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Meat Tenderization through Plant Proteases- A Mini Review

Review Paper | January 1, 2021

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Ali Ikram, Saadia Ambreen, Amber Tahseen, Areeg Azhar, Khadija Tariq, Tayyba Liaqat, Muhammad Babar Bin Zahid, Muhammad Abdul Rahim, Waseem Khalid, Naqash Nasir

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Int. J. Biosci.18( 1), 102-112, January 2021

DOI: http://dx.doi.org/10.12692/ijb/18.1.102-112


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The tenderness and quality of meat is very concerning for meat consumers. Meat tenderness relies on connective tissue, and muscle proteolytic ability. The use of various chemical tenders is the subject of the majority of research studies on the meat tenderness.  However, there are certain drawbacks of these chemical tenders on one or the other sensory characteristics of meat.  Few natural tenderizers may be used to counteract these adverse effects of chemical goods. Natural tenderizers are certain vegetables and fruits containing proteolytic enzymes that are responsible for rough meat tenderization. The use of exogenous proteases to enhance the tenderness of meat received tremendous interest in order to consistently produce meat tenderness as well as add value to low-grade cuts. The overview elaborates the sources, characteristics, and uses of plant proteases for the tenderization of meat. Furthermore, it highlights the impact of plant protease on the meat quality and effect on the meat proteins. Plant enzymes (including papain, ficin and bromelain) have been thoroughly studied as tenderizers for meat. The efficient use of such enzymes in raw meat calls for the determination of their enzyme kinetics and features and an understanding of the effect of the meat surrounding ambient (pH, temperature) conditions upon enzyme function. This allows for the creation of optimum conditions for tendering fresh meat and the removal or mitigation of any harmful effects on other quality characteristics.


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Meat Tenderization through Plant Proteases- A Mini Review

Aaslyng MD, Meinert L. 2017. Meat flavour in pork and beef–From animal to meal. Meat science 132, 112-117. https://doi.org/10.1016/j.meatsci.2017.04.012

Abdel-Naeem HH, Mohamed HM. 2016. Improving the physico-chemical and sensory characteristics of camel meat burger patties using ginger extract and papain. Meat science 118, 52-60. https://doi.org/10.1016/j.meatsci.2016.03.021

Abe M, Arai S. 1991. Some properties of a cysteine proteinase inhibitor from corn endosperm. Agricultural and biological chemistry 55(9), 2417-2418. https://doi.org/10.1080/00021369.1991.10870959

Ahmad MN, Hilmi NHN, Normaya E, Yarmo MA, Bulat KHK. 2020. Optimization of a protease extraction using a statistical approach for the production of an alternative meat tenderizer from Manihot esculenta roots. Journal of Food Science and Technology, 1-11. https://doi.org/10.1007/s13197-020-04317-5

Akpan I, Omojola A. 2015. Quality attributes of crude papain injected beef. Journal of Meat Science and Technology 3(04), 42-46.

Alarcon-Rojo AD, Carrillo-Lopez LM, Reyes-Villagrana R, Huerta-Jiménez M, Garcia-Galicia IA. 2019. Ultrasound and meat quality: A review. Ultrasonics sonochemistry 55, 369-382.

Albee KL, Bernasconi RJ, Edmunds T. 1997. Complete amino acid sequence of ananain and a comparison with stem bromelain and other plant cysteine proteases. Biochemical Journal 327(1), 199-202. https://doi.org/10.1042/bj3270199

Azarkan M, El Moussaoui A, Van Wuytswinkel D, Dehon G, Looze Y. 2003. Fractionation and purification of the enzymes stored in the latex of Carica papaya. Journal of Chromatography B 790(1-2), 229-238. https://doi.org/10.1016/S1570-0232(03)00084-9

Barberis S, Guzmán F, Illanes A, López-Santín J, Wilson L, Álvaro G, Clapés P. 2008. Study cases of enzymatic processes Enzyme Biocatalysis (p 253-378), Springer.

