食品与发酵工业 >

2026 , Vol. 52 >Issue 11: 261 - 270

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.042636

研究报告

不同pH值缓冲体系对骆驼肉肌原纤维蛋白及其热诱导凝胶功能特性的影响

  • 郑增拓 ,
  • 刘新旗 ,
  • TUYATSETSEG JAMBAL ,
  • 伊如勒 ,
  • 达立朝 ,
  • 梁建忠 ,
  • 李昱奇 ,
  • 吉日木图 ,
  • 孟和毕力格 ,
  • 明亮
展开
  • 1(内蒙古农业大学 食品科学与工程学院, 内蒙古 呼和浩特, 010018)
    2(中国-蒙古国生物高分子应用“一带一路”联合实验室, 内蒙古 呼和浩特, 010018)
    3(内蒙古国驼检测技术有限公司, 内蒙古 阿拉善盟, 750300)
    4(阿拉善右旗骆驼产业发展中心, 内蒙古 阿拉善盟, 750300)
    5(阿拉善右旗农业技术推广中心, 内蒙古 阿拉善盟, 750300)
    6(内蒙古农业大学 乳品生物技术与工程教育部重点实验室, 内蒙古 呼和浩特, 010018)
第一作者:硕士研究生(明亮副教授为通信作者,E-mail:bmlimau@163.com)

收稿日期: 2024-03-06

  修回日期: 2025-10-28

  网络出版日期: 2026-06-24

基金资助

中央引导地方科技发展资金项目(2025ZY0054);阿拉善盟科技计划项目(AMKJ2024-06);国家重点研发计划项目(2020YFE0203300)

收起

Effect of different pH value buffer systems on the functional properties of camel meat myofibrillar proteins and their thermally induced gels

  • ZHENG Zengtuo ,
  • LIU Xinqi ,
  • TUYATSETSEG JAMBAL ,
  • YI Rule ,
  • DA Lichao ,
  • LIANG Jianzhong ,
  • LI Yuqi ,
  • JI Rimutu ,
  • MENGHE Bilige ,
  • MING Liang
Expand
  • 1(College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, China)
    2(China-Mongolia “Belt and Road” Joint Laboratory for Biopolymer Application, Hohhot 010018, China)
    3(Inner Mongolia Guotuo Testing Technology Co.Ltd., Alxa League 750300, China)
    4(Alxa Right Banner Camel Industry Development Center, Alxa League 750300, China)
    5(Alxa Right Banner Agricultural Technology Extension Center, Alxa League 750300, China)
    6(Key Laboratory of Dairy Biotechnology and Engineering, Ministry of Education, Inner Mongolia Agricultural University, Hohhot 010018, China)

Received date: 2024-03-06

  Revised date: 2025-10-28

  Online published: 2026-06-24

Fold

摘要

该实验以骆驼肉肌原纤维蛋白(myofibrillar protein,MP)为研究对象,通过测定不同pH值体系下的骆驼肉MP的一系列指标,包括溶解性、疏水性、巯基含量、羰基含量、肌原纤维片段指数、粒径、zeta电位、SDS-PAGE、凝胶色泽和白度、凝胶保水性和微观结构,以探究不同pH值缓冲体系对骆驼肉MP及其热诱导凝胶的影响。结果显示:随着pH值的升高,MP的溶解性先增加后降低,在pH 6.5时达到最大值;疏水性逐渐降低;总巯基和活性巯基含量均呈下降趋势;羰基含量在pH 6.0时达到峰值。乳化活力指数在pH 5.5时最高,乳化液稳定系数在pH 6.5时最高。Zeta电位绝对值在pH 6.5时达到最大,粒径在pH 5.5时最大,且粒径分布随着pH值的升高而整体变小。SDS-PAGE结果显示,不同pH值下MP的蛋白条带清晰度和分子质量分布存在差异。凝胶的亮度(L*)和白度随pH值升高而增加,a*和b*随pH值上升而下降,凝胶保水性在pH 6.5时最高。微观结构观察显示,pH 6.5时凝胶结构最为致密且均匀。以上结果表明,pH值对骆驼肉MP的功能特性及其凝胶特性有显著影响,pH 6.5可能是骆驼肉MP及其凝胶的最佳pH值。该实验为骆驼肉制品的加工和研究提供了理论参考。

