Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review

To improve the quality of meat products is a constant focus for both the meat industry and scientists. As major components in meat protein, the gelation properties of myofibrillar proteins (MPs) predominantly determine the sensory quality and product yield of the final product. Naturally or artificially occurring covalent modifications are known to largely affect MP functionality by changing the protein structure and forming aggregates, leading to both favorable and unfavorable outcomes. The review aims to summarize the mechanisms associated with several covalent modifications and the recent developments in enhancing MP gelation properties. Various extrinsic and intrinsic parameters controlling oxidation, phenolic–protein interactions, enzyme catalysis, glycation, and isoelectric solubilization/precipitation, and their effects on the characteristics of heat-induced MP gels are discussed. This article provides an improved understanding of the covalent modifications that occur mainly in the MP system and how they can be utilized to promote its gelation properties. Covalent modifications exhibited dose-dependent and dual-role manners for MP gelation properties. Mild oxidation, enzyme catalysis, and isoelectric solubilization/precipitation treatment would be beneficial to form more aligned and cross-linked three-dimensional networks for MP gels because of moderate protein aggregation. However, an excessive aggregate impedes the MP gelation behavior, leading to reduced gelation quality. Glycation effectively increased hydrophilicity of MPs and phenolic conjugation provides MPs with novel bioactivity. A proper utilization of such a process or even a rational combination of them allowed us to enhance the gelation properties of MP with assorted appreciated functionalities and further improve the quality of meat products.     

Effect of microwave heating time on the gel properties of chicken myofibrillar proteins and their formation mechanism

The present work was conducted to illustrate the mechanism of gel formation of myofibrillar proteins (MPs) under different microwave heating times. The results showed that the denaturation enthalpy (ΔH) of the MPs significantly decreased when the heating time increased from 3 to 9 s and then completely disappeared as the heating time progressed, indicating that the MPs gradually denatured and subsequently aggregated with increasing heating time, which was further verified by the changes in the secondary structure, electrophoretic bands, and gel properties (e.g., water holding capacity and textural profiles) of the MPs. Microstructural images indicated that the MP gel formed under 12 s had the most compact network, indicating that extended microwave heating time could induce quality deterioration of MP gels. Moreover, the hydrophobic forces, electrostatic forces, and disulphide bonds of the MPs gradually intensified with increasing microwave heating time, suggesting that both non-covalent and covalent bonds could promote molecular denaturation and subsequent aggregation of MPs. In addition, correlation analysis revealed that the changes in the molecular conformation of MPs induced by different microwave heating times could effectively regulate the formation of MP gels and their related properties.     

Contribution of sarcoplasmic proteins to myofibrillar proteins gelation

Surimi, a refined protein extract, is produced by solubilizing myofibrillar proteins during the comminuting and salting stages of manufacturing. The resulting paste gels on heating to produce kamaboko or a range of analog shellfish such as crab claw, filament sticks, fish mushroom, and so on. The myosin molecule is the major myofibrillar protein in gelation. It is believed that washing steps during the traditional surimi process play an important role in enhancing the gel properties of the resultant kamaboko by removing water-soluble (sarcoplasmic, Sp-P) proteins. By contrast, some researchers claim that retaining Sp-P or adding it into the surimi gel network not only does not interfere with the action of myofibrillar proteins during the sol-gel transition step but also improves the gel characteristics of the resultant kamaboko. It seems that retention of Sp-P or their addition into raw surimi does enhance the textural properties of kamaboko gel perhaps by functioning as a proteinase inhibitor, particularly against trypsin and trypsin-like proteinases but this depends on the type of applied surimi process. Among different types of Sp-P, it has been claimed that some proteins such as endogenous transglutaminase (TGase) play a more important role than other Sp-P in bond formation, by catalyzing the cross-linking of myosin heavy chain (MHC) molecules during low-temperature setting of surimi, resulting a more elastic kamaboko gel.     

