement and Pancreatin Enzyme Treatment on the Processing Characteristics and Tenderness of Beef Semitendinosus muscle,” Meat Science, Vol. 84, No. 3, 2010, pp. 512-517. doi:10.1016/j.meatsci.2009.10.006
[9]	B. Gerelt, Y. Ikeuchi and A. Suzuki, “Meat Tenderization by Proteolytic Enzymes after Osmotic Dehydration,” Meat Science, Vol. 56, No. 3, 2000, pp. 311-318. doi:10.1016/S0309-1740(00)00060-7
[10]	K. Palka, “Changes in Intramuscular Connective Tissue and Collagen Solubility of Bovine M. Semitendinosus during Retorting,” Meat Science, Vol. 53, No. 3, 1999, pp. 189-194. doi:10.1016/S0309-1740(99)00047-9
[11]	J. R. Claus, J. K. Schilling, N. G. Marriott, S. E. Duncan, M. B. Solomon and H. Wang, “Tenderization of Chicken and Turkey Breasts with Electrically Produced Hydrodynamic Shockwaves,” Meat Science, Vol. 58, No. 3, 2001, pp. 283-286. doi:10.1016/S0309-1740(01)00027-4
[12]	A. Sriwatanapongse, M. Balaban and A. Teixeira, “Thermal Inactivation Kinetics of Bromelain in Pineapple Juice,” Journal of American Society of Agricultural Engineers, Vol. 43, No. 6, 2000, pp. 1703-1708.
[13]	L. Huang, H. Z. Qu, L. Zhang, S. S. Du, S. Yang, D. Y. Hao and X. P. Wang, “Purification and Characterization of a Proteolytic Enzyme from Fig Latex,” Journal of Chemistry, Vol. 24, No. 3, 2008, pp. 348-352.
[14]	J. Dreuth, J. Jansonius, R. Koekoek, H. Swen and B. Wolters, “Structure of Papain,” Nature, Vol. 218, 1968, pp. 929-932. doi:10.1038/218929a0
[15]	E. H. Thompson, I. D. Wolf and C. E. Allen, “Ginger Rhizome: a New Source of Proteolytic Enzyme,” Journal of Food Science, Vol. 38, No. 4, 1973, pp. 652-655. doi:10.1111/j.1365-2621.1973.tb02836.x
[16]	S. Ketnawa, S. Sai-Ut, T. Theppakorn, P. Chaiwut and S. Rawdkuen, “Partitioning of Bromelain from Pineapple peel (Nang Lae cultv.) by Aqueous Two Phase System,” Asian Journal of Food & Agro-Industry, Vol. 2, No. 4, 2009, pp. 457-468.
[17]	M. Espe, K. Ruohonen, M. Bjornevik, L. Froyland, R. Nortvedt and A. Kiessling, “Interactions between Ice Storage Time, Collagen Composition, Gaping and Textural Properties in Farmed Salmon Muscle Harvested at Different Times of the Year,” Aquaculture, Vol. 240, No. 1-4, 2004, pp. 489-504. doi:10.1016/j.aquaculture.2004.04.023
[18]	F. B. Wardlaw, L. H. Maccaskill and J. C. Acton, “Effect of Postmortem Muscle Changes in Poultry Meat Loaf Properties,” Journal of Food Science, Vol. 38, No. 3, 1973, pp.421-424. doi:10.1111/j.1365-2621.1973.tb01444.x
[19]	AOAC, “Official Methods of Analysis,” 16th Edition, Association of Official Analysis Chemists, Washington DC, 2000.
[20]	S. Benjakul, W. Visessanguan, S. Riebroy, S. Ishizaki and M. Tanaka, “Gel-forming Properties of Surimi Produced from Bigeye Snapper, Priacanthus Tayenus and P.macracanthus, Stored in Ice,” Journal of the Science of Food and Agriculture, Vol. 82, No. 13, 2002, pp. 1442-1451. doi:10.1002/jsfa.1207
[21]	Q. H. Lowry, N. J. Rosebrough, L. A. Farr and R. J. Randall, “Protein Measurement with the Folin Phenol Reagent,” Journal of Biological Chemistry, Vol. 193, No. 1, 1951, pp.256-275.
[22]	U. K. Laemmli, F. Beguin and G. Gujer-Kellenberger, “A Factor Preventing the Major Head Protein of Bacteriophage T4 from Random Aggregation,” Journal of Molecular Biology, Vol. 47, No. 1, 1970, pp. 69-74. doi:10.1016/0022-2836(70)90402-X
[23]	B. M. Naveena, “The Tenderization of Buffalo Meat Using Ginger Extract,” Journal of Muscle Foods, Vol., 15, No. 4, 2004, pp. 235-244. doi:10.1111/j.1745-4573.2004.06403.x
[24]	K. S. Ziauddin, D. N. Rao and B. L. Amla, “Effect of Lactic Acid, Ginger Extract and Sodium Chloride on Electrophoretic Pattern of Buffalo Muscle Proteins,” Journal of Food Science and Technology, Vol. 32, No. 3, 1995, pp. 224-226.