关键词： pH值; 肌原纤维蛋白; 骆驼肉; 功能特性; 热诱导凝胶

本文引用格式

郑增拓 , 刘新旗 , TUYATSETSEG JAMBAL , 伊如勒 , 达立朝 , 梁建忠 , 李昱奇 , 吉日木图 , 孟和毕力格 , 明亮 . 不同pH值缓冲体系对骆驼肉肌原纤维蛋白及其热诱导凝胶功能特性的影响[J]. 食品与发酵工业, 2026 , 52(11) : 261 -270 . DOI: 10.13995/j.cnki.11-1802/ts.042636

Abstract

This study focused on camel meat myofibrillar protein (MP), investigating a series of indicators across different pH value systems, including solubility, hydrophobicity, thiol content, carbonyl content, myofibrillar fragmentation index, particle size, zeta potential, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), gel color and whiteness, water-holding capacity, and microstructure.The objective was to explore the impact of various pH value buffer systems on camel MP and its thermally induced gels.Results indicated that as pH value increased, the solubility of MP initially increased then decreased, reaching its maximum at pH 6.5;hydrophobicity gradually decreased;total and reactive thiol contents both showed a decreasing trend;carbonyl content peaked at pH 6.0.Emulsification activity index was highest at pH 5.5, while emulsion stability index was highest at pH 6.5.The absolute value of the zeta potential reached its maximum at pH 6.5, whereas particle size was largest at pH 5.5, with particle size distribution becoming smaller overall as pH value increased.SDS-PAGE results revealed differences in the clarity and molecular weight distribution of protein bands under different pH value conditions.Gel brightness (L*) and whiteness increased with increasing pH, while a* and b* values decreased with rising pH value, and water-holding capacity was optimal at pH 6.5.Microstructural observations showed that at pH 6.5, the gel structure was the most compact and uniform.These findings suggest that pH value significantly affects the functional and gel-forming properties of camel MP, with pH 6.5 potentially being the optimal pH value for both MP and its gel formation.This study provides theoretical insights into the processing and research of camel meat products.

Key words： pH-value; myofibrillar proteins; camel meat; functional properties; heat-induced gels