鱼类肌原纤维蛋白热凝及流变特性研究进展

综述国内外有关肌原纤维蛋白热凝及流变性质最新研究进展,包括肌原纤维蛋白的组成、结构、性质、热凝机制和热凝动态流变等研究,并介绍影响热凝流变的主要因素。     

Interaction of fish myoglobin and myofibrillar proteins

ABSTRACT:  Interactions between fish myoglobin (Mb) and myofibrillar proteins were investigated in a Mb-natural actomyosin (NAM) model at 4 °C. Increases in metmyoglobin (MetMb) formation and the relative content of bound Mb were observed, as were decreases in whiteness and Ca²⁺-ATPase activity ( P < 0.05). During the first 6 h of incubation, Mb bound preferably to myosin at domains other than the head portion, as evidenced by measurable ATPase activity. The potential binding of Mb to myosin heads occurred after 24-h incubation as evidenced by the marked decrease in Ca²⁺-ATPase activity of the NAM–Mb mixture when compared to that of NAM alone ( P < 0.05). The interaction between fish Mb and myofibrillar proteins was more pronounced with increased storage time; formation of high-molecular-weight aggregates (> 206 kDa) also increased with time. Electrophoretic study revealed that disulfide bonds were not involved in Mb–NAM interactions.     

Improving the oxygen barrier of microcapsules using cellulose nanofibres

In this study, the oxygen barrier and physical properties of two maltodextrin/gum Arabic (MD/GA) (3:1 w/w) microcapsules with dextrose equivalence (DE) 26 and 6 were assessed with or without the incorporation of cellulose nanofibres (CNF). The oxygen diffusion coefficient (D_eff) was between 10.6 × 10⁻¹⁵ m² s⁻¹ and 17.3 × 10⁻¹⁵ m² s⁻¹ for all microcapsules. The addition of CNF improved the oxygen barrier of MD/GA microcapsules. The incorporation of CNF did not significantly impact T_g due to the low quantity of CNF present in the microcapsules. Wettability was higher in CNF incorporated microcapsules, and dispersibility was lower only for microcapsules with maltodextrin of DE 26. Spray-dried microcapsules exhibited poor flowability and high cohesiveness due to the moisture content (2.0–2.5%) of the powders. The results suggest that incorporation of CNF can increase the oxygen barrier of MD/GA microcapsules which may lead to better oxidative stability of micronutrients incorporated in the microcapsules.     

不同盐浓度下黄原胶对大豆分离蛋白—肌原纤维蛋白复合凝胶性质的影响

研究不同盐浓度下黄原胶对大豆分离蛋白(SPI)—肌原纤维蛋白(MP)复合体系凝胶特性和结构的影响。结果表明:在0.1,0.3 mol/L NaCl条件下,低含量SPI有利于MP—SPI复合体系的凝胶及提高凝胶持水性;黄原胶也可提高MP—SPI复合凝胶的持水性。环境扫描电镜显示:黄原胶的强持水能力及大豆蛋白的填充起到了凝胶促进作用。在高盐浓度下,SPI的加入,对于MP—SPI复合凝胶强度和持水性均有破坏效应;对于纯MP凝胶,黄原胶的加入会弱化凝胶强度,但可提升凝胶持水性;对于MP—SPI复合凝胶样品,随着黄原胶用量的增加,肌纤维蛋白—大豆蛋白复合凝胶的凝胶强度和持水性均呈现增加趋势。说明多糖—MP—SPI复合体系中,三者相互作用受盐浓度影响显著,在低盐条件下,低浓度大豆蛋白和高浓度黄原胶的加入可较好地改善复合蛋白凝胶性质。     

Manipulating interfacial behaviour and emulsifying properties of myofibrillar proteins by L-Arginine at low and high salt concentration

