Effect of the amount of red yeast red on the functional properties and structure of pork myofibrillar protein
LI Yixuan1, WANG Yue1, LU Xiaochuan1, KANG Mengyao1, SHANG Yongbiao1,2*
1 (College of Food Science, Southwest University, Chongqing 400716, China) 2 (Quality and Safety Risk Assessment Laboratory of Products Preservation (Chongqing), Ministry of Agriculture, Chongqing 400716, China) 3 (Chongqing Special Food Programme and Technology Research Center, Chongqing 400716, China)
Abstract: This paper aims to explore the effect of mulberry red addition on the functional properties of pork myofibrillar protein, and provide a theoretical basis for the development of low-nitrate meat products. The changes of the function index and molecular structure of pork MP were investigated by treating the longissimus dorsi muscle with the content of 0, 0.1%, 0.15%, 0.2% and 0.25%.With the increase of red yeast red concentration, the solubility, emulsifying, sulfhydryl content and storage modulus of MP increased first and then decreased. The carbonyl content and surface hydrophobicity decreased first and then increased. Infrared spectrum analysis showed that α-helix the content increased first and then decreased with the increase of red yeast red concentration, and the β-fold, β-turn and random curl content decreased first and then increased. Reducing the use of sodium nitrite will seriously affect the functional properties of MP. Low or high concentration of Monascus red has poor functional properties. When the concentration of Monascus red is 0.15%, it can significantly improve the functional properties of MP under low nitrite condition (P & lt;0.05).
李懿璇,王悦,鲁小川,等. 红曲红添加量对猪肉肌原纤维蛋白功能性质和结构的影响[J]. 食品与发酵工业, 2020, 46(2): 173-179.
LI Yixuan,WANG Yue,LU Xiaochuan,et al. Effect of the amount of red yeast red on the functional properties and structure of pork myofibrillar protein[J]. Food and Fermentation Industries, 2020, 46(2): 173-179.
KUROIWA Y, OKAMURA T, ISHII Y, et al. Enhancement of esophageal carcinogenesis in acid reflux model rats treated with ascorbic acid and sodium nitrite in combination with or without initiation[J]. Cancer Science,2008, 99(1):7-13.
KUTAMURA Y, UMEMURA T, OKAZAKI K, et al. Enhancing effects of simultaneous treatment with sodium nitrite on 2-amino-3-methylimidazo[4,5-f]quinoline-induced rat liver, colon and Zymbal′s gland carcinogenesis after initiation with diethylnitrosamine and 1,2-dimethylhydrazine[J]. International Journal of Cancer, 2010, 118(10):2 399-2 404.
LINSEISEN J,ROHRMANNS,NORATT, et al. Dietary intake of different types and characteristics of processed meat which might be associated with cancer risk--results from the 24-hour diet recalls in the European Prospective Investigation into Cancer and Nutrition (EPIC)[J]. Public Health Nutrition, 2006, 9(4):449-464.
CROSS A J, LEITZMANN M F, GAIL M H, et al. A prospective study of red and processed meat intake in relation to cancer risk.[J]. PloS Medicine, 2007, 4(12):e325.
FALOWO A B, FAYEMI P O, MUCHENJE V. Natural antioxidants against lipid-protein oxidative deterioration in meat and meat products: A review[J]. Food Research International, 2014, 64: 171-181.
HONG G P, XIONG Y L. Microbial transglutaminase-induced structural and rheological changes of cationic and anionic myofibrillar proteins[J]. Meat Science, 2012, 91(1): 36-42.
KUNARAYAKUL S, THAIPHANIT S, ANPRUNG P, et al. Optimization of coconut protein deamidation using protein-glutaminase and its effect on solubility, emulsification, and foaming properties of the proteins[J]. Food Hydrocolloids, 2017, 79:197-207.
AGYARE K K, ADDO K, XIONG Y L. Emulsifying and foaming properties of transglutaminase-treated wheat gluten hydrolysate as influenced by pH, temperature and salt[J]. Food Hydrocolloids, 2009, 23(1):72-81.
AMIRI A, SHARRIFIAN P, SOLTANIZADEH N. Application of ultrasound treatment for improving the physicochemical, functional and rheological properties of myofibrillar proteins[J]. International Journal of Biological Macromolecules, 2018, 111:139-147.
TOKUR B, KORKMAZ K. The effects of an iron-catalyzed oxidation system on lipids and proteins of dark muscle fish[J]. Food Chemistry, 2007, 104(2):754-760.
YONGSAWATDIGUL J, PARK J W. Thermal denaturation and aggregation of threadfin bream actomyosin[J]. Food Chemistry, 2003, 83(3):409-416.
CHELH I, GATELLIER P, SANTÉ-LGOUTELLIER V. Technical note: A simplified procedure for myofibril hydrophobicity determination[J]. Meat Science, 2006, 74(4):681-683.
LAEMMLI U K. Cleavage of structural proteins during the assembly of the head of bacteriophage-T4[J].Nature, 1970, 227(5 259): 680-685.
XIONG Yao, LI Qianru, MIAO Song, et al. Effect of ultrasound on physicochemical properties of emulsion stabilized by fish myofibrillar protein and canthan gum[J]. Food Weekly News, 2019,54:225-234.
HATTORI A, TAKAHASHI K. Calcium-induced weakening of skeletal muscle Z-Disks[J]. Journal of Biochemistry, 1982, 92(2):381-390.
WU Fan,SHI Xiaojie, ZOU Henan,et al.Effects of high-pressure homogenization on physicochemical, rheological and emulsifying properties of myofibrillar protein[J]. Journal of Food Engineering, 2019, 263: 272-279.
BENJAKUL S, VISESSANGUAN W C, THONGKAEW C,et al. Comparative study on physicochemical changes of muscle proteins from some tropical fish during frozen storage[J]. Food Research International, 2003, 36(8):787-795.
COFRADES S, CARBALLO J, CARECHE M, et al. Emulsifying properties of actomyosin from several species[J]. Foodence & Technology Lebensmittel Wissenschaft & Technologie, 1996, 29(4):379-383.