参考文献

[1] HAMED HAMMAD MOHAMMED H, JIN G F, MA M H, et al.Comparative characterization of proximate nutritional compositions, microbial quality and safety of camel meat in relation to mutton, beef, and chicken[J].LWT, 2020, 118:108714.
[2] KADIM I T, MAHGOUB O, PURCHAS R W.A review of the growth, and of the carcass and meat quality characteristics of the one-humped camel (Camelus dromedaries)[J].Meat Science, 2008, 80(3):555-569.
[3] RAIYMBEK G, FAYE B, KADIM I T, et al.Comparative fatty acids composition and cholesterol content in Bactrian (Camelus bactrianus) and dromedary camel (Camelus dromedarius) meat[J].Tropical Animal Health and Production, 2019, 51(7):2025-2035.
[4] LIU X H, TIAN G F, ZHAO J R, et al.Integrated ultra-high pressure and salt addition to improve the in vitro digestibility of myofibrillar proteins from scallop mantle (Patinopecten yessoensis)[J].Food Chemistry, 2024, 447:138985.
[5] ROUSSEL O P, PIGNANELLI C, HUBBARD E F, et al.Effects of intensified training with insufficient recovery on joint level and single muscle fibre mechanical function:The role of myofibrillar Ca2+ sensitivity[J].Applied Physiology, Nutrition, and Metabolism, 2024, 49(12):1646-1657.
[6] ZOU Y, SHI H B, XU P P, et al.Combined effect of ultrasound and sodium bicarbonate marination on chicken breast tenderness and its molecular mechanism[J].Ultrasonics Sonochemistry, 2019, 59:104735.
[7] KIM T K, LEE M H, YONG H I, et al.Porcine myofibrillar protein gel with edible insect protein:Effect of pH-shifting[J].LWT, 2022, 154:112629.
[8] DU X, ZHAO M N, PAN N, et al.Tracking aggregation behaviour and gel properties induced by structural alterations in myofibrillar protein in mirror carp (Cyprinus carpio) under the synergistic effects of pH and heating[J].Food Chemistry, 2021, 362:130222.
[9] ZHENG S Y, CHEN X T, WU J N, et al.Effect of pH on gelling properties of myofibrillar protein in large yellow croaker (Pseduosciaena croeca)[J].Journal of Biobased Materials and Bioenergy, 2019, 13(2):264-268.
[10] DING Y Q, LIU Y M, YANG H, et al.Effects of CaCl2 on chemical interactions and gel properties of surimi gels from two species of carps[J].European Food Research and Technology, 2011, 233(4):569-576.
[11] DAI H J, SUN Y, XIA W Y, et al.Effect of phospholipids on the physicochemical properties of myofibrillar proteins solution mediated by NaCl concentration[J].LWT, 2021, 141:110895.
[12] CHELH I, GATELLIER P, SANTÉ-LHOUTELLIER V.Technical note:A simplified procedure for myofibril hydrophobicity determination[J].Meat Science, 2006, 74(4):681-683.
[13] OLIVER C N, AHN B W, MOERMAN E J, et al.Age-related changes in oxidized proteins[J].Journal of Biological Chemistry, 1987, 262(12):5488-5491.
[14] WEI L, CAO L W, XIONG S B, et al.Effects of pH on self-assembly of silver carp myosin at low temperature[J].Food Bioscience, 2019, 30:100420.
[15] ILIAN M A, BEKHIT A E, BICKERSTAFFE R.The relationship between meat tenderization, myofibril fragmentation and autolysis of calpain 3 during post-mortem aging[J].Meat Science, 2004, 66(2):387-397.
[16] WANG Z M, LI L, JIA F Y, et al.Exploring the effect of pH-shifting on the gel properties and interaction of heat-induced Flammulina velutipes polysaccharide-porcine myofibrillar protein for improving the quality of Flammulina velutipes-pork patties[J].Food Chemistry, 2025, 465:142187.
[17] LAEMMLI U K.Cleavage of structural proteins during the assembly of the head of bacteriophage T4[J].Nature, 1970, 227(5259):680-685.
[18] CHEN Z H, DAI Z C, LIU C H, et al.Microbial transglutaminase promotes cross-linking for enhancing gelation of myofibrillar protein in frozen Litopenaeus vannamei through deamination reaction[J].Food Hydrocolloids, 2024, 147:109332.
[19] NI N, WANG Z Y, HE F, et al.Gel properties and molecular forces of lamb myofibrillar protein during heat induction at different pH values[J].Process Biochemistry, 2014, 49(4):631-636.
[20] LEE C H, CHIN K B.Influence of the pH and salt concentrations on physicochemical properties of pork myofibrillar protein gels added with cornstarch[J].Food Science of Animal Resources, 2020, 40(2):254-261.
[21] CHAN J T Y, OMANA D A, BETTI M.Effect of ultimate pH and freezing on the biochemical properties of proteins in Turkey breast meat[J].Food Chemistry, 2011, 127(1):109-117.