The present work examined the impact of L-Arginine (Arg) on the emulsifying properties, interfacial behaviour and conformational characteristics of myofibrillar proteins (MPs) at high (0.6 m ) and low (0.15 m ) salt concentration to maintain good emulsifying properties of MPs at low salt concentration. The data indicated that Arg increased the emulsifying activity index/emulsion stability index (EAI/ESI) and decreased the CI and droplet size of emulsions regardless of salt concentration. Raman spectra revealed that the α-helix content decreased from 60.30% to 51.26% at high salt concentration, and from 60.20% to 54.82% at low salt concentration in the presence of Arg. In addition, MPs treated with Arg exhibited a higher interfacial pressure and more rapidly diffusion to the oil surface. Meanwhile, Arg increased the interfacial protein loading. The results demonstrated that Arg caused the unfolding of MPs, promoting the adsorption of proteins and decreasing the interfacial tension, ultimately improving the stability of emulsions at low salt concentration.     

冷冻-解冻肌原纤维蛋白结构评价技术研究进展

肌肉类食品在加工和运输中常常经历冷冻-解冻的过程,严重破坏肌原纤维蛋白的结构与功能特性,进而降低肌肉食品的食用价值。因此,评价肌原纤维蛋白冷冻-解冻过程中结构特性的变化对于监测冻融肌肉食品的加工食用价值具有重要意义。本文针对现代检测技术在评价冻融肌原纤维蛋白结构特性方面的研究进展和应用情况进行了系统总结和分析,主要介绍了光谱学技术、显微镜技术、核磁共振技术、蛋白组学和分子动力学模拟等技术的研究应用现状。此外,比较了上述不同检测技术的优缺点,并对现代检测技术在评价肌原纤维蛋白品质特性方面的未来发展方向进行了展望,未来需进一步优化相关检测技术,使其操作更简单、更易实施,以期在冷冻肉品生产和加工工业化中推广应用并提供技术支持,旨在为提高冷冻肌肉食品品质提供科学参考。     

Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins

ABSTRACT:  The effects of ionic strength (0, 0.3, and 0.6 M KCl) and temperature (4 and 25 °C) on the interaction between fish myoglobin and myofibrillar proteins were investigated in a model system. Increases in the relative content of bound myoglobin and metmyoglobin formation in myoglobin-natural actomyosin (NAM) mixtures with concurrent decreases in whiteness and Ca²⁺-ATPase activity were observed with increasing ionic strength ( P < 0.05). The relative content of bound myoglobin and the oxidation of oxymyoglobin were generally greater at 25 °C than at 4 °C ( P < 0.05). Binding of myoglobin to NAM resulted in decreased whiteness ( P < 0.05). Ca²⁺-ATPase was not affected by temperature ( P > 0.05). SDS-PAGE patterns of protein samples suggested that myoglobin-NAM interactions did not involve disulfide bonds. The formation of high-molecular-weight aggregates (>206 kDa) was observed and was more pronounced at higher ionic strength and higher temperature.     

Transglutaminase Cross-linking of Whey/Myofibrillar Proteins and the Effect on Protein Gelation

ABSTRACT: Transglutaminse (TGase)-catalyzed interactions of whey (WPI)/myofibrillar (MPI) protein isolates were investigated under 5 conditions: (1) ionic strengths; (2) calcium/ethylenediaminetetra-acetic acid (EDTA); (3) enzyme:substrate ratio; (4) WPI:MPI ratio; and (5) preheating of WPI (80 °C). TGase treatments of MPI in distilled water converted myosin heavy chain and actin into lower-molecular-weight polypeptides. The reaction, accelerated by the presence of WPI but diminished by NaCl, was completely reversed upon extended incubation. There was no visible WPI/MPI cross-linking; and the enzyme:substrate or WPI:MPI ratio, preheating, calcium, and EDTA did not influence the enzyme reaction. TGase treatment did not alter the melting pattern of WPI/MPI mixtures, but markedly enhanced their thermal gelling ability.     