[25]	B. M. Naveena and S. K. Mendiratta, “Tenderization of Spent Hen Meat Using Ginger Extract,” British Poultry Science, Vol. 42, No. 3, 2001, pp. 344-350. doi:10.1080/00071660120055313
[26]	J. C. Forrest, E. D. Aberle, H. B. Hedrick, M. D. Judge and R. A. Merkel, “Principles of Meat Science,” Iowa: Kendall/Hunt Publishing Company, 1994.
[27]	S. T. Joo, R. G. Kauffman, B. C. Kim and G. B. Park, “The relationship of Sarcoplasmic and Myofibrillar Protein Solubility to Colour and Water-holding Capacity in Porcine Longissimus Muscle,” Meat Science, Vol. 52, No. 3, 1999, pp. 291-297. doi:10.1016/S0309-1740(99)00005-4
[28]	E. Huff-Lonergan and S. M. Lonergan, “Mechanism of Water Holding Capacity of Meat: The Role of Postmortem Biochemical and Structural Changes,” Meat Science, Vol. 71, No. 1, 2005, pp. 194-204. doi:10.1016/j.meatsci.2005.04.022
[29]	T. Goli, P. A. Nakhoul, N. Zakhia-Rozis, G. Trystram and P. Bohuon, “Chemical Equilibrium of Minced Turkey Meat in Organic Acid Solutions,” Meat Science, Vol. 75, No. 2, 2007, pp. 308-314. doi:10.1016/j.meatsci.2006.07.016
[30]	N. F. S. Gault, “The Relationship between Water-Holding Capacity and Cooked Meat Tenderness in Some Beef Muscles as Influenced by Acidic Conditions below the Ultimate pH,” Meat Science, Vol. 15, No. 1, 1985, pp. 15-30. doi:10.1016/0309-1740(85)90071-3
[31]	S. Rawdkuen, P. Pintathong, P. Chaiwut and S. Benjakul, “The Partitioning of Protease from Calotropis Procera Latex by Aqueous Two-Phase Systems and Its Hydrolytic Pattern on Muscle Proteins,” Food and Bioproducts Processing, Vol. 50, No. 3, 2010, pp. 145-149.
[32]	A. J. Miller, E. D. Strange and R. C. Whiting, “Improved Tenderness of Restructured Beef Steaks by a Microbial Collagenase Derived from Vibrio B-30,” Journal of Food Science, Vol. 54, No. 4, 1989, pp. 855-857. doi:10.1111/j.1365-2621.1989.tb07898.x
[33]	S. Schiaffino and C. Reggiani, “Molecular Diversity of Myofibrillar Proteins: Gene Regulation and Functional Significance,” Physiology Reviews, Vol. 76, No. 2, 1996, pp. 371-423.
[34]	E. Huff-Lonergan, F. C. Parrish and R. M. Robson, “Effects of Postmortem aging Time, Animal Age and Sex on Degradation of Titin and Nebulin in Bovine Longissimus Muscle,” Journal of Animal Science, Vol. 73, No. 4, 1995, pp. 1064-1073.
[35]	E. Bandman and D. Zdanis, “An Immunological Method to Assess Protein Degradation in Postmortem Muscle,” Meat Science, Vol. 22, No. 1, 1988, pp. 1-19. doi:10.1016/0309-1740(88)90023-X
[36]	J. C. Sawdy, S. A. Kaiser, N. R. St-Pierre and M. P. Wick, “Myofibrillar 1-D Fingerprints and Myosin Heavy Chain MS Analyses of Beef Loin at 36 h Postmortem Correlate with Tenderness at 7 Days,” Meat Science, Vol. 67, No. 3, 2004, pp. 421-426. doi:10.1016/j.meatsci.2003.11.014
[37]	N. Bhaskar, N. M. Sachindra,V. K. Modi, P. Z. Sakhare and N. S. Mahendrakar, “Preparation of Proteolytic Activity Rich Ginger and Evaluation of Its Tenderizing Effect of Spent-hen Muscles,” Journal of Muscle Foods, Vol. 17, No. 2, 2006, pp. 174-184. doi:10.1111/j.1745-4573.2006.00043.x
[38]	V. K. Jorgova, S. Danchev and A. Kostov, “Effect of Bacterial Enzyme Preparation on the Solubility and Electrophoretic Properties of Muscle Proteins,” Proceedings International Congress of Meat Science and Technology, Vol. 35, 1989, pp. 913-917.