Browse > Article
http://dx.doi.org/10.5851/kosfa.2022.e36

Effects of Protein Functionality on Myofibril Protein-Saccharide Graft Reaction  

Kim, Tae-Kyung (Research Group of Food Processing, Korea Food Research Institute)
Yong, Hae In (Division of Animal and Dairy Science, Chungnam National University)
Cha, Ji Yoon (Research Group of Food Processing, Korea Food Research Institute)
Kim, Yun Jeong (Research Group of Food Processing, Korea Food Research Institute)
Jung, Samooel (Division of Animal and Dairy Science, Chungnam National University)
Choi, Yun-Sang (Research Group of Food Processing, Korea Food Research Institute)
Publication Information
Food Science of Animal Resources / v.42, no.5, 2022 , pp. 849-860 More about this Journal
Abstract
The myofibril protein (MP) isolate-saccharide graft reactions was prepared using the Maillard reaction with saccharides. The effects of various saccharides on protein functionality and quality of the Maillard reaction were investigated and compared with those of MP. The grafting degree of the MP isolate-saccharide graft reaction was significantly higher in the reducing sugar-treated groups (lactose, glucose, fructose, and palatinose). The browning intensity of the MP isolate-saccharide graft reaction with fructose, sucrose, and erythitol was higher than that observed in the control reaction (p<0.05). MP that reacted with reducing sugars (glucose, fructose, palatinose, and lactose) had fainter bands than MP that reacted with non-reducing sugars (sucrose, erythitol, trehalose, sorbitol, and xylitol). MPs conjugated with glucose exhibited higher protein solubility. The palatinose and lactose treatments were maximum in water binding capacity, though no significant difference in oil binding capacity among the saccharide treatments was observed. The emulsion stability of the MP isolate-saccharide graft reaction with palatinose and erythitol was higher than that of the control reaction. Therefore, reducing sugars have good protein functionality in the MP isolate-saccharides graft reaction.
Keywords
myofibril protein; saccharide; graft reaction; reducing sugar; structure;
Citations & Related Records
Times Cited By KSCI : 2  (Citation Analysis)
연도 인용수 순위
1 Sun WW, Yu SJ, Yang XQ, Wang JM, Zhang JB, Zhang Y, Zheng EL. 2011. Study on the rheological properties of heat-induced whey protein isolate-dextran conjugate gel. Food Res Int 44:3259-3263.   DOI
2 Vigo MS, Malec LS, Gomez RG, Llosa RA. 1992. Spectrophotometric assay using o-phthaldialdehyde for determination of reactive lysine in dairy products. Food Chem 44:363-365.   DOI
3 Xiao Q, Woo MW, Hu J, Xiong H, Zhao Q. 2021. The role of heating time on the characteristics, functional properties and antioxidant activity of enzyme-hydrolyzed rice proteins-glucose Maillard reaction products. Food Biosci 43:101225.
4 Xu Y, Dong M, Tang C, Han M, Xu X, Zhou G. 2020. Glycation-induced structural modification of myofibrillar protein and its relation to emulsifying properties. LWT-Food Sci Technol 117:108664.
5 Yong H, Kim TK, Kim YB, Jung S, Choi YS. 2020. Functional and instrumental textural properties of reduced-salt meat emulsions with konjac gel: Combined effects of transglutaminase, isolate soy protein, and alginate. Int J Food Prop 23:1296-1309.   DOI
6 Yong HI, Kim TK, Choi HD, Jang HW, Jung S, Choi YS. 2021. Clean label meat technology: Pre-converted nitrite as a natural curing. Food Sci Anim Resour 41:173-184.   DOI
7 Zayas JF. 2012. Functionality of proteins in food. Springer Science & Business Media, Berlin, Germany.
8 Zeng X, Bai W, Zhu X, Dong H. 2017. Browning intensity and taste change analysis of chicken protein-sugar Maillard reaction system with antioxidants and different drying processes. J Food Process Preserv 41:e13117.
9 Beuchat LR. 1977. Functional and electrophoretic characteristics of succinylated peanut flour protein. J Agric Food Chem 25:258-261.   DOI
10 Barbut S, Sosnicki AA, Lonergan SM, Knapp T, Ciobanu DC, Gatcliffe LJ, Huff-Lonergan E, Wilson EW. 2008. Progress in reducing the pale, soft and exudative (PSE) problem in pork and poultry meat. Meat Sci 79:46-63.   DOI
11 Choi YS, Choi JH, Han DJ, Kim HY, Lee MA, Kim HW, Jeong JY, Kim CJ. 2011. Effects of rice bran fiber on heat-induced gel prepared with pork salt-soluble meat proteins in model system. Meat Sci 88:59-66.   DOI
12 Jia G, Nirasawa S, Ji X, Luo Y, Liu H. 2018. Physicochemical changes in myofibrillar proteins extracted from pork tenderloin thawed by a high-voltage electrostatic field. Food Chem 240:910-916.   DOI
13 de Oliveira FC, Coimbra JSR, de Oliveira EB, Zuniga ADG, Rojas EEG. 2016. Food protein-polysaccharide conjugates obtained via the Maillard reaction: A review. Crit Rev Food Sci Nutr 56:1108-1125.   DOI
14 Guan JJ, Qiu AY, Liu XY, Hua YF, Ma YH. 2006. Microwave improvement of soy protein isolate-saccharide graft reactions. Food Chem 97:577-585.   DOI
15 He W, Tian L, Zhang S, Pan S. 2021. A novel method to prepare protein-polysaccharide conjugates with high grafting and low browning: Application in encapsulating curcumin. LWT-Food Sci Technol 145:111349.
