•  
  •  
 

Abstract

Objective:The objective of this study is to investigate the protein changes mechanism of buffalo meat during low temperature storage.Methods:Buffalo meat samples were stored at 4, -18 and -60 ℃, respectively, and the contents of total protein, surface hydrophobicity, total sulfhydryl, free sulfhydryl and carbonyl values were determined, following the analysis of the correlation among those protein indicators. Results:The results showed that the contents of total protein, total sulfhydryl and free sulfhydryl of buffalo meat decreased, with the extension of storage time, while the surface hydrophobicity and carbonyl value of buffalo meat increased. The protein oxidation increased showing linear relationship to the storage temperature. During cold or frozen storage, the total protein content was extremely significantly positively correlated with the contents of total sulfhydryl and free sulfhydryl (P<0.01), while negatively correlated with surface hydrophobicity and carbonyl value (P<0.01). The surface hydrophobicity was extremely significantly positively correlated with carbonyl value (P<0.01), while negatively correlated with the contents of total protein, total sulfhydryl and free sulfhydryl (P<0.01).Conclusion: The degree of protein oxidation of buffalo meat stored at -60 ℃ was the lowest, with the quality characteristics of buffalo meat maintained better, and its fresh-keeping effect was better than that of buffalo meat stored at 4 ℃ and -18 ℃.

Publication Date

7-7-2022

First Page

137

Last Page

142

DOI

10.13652/j.issn.1003-5788.2022.02.023

References

[1] 刘纯友,付春婷,许金蓉,等.低温贮藏过程中水牛肉品质变化研究[J].食品工业科技,2020,41(2):273-278.LIU Chun-you,FU Chun-ting,XU Jin-rong,et al.Quality changes of buffalo meat during low temperature storage[J].Science and Technology of Food Industry,2020,41(2):273-278.
[2] STASIO L D,BRUGIAPAGLIA A.Current knowledge on river buffalo meat:A critical analysis[J].Animals,2021,11:2 111.
[3] CRUZ L D,GIBSON T J,GUERRERO-LEGARRETA I,et al.The welfare of water buffaloes during the slaughter process:A review[J].Livestock Science,2018,212:22-33.
[4] 李倩,尉立刚,杨钰昆,等.冻藏时间对猪肉中肌原纤维蛋白氧化程度的影响[J].食品与机械,2020,36(1):157-160,165.LI Qian,WEI Li-gang,YANG Yu-kun,et al.Effect of freezing time on the degree of oxidation of myofibrillar protein in pork[J].Food & Machinery,2020,36(1):157-160,165.
[5] 刘爽,李翔,唐华丽.类PSE禽肉(肉鸡、火鸡)加工特性及蛋白质功能性质改善研究进展[J].食品与机械,2021,37(5):209-214.LIU Shang,LI Xiang,TANG Hua-li.Progress in processing characteristics and improving functional properties of proteins in PSE-like poultry meat(broiler and turkey)[J].Food & Machinery,2021,37(5):209-214.
[6] BAO Y,ERTBJERG P.Effect of protein oxidation on the texture and water-holding of meat:A review[J].Critical Reviews in Food Science and Nutrition,2018,59(22):3 564-3 578.
[7] 孟彤,刘源,仇春泱,等.蛋白质氧化及对肉品品质影响[J].中国食品学报,2015,15(1):173-181.MENG Tong,LIU Yuan,CHOU Chun-yang,et al.Research progress on protein oxidation mechanisms and its effects on meat quality[J].Journal of Chinese Institute of Food Science and Technology,2015,15(1):173-181.
[8] LU Xiao,ZHANG Yi-min,XU Bao-chen,et al.Protein degradation and structure changes of beef muscle during superchilled storage[J].Meat Science,2020,168:108180.
[9] HOLMAN B W,COOMBS C E,MORRIS S,et al.Effect of long term chilled(up to 5 weeks)then frozen(up to 12 months)storage at two different sub-zero holding temperature on beef:3.Protein structure degradation and a marker of protein oxidation[J].Meat Science,2018,139:171-178.
[10] PARK D,XIONG Y L,ALDERTON A L,et al.Biochemical changes in myofibrillar protein exposed to three oxidizing systems[J].Journal of Agricultural and Food Chemistry,2006,54(12):4 445-4 451.
[11] CHELH I,GATELLIER P,SANTE L.Technical note:A simplified procedure for myofibril hydrophobicity determination[J].Meat Science,2006,74(4):681-683.
[12] 周果,杨文鸽,崔燕,等.超高压处理对三疣梭子蟹感官及其肌原纤维蛋白生化特性的影响[J].食品科学,2017,38(23):269-274.ZHOU Guo,YANG Wen-ge,CUI Yan,et al.Effect of ultra-high pressure on sensory and biochemical properties of myofibrillar protein from Portunus trituberculatus[J].Food Science,2017,38(23):269-274.
[13] RYSMAN T,HECKE T V,POUKE C V,et al.Protein oxidation and proteolysis during storage and in vitro digestion of pork and beef patties[J].Food Chemistry,2016,209:177-184.
[14] 马丽华,王卫东,宋慧,等.不同包装对肉品贮藏期间蛋白质氧化影响的研究[J].食品科技,2017,42(5):106-110.MA Li-hua,WANG Wei-dong,SONG Hui,et al.Effect of different manner of packing on protein oxidation in the storage period of meat[J].Food Science and Technology,2017,42(5):106-110.
[15] SHAFI J,WAHEED K N,YAQOOB S S,et al.Effect of icing on quality of silver carp during frozen storage[J].Journal of Food Processing and Preservation,2020,44:e14654.
[16] FENG Xian-chao,LI Chen-yi,ULLAH Niamat,et al.Susceptibility of whey protein isolate to oxidation and changes in physicochemical,structural,and digestibility characteristics[J].Journal of Dairy Science,2015,98(11):7 602-7 613.
[17] SANO T,OHNO T,OTSUKA-FUCHINO H,et al.Carp natural actomyosin:Thermal denaturation mechanism[J].Journal of Food Science,2010,59(5):1 002-1 008.
[18] TAO Ying-mei,MA Lu,LI Dong-dong,et al.Changes in oxidation and secondary structure of myofibrillar protein,water distribution,and quality of vacuum packaged Tan mutton during storage at different temperatures[J].Journal of Food Processing and Preservation,2021,45:e15647.
[19] ZHANG Ming-cheng,HAILI Niu,CHEN Qian,et al.Influence of ultrasound-assisted immersion freezing on the freezing rate and quality of porcine longissimus muscles[J].Meat Science,2018,136:1-8.
[20] LI Fang-fei,DU Xin,REN Yan-ming,et al.Impact of ice structuring protein on myofibrillar protein aggregation behavior and structure property of quick-frozen patty during frozen storage[J].International Journal of Biological Macromolecules,2021,178:136-142.

Share

COinS
 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.