Oxidative characteristics and gel properties of porcine myofibrillar proteins affected by l-lysine and l-histidine in a dose-dependent manner at a low and high salt concentration

This study investigated the effects of l -lysine (Lys) and l -histidine (His) on the oxidative characteristics and gel properties of porcine myofibrillar proteins (MP). Results showed that Lys and His had a strong ferrous ion-chelating ability and hydroxyl radical-scavenging activity. Moreover, Lys and His inhibited the protein carbonyl formation and MP aggregation at 0.2 M and 0.6 M NaCl, respectively, in a dose-dependent manner. Furthermore, 2 and 4 mg mL⁻¹ Lys and His decreased the oxidation-induced loss of the tertiary structure of MP accompanied by the lower surface hydrophobicity. The water-holding capacity and gel strength of MP gels increased with increasing Lys and His concentrations due to more regular and lamellar structures with smaller and homogeneous pores at 0.6 M NaCl and more orderly crosslinking via fibrous filament at 0.2 M NaCl. In summary, Lys and His chelated the ferrous ions and scavenged hydroxyl radicals, decreased the oxidation-induced physicochemical changes, thus preventing oxidative damage during the formation of a three-dimensional gel network, which resulted in better gel quality.     

Evaluation of pH‐treated fish sarcoplasmic proteins on rheological properties of fish myofibrillar protein mediated by microbial transglutaminase

Fish sarcoplasmic protein (SP) could be exploited in the water‐holding agent for fish protein gels, except that the gel strength is reduced. The adjustment of pH could modify protein interactions to overcome the inferior effect. Fish SP solutions were adjusted to pH 3 or 12, neutralised to pH 7 and lyophilised to be pH‐treated SPs. These SPs along with lyophilised untreated SP (Normal SP) were incorporated into fish myofibrillar protein (MP) with microbial transglutaminase (MTG). The denaturation temperature (T_d) of MP mixed with normal SP was 66 °C with the lowest shear stress value. The denaturation of MP mixed with pH‐treated SP reduced to be 57 °C, resulting in increased shear stress. The cooking loss of MP gel was reduced by adding pH‐treated SPs, while the breaking forces were similar to control. The result indicated that pH‐treated SPs could be used to reduce cooking loss of MTG‐mediated MP gels without affecting the gelling properties.     

微纳米纤维素材料的微流控制备技术研究进展

为深入分析微流控技术制备微纳米纤维素材料的研究现状,促进其在各领域应用,综述了以纤维素及纳米纤维素为原料,以微流控技术为基础,结合快速冷冻法、原位界面络合法等技术,制备纤维素及纳米纤维素微球和微胶囊、纤维长丝、薄膜、微管、水凝胶的最新研究进展;针对微流控技术制备微纳米纤维素材料存在的挑战,提出了克服材料缺陷,提升微通道...     

Post-mortem changes in myofibrillar proteins of breast and leg muscles from broilers,spent hens and Taiwanese Country Chickens

Post mortem ageing at 4°C was studied in the breast and leg muscles from broilers, White Leghorn spent hens and Taiwanese Country Chickens (TCC). Purified myofibrils were prepared from muscles after 0, 1, 3, 5, and 7 days of post mortem storage at 4°C. SDS-PAGE was used to examine the changes in myofibrillar proteins of the muscles. Results showed that 30 kDa components appealed earlier in the breast muscles than in the leg muscles and in the order: broiler, TCC, and spent hen. The intensity of 30 kDa band increased with post mortem time. In the breast muscles, a decrease in the intensity of the α-actinin band could be observed at 1 day post mortem in broilers and TCC and at 3 days post mortem in spent hens. This decrease, however, could not be found in the leg samples until 5 or 7 day post mortem. Titin 1 band disappeared within 3 day post mortem in the breast samples but within 5 days in the leg samples. Similar results could be observed in the degradation of nebulin although traces of nebulin remained in the teg muscles of TCC after 7 days post mortem.