Food and Fermentation Industries >

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

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

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
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  • 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

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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

Cite this article

ZHENG Zengtuo , LIU Xinqi , TUYATSETSEG JAMBAL , YI Rule , DA Lichao , LIANG Jianzhong , LI Yuqi , JI Rimutu , MENGHE Bilige , MING Liang . Effect of different pH value buffer systems on the functional properties of camel meat myofibrillar proteins and their thermally induced gels[J]. Food and Fermentation Industries, 2026 , 52(11) : 261 -270 . DOI: 10.13995/j.cnki.11-1802/ts.042636

References

[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.
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