Barrett AJ, Chen JM. 2004. Thimet oligopeptidase Handbook of proteolytic enzymes (p 352-356), Elsevier. https://doi.org/10.1016/B978-0-12-079611-3.50093-8

Bhat ZF, Morton JD, Mason SL, Bekhit AEDA. 2018. Applied and emerging methods for meat tenderization: A comparative perspective. Comprehensive Reviews in Food Science and Food Safety 17(4), 841-859. https://doi.org/10.1111/1541-4337.12356

Calkins CR, Sullivan G. 2007. Adding enzymes to improve beef tenderness. Beef Facts Product Enhancement, National Cattleman’s Beef Associat-ion. Centennial Colorado: Cattlemen’s Beef Board.

Cdc C. 2011. Estimates of foodborne illness in the United States. Atlanta: Center for Disease Control and Prevention (CDC).

Chaurasiya RS, Sakhare P, Bhaskar N, Hebbar HU. 2015. Efficacy of reverse micellar extracted fruit bromelain in meat tenderization. Journal of food science and technology 52(6), 3870-3880.

Chuapoehuk P, Raksakulthai N. 1991. Use of papain and bromelin in the production of oyster sauce. Witthayasan Kasetsart sakha Witthayasat.

Cstorer A, Ménard R. 1994. Catalytic mechanism in papain family of cysteine peptidases Methods in enzymology (Vol. 244, pp. 486-500): Elsevier. https://doi.org/10.1016/0076-6879(94)44035-2

eddine Derardja A, Pretzler M, Kampatsikas I, Barkat M, Rompel A. 2019. Inhibition of apricot polyphenol oxidase by combinations of plant proteases and ascorbic acid. Food chemistry: X, 4, 100053. https://doi.org/10.1016/j.fochx.2019.100053

Ellies-Oury MP, Cantalapiedra-Hijar G, Durand D, Gruffat D, Listrat A, Micol D, Saracco J. 2016. An innovative approach combining animal performances, nutritional value and sensory quality of meat. Meat science 122, 163-172. https://doi.org/10.1016/j.meatsci.2016.08.004

Eshamah H, Han I, Naas H, Acton J, Dawson P. 2014. Antibacterial effects of natural tenderizing enzymes on different strains of Escherichia coli O157: H7 and Listeria monocytogenes on beef. Meat science 96(4), 1494-1500. https://doi.org/10.1016/j.meatsci.2013.12.010

Foegeding EA, Larick D. 1986. Tenderization of beef with bacterial collagenase. Meat science 18(3), 201-214. https://doi.org/10.1016/0309-1740(86)90034-3

Grzonka Z, Kasprzykowski F, Wiczk W. 2007. Cysteine proteases Industrial enzymes (p 181-195): Springer.

Gudbjörnsdóttir B, Suihko ML, Gustavsson P,  Thorkelsson G, Salo S, Sjöberg AM, Bredholt S. 2004. The incidence of Listeria monocytogenes in meat, poultry and seafood plants in the Nordic countries. Food Microbiology 21(2), 217-225. https://doi.org/10.1016/S0740-0020(03)00012-1

Gurumallesh P, Alagu K, Ramakrishnan B, Muthusamy S. 2019. A systematic reconsideration on proteases. International journal of biological macromolecules 128, 254-267. https://doi.org/10.1016/j.ijbiomac.2019.01.081

Hage DS, Anguizola JA, Bi C, Li R, Matsuda R, Papastavros E, Zheng X. 2012. Pharmaceutical and biomedical applications of affinity chromatography: recent trends and developments. Journal of pharmaceutical and biomedical analysis 69, 93-105. https://doi.org/10.1016/j.jpba.2012.01.004

Huet J, Looze Y, Bartik K, Raussens V, Wintjens R, Boussard P. 2006. Structural characterization of the papaya cysteine proteinases at low pH. Biochemical and biophysical research communications 341(2), 620-626. https://doi.org/10.1016/j.bbrc.2005.12.210

Ionescu RE, Fillit C, Jaffrezic-Renault N, Cosnier S. 2008. Urease–gelatin interdigitated microelectrodes for the conductometric determination of protease activity. Biosensors and Bioelectronics 24(3), 489-492. https://doi.org/10.1016/j.bios.2008.06.021

