Effect of Freeze-thaw Cycles and Papain Treatments on Quality of Pork
Abstract
The objective of this research was to study the effect of freeze-thaw processes and papain treatment to improve the tenderness of pork. The pork samples were frozen-thawed for 0, 1, 3, and 5 cycles before immersed in 0.5% papain solution. The pH, water holding capacity, drip loss, cooking loss, total exudate loss, moisture, texture, and color of the samples were evaluated. The result showed that the drip loss increased as the number of freeze-thaw cycles increased from 0.49 to 5.21 g/100g. The immersion in papain solution slightly decreased pH of the samples (p<0.05). The freeze-thaw for 5 cycles combined with the immersion in papain solution for 2 hr greatly decreased water holding capacity and moisture content of the samples while the highest increased in cooking loss and total exudate loss were observed (p<0.05). The samples which were frozen and thawed previously immersed in papain solution had a lower hardness value than the enzyme-treated samples without freezing. However, no significant difference in shear force was observed (p>0.05). The freeze-thaw for 3 and 5 cycles before immersion in the enzyme solution resulted in the lowest chewiness (p<0.05). The sample which was frozen-thawed for 3 cycles before immersed in enzyme solution had lightness, redness, and yellowness value similar to the control sample and had lower total exudate loss than the sample that has been frozen and thawed for 5 cycles before immersed in the enzyme solution. Therefore, the frozen-thaw for 3 cycles before immersed in 0.5% papain solution was the most suitable method for improving the texture of pork. Keywords : pork, papain, freezing, tenderness, water holding capacityReferences
Abdel-Naeem, H.H., & Mohanmed, H.M. (2016). Improving the physico-chemical and sensory characteristics of camel burger patties using ginger extract and papain. Meat Science, 118, 52-60.
Ali, S., Zhang, W., Rajput, N., Khan, M. A., Li, C.B., & Zhou, G.H., (2015). Effect of multiple freeze-thaw cycles on the quality of chicken breast meat. Food Chemistry, 173, 808-814.
AOAC. (1990). Official Method of Analysis. (15th). Virginia: The Association of Official Analysis Chemical Chemists.
Aroeira, C.N., Filho, R.A.T, Fontes, P.R., Gomide, L.A.M., Ramos, A.L.S., Ladeira, M.M., & Ramos, E.M. (2016). Freezing, thawing and aging effects on beef tenderness from Bos indicus and Bos Taurus cattle. Meat Science, 166, 118-125.
Astruc, T. (2014). Muscle structure and digestive enzyme bioaccessibility to intracellular compartments. In M. Boland, M. Golding & H. Singh. (Eds.), Food Structures, Digestion and Health. (pp. 193-222). San Diego: Academic Press.
Buyukyavuz, A. (2014). Effect of Bromelain on Duck Breast Meat Tenderization. Retrieved April 20, 2019, from https://tigerprints.clemson.edu/all_theses/1929.
Dias, J., Nunes, M.L., & Mendes, R. (1994). Effect of frozen storage on the chemical and physical properties of black and silver scabbard fish. Journal of the Science of Food and Agriculture, 66, 327–335.
Gokoglu, N., Yerlikaya, P., Ucak, I., & Yatmaz, H.A. (2016). Effect of bromelain and papain enzymes addition on physicochemical and textural properties of squid (Loligo vulgaris). Journal of Food Measurement and Characterization, 11(1), 347-353.
Ha, M., Bekhit, A.E.-D.A., Carne, A., & Hopkins, D.L. (2012). Characterisation of commercial papain, bromelain, actinidin and zingibain protease preparations and their activities toward meat proteins. Food Chemistry, 134(1), 95-105.
Huidobro, F.R.D., Miguel, E., Blázquez, B., & Onega, E. (2005). A comparison between two methods (Warner–Bratzler and Texture Profile Analysis) for testing either raw meat or cooked meat. Meat Science, 69(3), 527-536.
Kemp, C.M., Sensky,P.L., Bardsley, R.G., Buttery, P.J., & Parr, T. (2010). Tenderness – an enzymatic view.
Meat Science, 84(2), 248-256.
Ketnawa, S., & Rawdkuen, S. (2011). Application of bromelain extract for muscle foods tenderization.
Food and Nutrition Sciences, 2, 393-401.
Kim, G.D., Jung, E.Y., Lim, H.Y., Yang, H.S., Joo, S.T., & Jeong, J.Y. (2013). Influence of meat exudates
on the quality characteristics of fresh and freeze-thawed pork. Meat Science, 95, 323-329.