[22] XUE C F, PEI Z S, WEN P, et al.Effects of pH and NaCl on the spatial structure and conformation of myofibrillar proteins and the emulsion gel system:Insights from computational molecular dynamics on myosin of golden pompano[J].Gels, 2023, 9(4):270.
[23] KONG D W, HAN R W, YUAN M D, et al.Ultrasound combined with slightly acidic electrolyzed water thawing of mutton:Effects on physicochemical properties, oxidation and structure of myofibrillar protein[J].Ultrasonics Sonochemistry, 2023, 93:106309.
[24] LE H S, TING L, JUN C, et al.Gelling properties of myofibrillar protein from abalone (Haliotis discus Hannai Ino) muscle[J].International Journal of Food Properties, 2018, 21(1):277-288.
[25] YU Q Q, HONG H, LIU Y Y, et al.Oxidation affects pH buffering capacity of myofibrillar proteins via modification of histidine residue and structure of myofibrillar proteins[J].International Journal of Biological Macromolecules, 2024, 260:129532.
[26] PAN N, WAN W, DU X, et al.Mechanisms of change in emulsifying capacity induced by protein denaturation and aggregation in quick-frozen pork patties with different fat levels and freeze-thaw cycles[J].Foods, 2021, 11(1):44.
[27] LI H Y, ZHAO M H, LI J H, et al.Advancing the pH-driven encapsulation technique of curcumin:Molecular interaction shifts due to structural and charge variations[J].Food Hydrocolloids, 2024, 152:109952.
[28] ZHOU Y, WANG Y, HE J, et al.Evaluating the profile of myofibrillar proteins and its relationship with tenderness among five styles of dry-cured hams[J].International Journal of Food Science & Technology, 2021, 56(1):259-268.
[29] 董智铭, 么紫瑶, 姜萩婉, 等.超声功率对牛肉干品质及牛肉肌原纤维蛋白结构的影响[J].食品科学, 2023, 44(19):27-34.
DONG Z M, YAO Z Y, JIANG Q W, et al.Effect of ultrasonic power on the quality and myofibrillar protein structure of beef jerky[J].Food Science, 2023, 44(19):27-34.
[30] ZHANG T, XUE Y, LI Z J, et al.Effects of ozone-induced oxidation on the physicochemical properties of myofibrillar proteins recovered from bighead carp (Hypophthalmichthys nobilis)[J].Food and Bioprocess Technology, 2015, 8(1):181-190.
[31] LIU Q, CHEN Q, KONG B H, et al.The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp (Cyprinus carpio) surimi[J].LWT - Food Science and Technology, 2014, 57(2):603-611.
[32] MA W H, YANG Q, FAN X, et al.Modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathione[J].Food Chemistry, 2022, 14:100318.
[33] 屈莎, 胡婷, 唐善虎, 等.牦牛肉肌原纤维蛋白在不同pH值条件下的分子结构变化[J].现代食品科技, 2023, 39(8):85-93.
QU S, HU T, TANG S H, et al.Molecular structure changes of yak myofibrillar proteins via protein oxidation at different pH values[J].Modern Food Science & Technology, 2023, 39(8):85-93.
[34] GE L H, XU Y S, XIA W S, et al.Synergistic action of cathepsin B, L, D and calpain in disassembly and degradation of myofibrillar protein of grass carp[J].Food Research International, 2018, 109:481-488.
[35] BOETTGER D, BERGMANN H, KUEHN B, et al.Evolutionary imprint of catalytic domains in fungal PKS-NRPS hybrids[J].ChemBioChem, 2012, 13(16):2363-2373.
[36] 董唯, 白登荣, 窦川林, 等.不同体系条件下γ-聚谷氨酸复合TGase处理对肌原纤维蛋白功能性质的影响[J].肉类研究, 2018, 32(5):1-8.
DONG W, BAI D R, DOU C L, et al.Effects of γ-polyglutamic acid combined with transglutaminase treatment on the functional properties of myofibrillar protein under different conditions[J].Meat Research, 2018, 32(5):1-8.
[37] WANG Y D, ZHUANG Y, YAN H, et al.The influence of pH and monovalent/divalent cations on the structural and physicochemical properties of myofibrillar protein from silver carp[J].Food Chemistry, 2023, 404:134519.
[38] 屈莎, 胡婷, 唐善虎, 等.不同pH值下蛋白氧化对牦牛肉肌原纤维蛋白凝胶特性的影响[J].现代食品科技, 2024, 40(1):121-127.
QU S, HU T, TANG S H, et al.Effects of protein oxidation at different pH values on the gelling properties of myofer fibroin in yak muscle[J].Modern Food Science & Technology, 2024, 40(1):121-127.
[39] SIRISON J, ISHII T, MATSUMIYA K, et al.Comparison of surface and foaming properties of soy lipophilic protein with those of glycinin and β-conglycinin[J].Food Hydrocolloids, 2021, 112:106345.
[40] ZHANG Z Y, REGENSTEIN J M, ZHOU P, et al.Effects of high intensity ultrasound modification on physicochemical property and water in myofibrillar protein gel[J].Ultrasonics Sonochemistry, 2017, 34:960-967.
Options
文章导航

/

〈 〉

技术支持：北京玛格泰克科技发展有限公司