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

Guo, Xiuyun; Zhang, Yawei; Jamali, Muneer Ahmed; Peng, Zengqi

doi:10.1111/ijfs.14752

Cited by 19 publications

(8 citation statements)

References 53 publications

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“…As discussed earlier, the solubility of protein is crucial for better emulsifying properties; therefore, the higher solubility of API at pH 7 and 9 with distilled water as well as with ionic salts compared to pH 3 shows higher Г values. Similar results for Г in the presence of ionic salts have been reported for myofibrillar protein stabilize emulsion [ 28 ]. The results further suggest that the presence of ionic salts does not resist the migration of protein to the interfacial layer.…”

Section: Resultssupporting

confidence: 87%

Effects of pH and Ionic Salts on the Emulsifying and Rheological Properties of Acorn Protein Isolate

et al. 2022

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This study was designed to evaluate the emulsifying and rheological properties of acorn protein isolate (API) in different pH mediums (pH 3, 7 and 9) and in the presence of ionic salts (1 M NaCl and 1 M CaCl2). API shows higher solubility in distilled water at pH 7, while at the same pH, a decrease in solubility was observed for API in the presence of CaCl2 (61.30%). A lower emulsifying activity index (EAI), lower stability index (ESI), larger droplet sizes and slight flocculation were observed for API in the presence of salts at different pHs. Importantly, CaCl2 treated samples showed relevantly higher EAI (252.67 m2/g) and ESI (152.67 min) values at all pH as compared to NaCl (221.76 m2/g), (111.82 min), respectively. A significant increase in interfacial protein concentration (4.61 mg/m2) was observed for emulsion at pH 9 with CaCl2, while the major fractions of API were observed in an interfacial layer after SDS-PAGE analysis. All of the emulsion shows shear thinning behavior (τc > 0 and n < 1), while the highest viscosity was observed for emulsion prepared with CaCl2 at pH 3 (11.03 ± 1.62). In conclusion, API, in the presence of ionic salts at acidic, neutral and basic pH, can produce natural emulsions, which could be substitutes for synthetic surfactants for such formulations.

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Section: Resultssupporting

confidence: 87%

Effects of pH and Ionic Salts on the Emulsifying and Rheological Properties of Acorn Protein Isolate

et al. 2022

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“…Particle size distribution was measured according to our previous method using a Malvern Mastersizer 3000 (Malvern Instruments Co. Ltd., Great Malvern, UK) (Guo et al ., 2021). Water was used as a dispersant.…”

Section: Methodsmentioning

confidence: 99%

“…MP were extracted according to the method listed in our previous study (Guo et al ., 2021). The samples were processed at 0–s4 °C to minimise the proteolysis or protein denaturation.…”

Section: Methodsmentioning

confidence: 99%

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

Guo

Meng

et al. 2022

Int J of Food Sci Tech

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Summary 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.

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“…However, due to the poor functional properties of natural MP, Hou et al 10.3389/fnut.2023.1116100 MP-stabilized emulsions are usually easy to aggregate and flocculate, leading to the difficult in application of MP in the food industry (7). Furthermore, the emulsifying properties of MP are related to protein molecular size and protein conformational characteristics (8). Therefore, modification methods that can cause changes in the conformational characteristics or molecular size of MP may improve the emulsifying properties of MP, thus enhancing the quality of emulsified-type meat products.…”

Section: Introductionmentioning

confidence: 99%

Effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia (Oreochromis niloticus) myofibrillar protein

et al. 2023

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The purpose of this research was to explore the different hydrodynamic cavitation (HC) times (0, 5, 10, 15, 20 min; power 550 W, pressure 0.14 MPa) on the emulsifying properties of tilapia myofibrillar protein (TMP). Results of pH, particle size, turbidity, solubility, surface hydrophobicity, and reactive sulfhydryl (SH) group indicated that HC changed the structure of TMP, as confirmed by the findings of intrinsic fluorescence and circular dichroism (CD) spectra. Furthermore, HC increased the emulsifying activity index (EAI) significantly (P < 0.05) and changed the emulsifying stability index (ESI), droplet size, and rheology of TMP emulsions. Notably, compared with control group, the 10-min HC significantly decreased particle size and turbidity but increased solubility (P < 0.05), resulting in accelerated diffusion of TMP in the emulsion. The prepared TMP emulsion showed the highest ESI (from 71.28 ± 5.50 to 91.73 ± 5.56 min), the smallest droplet size (from 2,754 ± 110 to 2,138 ± 182 nm) and the best rheological properties, as demonstrated by the microstructure photographs. Overall, by showing the effect of HC in improving the emulsifying properties of TMP, the study demonstrated HC as a potential technique for meat protein processing.

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

Abstract: L‐Arginine changes the conformational characteristics and interfacial behaviour of myofibrillar proteins, thus improving the physical stability of soybean oil‐myofibrillar proteins emulsions.

Cited by 19 publications

References 53 publications

Effects of pH and Ionic Salts on the Emulsifying and Rheological Properties of Acorn Protein Isolate

Effects of pH and Ionic Salts on the Emulsifying and Rheological Properties of Acorn Protein Isolate

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

Effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia (Oreochromis niloticus) myofibrillar protein

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