Leygonie, C., Britz, T.J., & Hoffman, L.C. (2012). Impact of freezing and thawing on the quality of meat :
Review. Meat Science, 91, 93-98.
Liu, C., Xiong, Y.L., & Rentfrow, G.K. (2011). Kiwifruit protease extract injection reduces toughness of pork
loin muscle induced by freeze-thaw abuse. LWT- Food Science and Technology, 44, 2026-2031.
Mackie, I.M. (1993). The effects of freezing on flesh protein. Food Reviews International, 9, 575-700.
National statistics office Thailand. (2018). Report on the 2017 survey of the older persons in Thailand.
Bangkok: National statistics office Thailand, Ministry of digital economy and society. (in Thai)
Nontaloon, K, & Sirijariyawat, A. (2018). Effect of type and concentration of enzyme on meat tenderness.
Khon Kaen Agriculture Journal, 46(Supplement 1), 100-105. (in Thai)
Pawar, V.D., Mule, B.D., & Machewad, G.M. (2007). Effect of marination with ginger rhizome extract on
properties of raw and cooked chevon. Journal of Muscle Foods, 18(4), 349-369.
Purslow, P., Oiseth, S., Hughes, J., & Warner, R. (2016). The structural basis of cooking loss in beef: variations with temperature and ageing. Food Research International, 89, 739-748.
Qi, J., Li, C., Chen, Y., Gao, F., Xu, X., & Zhou, G. (2012). Changes in meat quality of ovine longissimus dorsi muscle in response to repeated freeze and thaw. Meat Science, 92(4), 619-626.
Rawdkuen, S., Jaimakreu, M., & Benjakul, S. (2013). Physicochemical properties and tenderness of meat samples using proteolytic extract from Calotropis Procera Latex. Food Chemistry, 136(2), 909-916.
Srinivasan, S., Xiong, Y.L., Blanchard, S.P., & Tidwell, J.H. (1997). Physicochemical changes in prawns (Machrobrachium rosenbergii) subjected to multiple freeze – thaw cycles. Journal of Food Science, 62, 123-127.
Sullivan, G.A., & Calkins, C.R. (2010). Application of exogenous enzymes to beef muscle of high and low-connective tissue. Meat Science, 85, 730-734.
Wardlaw, F., McCaskill, L., & Acton, J. (1973). Effect of postmortem muscle changes on poultry meat loaf properties. Journal of Food Science, 38(3), 421-423.
Xia, X., Kong, B., Liu, Q., & Liu, J. (2009). Physicochemical change and protein oxidation in porcine longissimus dorsi as influenced by different freeze–thaw cycles. Meat Science, 83, 239-243.
Xia, X., Kong, B., Xiong, Y., & Ren, Y. (2010). Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation. Meat Science, 85, 481-486.
Zaritzky, N. (2006). Physical-chemical principles in freezing. In D.W. Sun. (Eds.), Handbook of Frozen Food Processing and Packaging. (pp.4-31). Boca Roton: CRC Press.
Ali, S., Zhang, W., Rajput, N., Khan, M. A., Li, C.B., & Zhou, G.H., (2015). Effect of multiple freeze-thaw cycles on the quality of chicken breast meat. Food Chemistry, 173, 808-814.
AOAC. (1990). Official Method of Analysis. (15th). Virginia: The Association of Official Analysis Chemical Chemists.
Aroeira, C.N., Filho, R.A.T, Fontes, P.R., Gomide, L.A.M., Ramos, A.L.S., Ladeira, M.M., & Ramos, E.M. (2016). Freezing, thawing and aging effects on beef tenderness from Bos indicus and Bos Taurus cattle. Meat Science, 166, 118-125.
Astruc, T. (2014). Muscle structure and digestive enzyme bioaccessibility to intracellular compartments. In M. Boland, M. Golding & H. Singh. (Eds.), Food Structures, Digestion and Health. (pp. 193-222). San Diego: Academic Press.
Buyukyavuz, A. (2014). Effect of Bromelain on Duck Breast Meat Tenderization. Retrieved April 20, 2019, from https://tigerprints.clemson.edu/all_theses/1929.
Dias, J., Nunes, M.L., & Mendes, R. (1994). Effect of frozen storage on the chemical and physical properties of black and silver scabbard fish. Journal of the Science of Food and Agriculture, 66, 327–335.