Kang CK, Rice EE. 1970. Degradation of various meat fractions by tenderizing enzymes. Journal of food science 35(5), 563-565. https://doi.org/10.1111/j.1365-2621.1970.tb04809.x

Kemp C M, Sensky PL, Bardsley RG, Buttery PJ, Parr T. 2010. Tenderness–An enzymatic view. Meat science 84(2), 248-256. https://doi.org/10.1016/j.meatsci.2009.06.008

Ketnawa S, Rawdkuen S. 2011. Application of bromelain extract for muscle foods tenderization. Food and Nutrition Sciences 2(05), 393. https://doi.org/10.4236/fns.2011.25055

Konno K, Hirayama C, Nakamura M, Tateishi K, Tamura Y, Hattori M, Kohno K. 2004. Papain protects papaya trees from herbivorous insects: role of cysteine proteases in latex. The Plant Journal 37(3), 370-378. https://doi.org/10.1046/j.1365-313X.2003.01968.x

Llerena-Suster CR, Priolo NS, Morcelle SR. 2011. Sodium tetrathionate effect on papain purification from different Carica papaya latex crude extracts. Preparative biochemistry & biotechnology 41(2), 107-121. https://doi.org/10.1080/10826068.2011.544230

Taylor MJ, Hopkins LD. 2011. Patents for stretching and shaping meats. Recent patents on food, nutrition & agriculture 3(2), 91-101.

Maltin C, Balcerzak D, Tilley R, Delday M. 2003. Determinants of meat quality: tenderness. Proceedings of the Nutrition Society 62(2), 337-347. https://doi.org/10.1079/PNS2003248    https://doi.org/10.1079/PNS2003248

Maróstica MR, Pastore GM. 2010. Some nutritional, technological and environmental advances in the use of enzymes in meat products. Enzyme research, 2010.

Mullen AM, Alvarez C, Zeugolis DI, Henchion M, O’Neill E, Drummond L. 2017. Alternative uses for co-products: Harnessing the potential of valuable compounds from meat processing chains. Meat science 132, 90-98. https://doi.org/10.1016/j.meatsci.2017.04.24

Nanda RF, Rini B, Syukri D, Thu NNA, Kasim A. 2020. A Review: Application of Bromelain Enzymes in Animal Food Products. Andalasian International Journal of Agriculture and Natural  Sciences (AIJANS) 1(01), 33-44.

Napper A, Bennett S, Borowski M, Holdridge M, Leonard M, Rogers E, Shames S. 1994. Purification and characterization of multiple forms of the pineapple-stem-derived cysteine proteinases ananain and comosain. Biochemical Journal 301(3), 727-735. https://doi.org/10.1042/bj3010727

Naveena B, Kiran M, Reddy KS, Ramakrishna C, Vaithiyanathan S, Devatkal SK. 2011. Effect of ammonium hydroxide on ultrastructure and tenderness of buffalo meat. Meat science 88(4), 727-732. https://doi.org/10.1016/j.meatsci.2011.03.005

Naveena B, Mendiratta S, Anjaneyulu A. 2004. Tenderization of buffalo meat using plant proteases from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome). Meat science 68(3), 363-369. https://doi.org/10.1016/j.meatsci.2004.04.004

Norazmi M, Shahrain M, Normaya E, Nor M, Iqbal A, Halim K. 2020. The Applicability of Using a Protease Extracted from Cashew Fruits (Anacardium occidentale), as Possible Meat Tenderizer: An Experimental Design Approach. Journal of texture studies. https://doi.org/10.1111/jtxs.12529

Oad F, Lakho A, Khan A, Ansari A, Sheikh F, Khail M. 2001. Economics of papaya in Malir district, Karachi–Pakistan. International Journal of Agriculture and Biology 4, 477-481.

Ogunjobi AA, Ogunjobi T. 2011. Comparative study of antibacterial activities of ethanol extracts of the bark and seeds of garcinia kola and caricapapaya. African Journal of Biomedical Research 14(2), 147-152.

