Rheology and microstructure of myofibrillar protein–olive oil composite gels: effect of different non‐meat protein as emulsifier

Wu, Mangang; Fei, Litian; Zhuang, Tao; Lei, Shumin; Ge, Qingfeng; Yu, Hai; Wang, Jiahao; Wang, Yaosong

doi:10.1002/jsfa.8528

Cited by 26 publications

(13 citation statements)

References 34 publications

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“…These interactions could enhance the protein structure and retain more water. Moreover, Wu et al also observed increased WHC in heat-induced non-animal protein gels and they attributed it to a filling effect of oil droplets [ 41 ]. However, our results in Section 3.6 suggested that oil droplets are not acting as active fillers and therefore not interacting with the protein matrix, since the elastic modulus of the gels was decreasing with increasing oil content.…”

Section: Results and Discussionmentioning

confidence: 99%

Design of a Functional Pea Protein Matrix for Fermented Plant-Based Cheese

Masiá

Jensen

Petersen

et al. 2022

Foods

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The production of a fermented plant-based cheese requires understanding the behavior of the selected raw material prior to fermentation. Raw material processing affects physicochemical properties of plant protein ingredients, and it determines their ability to form fermentation-induced protein gels. Moreover, the addition of oil also influences structure formation and therefore affects gel firmness. This study focuses on identifying and characterizing an optimal pea protein matrix suitable for fermentation-induced plant-based cheese. Stability and gel formation were investigated in pea protein matrices. Pea protein isolate (PPI) emulsions with 10% protein and 0, 5, 10, 15, and 20% olive oil levels were produced and further fermented with a starter culture suitable for plant matrices. Emulsion stability was evaluated through particle size, ζ-potential, and back-scattered light changes over 7 h. Gel hardness and oscillation measurements of the fermented gels were taken after 1 and 7 days of storage under refrigeration. The water-holding capacity of the gels was measured after 7 days of storage and their microstructure was visualized with confocal microscopy. Results indicate that all PPI emulsions were physically stable after 7 h. Indeed, ζ-potential did not change significantly over time in PPI emulsions, a bimodal particle size distribution was observed in all samples, and no significant variation was observed after 7 h in any of the samples. Fermentation time oscillated between 5.5 and 7 h in all samples. Higher oil content led to weaker gels and lower elastic modulus and no significant changes in gel hardness were observed over 7 days of storage under refrigeration in closed containers. Water-holding capacity increased in samples with higher olive oil content. Based on our results, an optimal pea protein matrix for fermentation-induced pea protein gels can be produced with 10% protein content and 10% olive oil levels without compromising gel hardness.

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Section: Results and Discussionmentioning

confidence: 99%

Design of a Functional Pea Protein Matrix for Fermented Plant-Based Cheese

Masiá

Jensen

Petersen

et al. 2022

Foods

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“…The protein components of MP, CPI and composite protein were investigated according to the reported method by Wu et al, with a 12% acrylamide separation gel (pH 8.8) and a 5% acrylamide stacking gel (pH 6.8) 26 . The MP‐CPI composite sols were diluted to 1 mg mL −1 and then mixed with SDS‐PAGE leading buffer (containing SDS, β ‐mercaptoethanol, bromophenol blue and glycerol) at a ratio of 1:1.…”

Section: Methodsmentioning

confidence: 99%

Effect of chickpea (Cicer arietinum L.) protein isolate on the heat‐induced gelation properties of pork myofibrillar protein

Chen

Dong

et al. 2020

J Sci Food Agric

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BACKGROUND Heat‐induced composite gels were prepared with 30 mg mL−1 pork myofibrillar protein (MP) and chickpea protein isolate (CPI) (0, 3, 6, 9, 12, and 15 g kg−1) in 0.6 mol L−1 NaCl, at pH 7.0. The gel strength, water‐holding capacity, rheological properties, and microstructure of MP‐CPI composite gels were investigated. RESULTS Chickpea protein isolate improved (P < 0.05) gel strength and water‐holding capacity of the MP composite gels. The rheological properties of MP‐CPI composite gels were improved significantly by the addition of CPI. Meanwhile, the effects of CPI on the storage modulus of composite gels were positively correlated with the increased addition of CPI. Furthermore, according to low‐field nuclear magnetic resonance (LF‐NMR) results, the addition of CPI reduced the relaxation time of the composite gels and the relaxation peak area of free water, indicating that CPI could improve the water‐holding capacity of MP‐CPI composite gels. The microstructure of MP‐CPI composite gels presented smaller and more uniform pores, which means that more water could be retained. CONCLUSION The addition of chickpea protein isolate improved the gel strength, water‐holding capacity, rheological properties, and microstructure of MP gels, indicating that CPI could be a potential protein additive to improve the microstructure, texture, and functional quality of meat products. © 2020 Society of Chemical Industry

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“…At the same time, confocal laser scanning microscopy observations proved that zein hydrolysate could absorb to the lipid droplet surfaces and form a protective coating, helping prevent the droplets from aggregating and subsequently enhancing the oxidative stability of the MP emulsion. Likewise, various non‐meat protein additives including SPI, sodium caseinate, and egg‐white protein isolate were added into heat‐induced pork MP‐olive oil composite gels as surfactants to investigate the change in the rheological properties and microstructure of the composite gels (Wu, Fei, Zhuang, Lei, & Wang, 2017). The authors opined that adding olive oil pre‐emulsified by sodium caseinate and egg‐white protein could enhance the gel strength and improve the dynamic rheological properties of MP composite during its transformation from sol to gel.…”

Section: Modification Of Mpmentioning

confidence: 99%

Modification of myofibrillar protein functional properties prepared by various strategies: A comprehensive review

2020

Comp Rev Food Sci Food Safe

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Today, both consumers and food industry producers have exhibited an ever‐growing interest in improving and broadening the functional performance of proteins in food industry. Myofibrillar protein (MP) is mainly responsible for texture, yield and organoleptic characteristics of final meat products. To increase functional properties of MP, technological and nutritional improvement of MP is needed to modify its structure and functionalities. Considerable approaches, including additives, oxidation treatments, and novel food processing technologies, have been utilized to modify its functional properties to manufacture acceptable meat products with lower cost and more desirable nutritional characteristics. However, a comprehensive summary of structural and functional changes of MP in response to different modification strategies is still lacking. Hence, in this review paper, our main goal is first to provide an overview of the functional characteristics of MP. Then, this review will mainly discuss the current knowledge on the functional changes of MP caused by various modification methods and will present some examples of previous works and recent progress. Finally, future outlooks are presented to tailor the manufacture of functionality enhanced and value‐added muscle‐based products and enable modified MP can be applied as a novel meat ingredient in food industry.

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Rheology and microstructure of myofibrillar protein–olive oil composite gels: effect of different non‐meat protein as emulsifier

Cited by 26 publications

References 34 publications

Design of a Functional Pea Protein Matrix for Fermented Plant-Based Cheese

Design of a Functional Pea Protein Matrix for Fermented Plant-Based Cheese

Effect of chickpea (Cicer arietinum L.) protein isolate on the heat‐induced gelation properties of pork myofibrillar protein

Modification of myofibrillar protein functional properties prepared by various strategies: A comprehensive review

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