16 Li Y, Zhong F, Ji W, Yokoyama W, Shoemaker CF, Zhu S, Xia W. 2013. Functional properties of Maillard reaction products of rice protein hydrolysates with mono-, oligo- and polysaccharides. Food Hydrocoll 30:53-60.   DOI
17 Kim TK, Ku SK, Kim YB, Jeon KH, Choi YS. 2017. Substitution and technology trend of synthetic additives in processed meat industry: Nitrite and phosphate. Food Sci Anim Resour Ind 6:98-108.
18 Kim TK, Yong HI, Kim YB, Jung S, Kim HW, Choi YS. 2021b. Effects of organic solvent on functional properties of defatted proteins extracted from Protaetia brevitarsis larvae. Food Chem 336:127679.
19 Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.   DOI
20 Li R, Cui Q, Wang G, Liu J, Chen S, Wang X, Wang X, Jiang L. 2019. Relationship between surface functional properties and flexibility of soy protein isolate-glucose conjugates. Food Hydrocoll 95:349-357.   DOI
21 Mu L, Zhao M, Yang B, Zhao H, Cui C, Zhao Q. 2010. Effect of ultrasonic treatment on the graft reaction between soy protein isolate and gum acacia and on the physicochemical properties of conjugates. J Agric Food Chem 58:4494-4499.   DOI
22 Nooshkam M, Varidi M, Bashash M. 2019. The Maillard reaction products as food-born antioxidant and antibrowning agents in model and real food systems. Food Chem 275:644-660.   DOI
23 Starowicz M, Zielinski H. 2019. How Maillard reaction influences sensorial properties (color, flavor and texture) of food products? Food Rev Int 35:707-725.   DOI
24 Li H, Wu CJ, Yu SJ. 2018. Impact of microwave-assisted heating on the pH value, color, and flavor compounds in glucose-ammonium model system. Food Bioprocess Technol 11:1248-1258.   DOI
25 Kim TK, Yong HI, Jung S, Kim HW, Choi YS. 2021a. Effect of reducing sodium chloride based on the sensory properties of meat products and the improvement strategies employed: A review. J Anim Sci Technol 63:725-739.   DOI
26 Chevalier F, Chobert JM, Popineau Y, Nicolas MG, Haertle T. 2001. Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar. Int Dairy J 11:145-152.   DOI
27 Hemung BO, Chin KB. 2015. Evaluation of acid-treated fish sarcoplasmic proteins on physicochemical and rheological characteristics of pork myofibrillar protein gel mediated by microbial transglutaminase. Korean J Food Sci Anim Resour 35:50-57.   DOI
28 Wong BT, Day L, Augustin MA. 2011. Deamidated wheat protein-dextran Maillard conjugates: Effect of size and location of polysaccharide conjugated on steric stabilization of emulsions at acidic pH. Food Hydrocoll 25:1424-1432.   DOI
29 Xu Y, Han M, Huang M, Xu X. 2021. Enhanced heat stability and antioxidant activity of myofibrillar protein-dextran conjugate by the covalent adduction of polyphenols. Food Chem 352:129376.
30 Yu M, He S, Tang M, Zhang Z, Zhu Y, Sun H. 2018. Antioxidant activity and sensory characteristics of Maillard reaction products derived from different peptide fractions of soybean meal hydrolysate. Food Chem 243:249-257.   DOI
31 Lee SH, Joo ST, Ryu YC. 2010. Skeletal muscle fiber type and myofibrillar proteins in relation to meat quality. Meat Sci 86:166-170.   DOI
32 Li Y, Zhang X, Lu F, Kang ZL. 2021. Effect of sodium bicarbonate and sodium chloride on aggregation and conformation of pork myofibrillar protein. Food Chem 350:129233.
33 Naranjo GB, Malec LS, Vigo M. 1998. Reducing sugars effect on available lysine loss of casein by moderate heat treatment. Food Chem 62:309-313.   DOI
34 Desmond E. 2006. Reducing salt: A challenge for the meat industry. Meat Sci 74:188-196.   DOI
35 Zhang C, Chen Y, Yin Y, Ji HH, Shim WB, Hou Y, Zhou M, Li XD, Ma Z. 2015. A small molecule species specifically inhibits Fusarium myosin I. Environ Microbiol 17:2735-2746.   DOI