Picard B, Gagaoua M. 2017. Proteomic investigations of beef tenderness Proteomics in Food Science (p 177-197): Elsevier. https://doi.org/10.1016/B978-0-12-804007-2.00011-4

Qihe C, Guoqing H, Yingchun J, Hui N. 2006. Effects of elastase from a Bacillus strain on the tenderization of beef meat. Food chemistry 98(4), 624-629. https://doi.org/10.1016/j.foodchem.2005.06.043

Ramanathan R, Mafi GG, Yoder L, Perry M, Pfeiffer M, VanOverbeke DL, Maheswarappa NB. 2020. Biochemical changes of postmortem meat during the aging process and strategies to improve the meat quality. In Meat Quality Analysis (p 67-80). Academic Press. https://doi.org/10.1016/B978-0-12-819233-7.00005-7

Ramezani R, Aminlari M, Fallahi H. 2003. Effect of chemically modified soy proteins and ficin‐tenderized meat on the quality attributes of sausage. Journal of food science 68(1), 85-88. https://doi.org/10.1111/j.1365-2621.2003.tb14119.x

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. https://doi.org/10.1016/j.foodchem.2012.08.077

Renand G, Picard B, Touraille C, Berge P, Lepetit J. 2001. Relationships between muscle characteristics and meat quality traits of young Charolais bulls. Meat science 59(1), 49-60. https://doi.org/10.1016/S0309-1740(01)00051-1

Schwimmer S. 1981. Source book of food enzymology: AVI Publishing Co. Inc.

Smith J, Hong-Shum L. 2011. Food additives data book: John Wiley & Sons.

Sullivan GA, Calkins C. 2010. Application of exogenous enzymes to beef muscle of high and low-connective tissue. Meat science 85(4), 730-734. https://doi.org/10.1016/j.meatsci.2010.03.033

Tewari BB, Subramanian G, Gomathinayagm R. 2014. Antimicrobial properties of Carica papaya (Papaya) different Leaf Extract against E. coli, S. aureus and C. albicans. American Journal of Pharmacology and Pharmacotherapeutics 1(1), 025-039.

Thorslund CA, Sandøe P, Aaslyng MD, Lassen J. 2016. A good taste in the meat, a good taste in the mouth–Animal welfare as an aspect of pork quality in three European countries. Livestock science 193, 58-65. https://doi.org/10.1016/j.livsci.2016.09.007

Toohey E, Kerr M, Van de Ven R, Hopkins D. 2011. The effect of a kiwi fruit based solution on meat traits in beef m. semimembranosus (topside). Meat science 88(3), 468-471. https://doi.org/10.1016/j.meatsci.2011.01.028

Veiseth E, Shackelford S, Wheeler T, Koohmaraie M. 2004. Factors regulating lamb longissimus tenderness are affected by age at slaughter. Meat science 68(4), 635-640. https://doi.org/10.1016/j.meatsci.2004.05.015

Wada M, Suzuki T, Yaguti Y, Hasegawa T. 2002. The effects of pressure treatments with kiwi fruit protease on adult cattle semitendinosus muscle. Food chemistry 78(2), 167-171. https://doi.org/10.1016/S0308-8146(01)00395-8

Wang LL, Han L, Ma XL, Yu QL, Zhao SN. 2017. Effect of mitochondrial apoptotic activation through the mitochondrial membrane permeability transition pore on yak meat tenderness during postmortem aging. Food chemistry 234, 323-331. https://doi.org/10.1016/j.foodchem.2017.04.185

Wheeler T, Shackelford S, Koohmaraie M. 200. Variation in proteolysis, sarcomere length, collagen content, and tenderness among major pork muscles. Journal of Animal Science 78(4), 958-965. https://doi.org/10.2527/2000.784958x

Wiederanders B. 2003. Structure-function relationships in class CA1 cysteine peptidase propeptides. Acta Biochimica Polonica 50(3), 691-713. https://doi.org/10.18388/abp.2003_3661

Zhao GY, Zhou MY, Zhao HL, Chen XL, Xie BB, Zhang XY, Zhang YZ. 2012. Tenderization effect of cold-adapted collagenolytic protease MCP-01 on beef meat at low temperature and its mechanism. Food chemistry 134(4), 1738-1744. https://doi.org/10.1016/j.foodchem.2012.03.118