Gokoglu, N., Yerlikaya, P., Ucak, I., & Yatmaz, H.A. (2016). Effect of bromelain and papain enzymes addition on physicochemical and textural properties of squid (Loligo vulgaris). Journal of Food Measurement and Characterization, 11(1), 347-353.
Ha, M., Bekhit, A.E.-D.A., Carne, A., & Hopkins, D.L. (2012). Characterisation of commercial papain, bromelain, actinidin and zingibain protease preparations and their activities toward meat proteins. Food Chemistry, 134(1), 95-105.
Huidobro, F.R.D., Miguel, E., Blázquez, B., & Onega, E. (2005). A comparison between two methods (Warner–Bratzler and Texture Profile Analysis) for testing either raw meat or cooked meat. Meat Science, 69(3), 527-536.
Kemp, C.M., Sensky,P.L., Bardsley, R.G., Buttery, P.J., & Parr, T. (2010). Tenderness – an enzymatic view.
Meat Science, 84(2), 248-256.
Ketnawa, S., & Rawdkuen, S. (2011). Application of bromelain extract for muscle foods tenderization.
Food and Nutrition Sciences, 2, 393-401.
Kim, G.D., Jung, E.Y., Lim, H.Y., Yang, H.S., Joo, S.T., & Jeong, J.Y. (2013). Influence of meat exudates
on the quality characteristics of fresh and freeze-thawed pork. Meat Science, 95, 323-329.
Leygonie, C., Britz, T.J., & Hoffman, L.C. (2012). Impact of freezing and thawing on the quality of meat :
Review. Meat Science, 91, 93-98.
Liu, C., Xiong, Y.L., & Rentfrow, G.K. (2011). Kiwifruit protease extract injection reduces toughness of pork
loin muscle induced by freeze-thaw abuse. LWT- Food Science and Technology, 44, 2026-2031.
Mackie, I.M. (1993). The effects of freezing on flesh protein. Food Reviews International, 9, 575-700.
National statistics office Thailand. (2018). Report on the 2017 survey of the older persons in Thailand.
Bangkok: National statistics office Thailand, Ministry of digital economy and society. (in Thai)
Nontaloon, K, & Sirijariyawat, A. (2018). Effect of type and concentration of enzyme on meat tenderness.
Khon Kaen Agriculture Journal, 46(Supplement 1), 100-105. (in Thai)
Pawar, V.D., Mule, B.D., & Machewad, G.M. (2007). Effect of marination with ginger rhizome extract on
properties of raw and cooked chevon. Journal of Muscle Foods, 18(4), 349-369.
Purslow, P., Oiseth, S., Hughes, J., & Warner, R. (2016). The structural basis of cooking loss in beef: variations with temperature and ageing. Food Research International, 89, 739-748.
Qi, J., Li, C., Chen, Y., Gao, F., Xu, X., & Zhou, G. (2012). Changes in meat quality of ovine longissimus dorsi muscle in response to repeated freeze and thaw. Meat Science, 92(4), 619-626.
Rawdkuen, S., Jaimakreu, M., & Benjakul, S. (2013). Physicochemical properties and tenderness of meat samples using proteolytic extract from Calotropis Procera Latex. Food Chemistry, 136(2), 909-916.
Srinivasan, S., Xiong, Y.L., Blanchard, S.P., & Tidwell, J.H. (1997). Physicochemical changes in prawns (Machrobrachium rosenbergii) subjected to multiple freeze – thaw cycles. Journal of Food Science, 62, 123-127.
Sullivan, G.A., & Calkins, C.R. (2010). Application of exogenous enzymes to beef muscle of high and low-connective tissue. Meat Science, 85, 730-734.
Wardlaw, F., McCaskill, L., & Acton, J. (1973). Effect of postmortem muscle changes on poultry meat loaf properties. Journal of Food Science, 38(3), 421-423.
Xia, X., Kong, B., Liu, Q., & Liu, J. (2009). Physicochemical change and protein oxidation in porcine longissimus dorsi as influenced by different freeze–thaw cycles. Meat Science, 83, 239-243.
Xia, X., Kong, B., Xiong, Y., & Ren, Y. (2010). Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation. Meat Science, 85, 481-486.
Zaritzky, N. (2006). Physical-chemical principles in freezing. In D.W. Sun. (Eds.), Handbook of Frozen Food Processing and Packaging. (pp.4-31). Boca Roton: CRC Press.
Downloads
Published
2020-01-09
Issue
Section
Research Article
