Synergistic Effect of Calcium Chloride-Fig Protease-Kiwifruit Protease Blend as Meat Tenderizer on Myofibrillar Protein Structure of Rabbit Meat

Abstract

Abstract: ABSTRACT：To study the synergistic tenderization mechanism of compound tenderizer composed of calcium chloride, fig protease and kiwifruit protease on the structure of myofibrillar protein in rabbit hind leg meat, the related protein indicators of the rabbit meat which were treated with compound tenderizer were compared with those treated with the three single tenderizers. The results showed that the compound tenderizer can degrade myofibrillar protein more moderately and effectively (p<0.05); the surface hydrophobicity of myofibrillar protein in calcium chloride group was significantly higher than that in single enzyme groups (p<0.05);The solubility and soluble protein content of myofibrillar protein in single enzyme groups were significantly higher than those in calcium chloride group (p<0.05); the electrophoresis map showed that the myosin light chain and C-protein are mainly degraded by fig protease and the myosin heavy chain is mainly degraded by kiwifruit protease. The above results indicate that there is a synergistic effect among the components of the compound tenderizer, the synergistic mechanism of the compound tenderizer on the level of protein structure was that the calcium chloride makes the protein unfold vigorously and more enzyme binding sites are exposed, moreover those two enzymes have different specificity so that the tenderization effect are ed.

Key words: Compound tenderizer, Calcium chloride, Fig protease, Kiwifruit protease, Myofibrillar protein, Synergistic Effect

CLC Number:

TS251.5+4

References

参考文献
[1] Shin H G, Choi Y M, Kim H K, et al. Tenderization and fragmentation of myofibrillar proteins in bovine longissimus dorsi muscle using proteolytic extract from Sarcodon aspratus[J]. LWT - Food Science and Technology. 2008, 41(8): 1389-1395.
[2] Bhat Z F, Morton J D, Mason S L, et al. Role of calpain system in meat tenderness: A review[J]. Food Science and Human Wellness. 2018, 7(3): 196-204.
[3] Li X, Sun Y, Pan D, et al. The effect of CaCl 2 marination on the tenderizing pathway of goose meat during conditioning[J]. Food Research International. 2017, 102: 487.
[4] Ha M, Bekhit A E A, Carne A, et al. Characterisation of commercial papain, bromelain, actinidin and zingibain protease preparations and their activities toward meat proteins[J]. Food Chemistry. 2012, 134(1): 95-105.
[5] Fernández-Lucas J, Casta Eda D, Hormigo D. “New trends for a classical enzyme: Papain, a biotechnological success story in the food industry”[J]. Trends in Food Science & Technology. 2017, 68: S1005189810.
[6] Homaei A, Stevanato R, Etemadipour R, et al. Purification, catalytic, kinetic and thermodynamic characteristics of a novel ficin from Ficus johannis[J]. Biocatalysis & Agricultural Biotechnology. 2017, 10: S1853534904.
[7] Zhu X, Lovedeep K, Mike B. Thermal inactivation of Actinidin as affected by meat matrix[J]. Meat Science. 2018, 145: S796512555.
[8] Dalle Zotte A, Szendr? Z. The role of rabbit meat as functional food[J]. Meat Science. 2011, 88(3): 319-331.
[9] 宋丽坤. 油炸兔肉品质改良及保藏中品质变化研究[D]. 四川农业大学, 2016.
[10] 李明奇，贺稚非，李少博，等. 氯化钙-无花果蛋白酶-猕猴桃蛋白酶复合嫩化剂体系改善兔肉嫩度和保水性的工艺优化[J]. 食品与发酵工业. 2019, 45(18): 120-129.
[11] Wang Z, Zhifei H, Xiao G, et al. The Effects of Lipid Oxidation Product Acrolein on the Structure and Gel Properties of Rabbit Meat Myofibrillar Proteins[J]. Food Biophysics. 2018: 1-13.
[12] 王兆明. 兔肉滚揉腌制工艺及品质特性变化研究[D]. 西南大学, 2016.
[13] Agyare K K, Xiong Y L, Addo K. Influence of salt and pH on the solubility and structural characteristics of transglutaminase-treated wheat gluten hydrolysate[J]. Food Chemistry. 2008, 107(3): 1131-1137.
[14] 罗海波. 对虾干加工中嫩化及重组技术的研究[D]. 南京农业大学, 2006.
[15] Chelh I, Gatellier P, Sante?lhoutellier V. Technical note: A simplified procedure for myofibril hydrophobicity determination[J]. Meat Science. 2006, 74(4): 681-683.
[16] Hopkins D L, Thompson J M. The relationship between tenderness, proteolysis, muscle contraction and dissociation of actomyosin[J]. Meat Science. 2001, 57(1): 1-12.
[17] Pigott R S, Kenney P B, Slider S, et al. Formulation Protocol and Dicationic Salts Affect Protein Functionality of Model System Beef Batters[J]. Journal of Food Science. 2000, 65(7
): 1151-11154.
[18] Wang Y, Zhou Y, Li P, et al. Combined effect of CaCl2 and high pressure processing on the solubility of chicken breast myofibrillar proteins under sodium-reduced conditions[J]. Food Chemistry. 2018, 269: 236-243.
[19] Yu W, Ying Z, Pei-Jun L, et al. Combined effect of CaCl 2 and high pressure processing on the solubility of chicken breast myofibrillar proteins under sodium-reduced conditions[J]. Food Chemistry. 2018: S646972840X.
[20] Aminlari M, Shekarforoush S S, Gheisari H R, et al. Effect of actinidin on the protein solubility, water holding capacity, texture, electrophoretic pattern of beef, and on the quality attributes of a sausage product[J]. Journal of Food Science. 2010, 74(3): C221-C226.
[21] Du L, Zhou G, Xu X, et al. Study on kinetics of mass transfer in water-boiled salted duck during wet-curing[J]. Journal of Food Engineering. 2010, 99(4): 578-584.
[22] Jia N, Wang L, Shao J, et al. Changes in the structural and gel properties of pork myofibrillar protein induced by catechin modification[J]. Meat Science. 2017, 127: 45-50.
[23] 王发祥，李强，俞健，等. 草鱼冷藏过程中肌肉蛋白质结构特征的变化[J]. 食品与发酵工业. 2015, 41(6): 196-199.
[24] Shin H, Choi Y, Kim H, et al. Tenderization and fragmentation of myofibrillar proteins in bovine longissimus dorsi muscle using proteolytic extract from Sarcodon aspratus[J]. LWT - Food Science and Technology. 2008, 41(8): 1389-1395.
[25] Liu C, Xiong Y L, Rentfrow G K. Kiwifruit protease extract injection reduces toughness of pork loin muscle induced by freeze–thaw abuse[J]. LWT - Food Science and Technology. 2011, 44(10): 2026-2031.