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Meat Proteins: Processing Functionality, Structure-Function Relationships and Interactions

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A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Physics and (Bio)Chemistry".

Deadline for manuscript submissions: closed (31 July 2022) | Viewed by 16273

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Prof. Dr. Peng Wang

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Guest Editor

College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
Interests: meat protein; meat quality; molecular assembly; bioavailability
Special Issues, Collections and Topics in MDPI journals

Dr. Shengjie Li

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Guest Editor

School of Food Science and Technology, Dalian Polytechnic University, Dalian, China
Interests: meat protein; meat processing
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In meat proteins, functional properties generally refer to the physicochemical performance of meat proteins in processing. Texture, moisture retention, solubility/extractability, and emulsification of processed meat foods are influenced by the functionality of the protein. Driven by the demand for new products with less fat, less salt, and more bioactive substances, researchers working on meat products are forced to improve the functionality of meat proteins. However, this is still limited to an understanding of structure–function mechanisms of protein based innovative meat food.

The goal of this Special Issue is to inspire the innovation of knowledge and technology in the topic of “Meat Proteins: Processing Functionality, Structure–Function Relationships and Interactions”. Specifically, this Special Issue should include but is not limited to the following fields: i) structural modification by physical fields for value-added meat food; ii) chemical modification on meat proteins to get improved functional food; iii) meat proteins as an emulsifier to form functional fatty acid meat food emulsion; iv) construction of meat proteins to make new food materials and deliver active substances; v) relationships and interactions between muscle food proteins structure and 3D printability.

Prof. Dr. Peng Wang
Dr. Shengjie Li
Guest Editors

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Keywords

meat proteins
meat protein gelation
meat protein emulsion
protein structure–function relationship
protein structure–function interaction
protein physical modification
protein chemical modification

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Published Papers (6 papers)

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Research

14 pages, 1162 KiB

Open AccessArticle

Effect of Oudemansiella raphanipies Powder on Physicochemical and Textural Properties, Water Distribution and Protein Conformation of Lower-Fat Pork Meat Batter

by Yingying Zhao, Yanqiu Wang, Ke Li and Igor Mazurenko

Foods 2022, 11(17), 2623; https://doi.org/10.3390/foods11172623 - 29 Aug 2022

Cited by 4 | Viewed by 2304

Abstract

The effects of the addition of different amounts (0%, 1%, 2%, 3% and 4%) of Oudemansiella raphanipies powder (ORP) to lower-fat pork batter on its physicochemical, textural and rheological properties, water distribution and protein conformation were evaluated. The results showed that the addition of ORP from 0% to 4% significantly decreased the pH and L* value of pork batter (p < 0.05); however, it also increased the a* value and enhanced the cooking yield of pork batter from 77% to 92%. Pork batter with 1–2% ORP added had an improved texture profile and a higher storage modulus (G’), but the addition of 3–4% ORP resulted in an inferior texture of pork batter and G’. LF-NMR showed that the addition of ORP significantly increased the peak area ratio of immobile water and reduced the peak area ratio of free water (p < 0.05). ORP significantly affected protein secondary structure of pork batter. The α-helix content of pork batter with 1–2% ORP decreased and β-sheet content increased. Overall, the addition level of 1–2% ORP effectively improved the texture and water holding capacity of lower-fat emulsified sausage and provides a new reference for developing nutritional meat products. Full article

(This article belongs to the Special Issue Meat Proteins: Processing Functionality, Structure-Function Relationships and Interactions)

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13 pages, 2802 KiB

Open AccessArticle

The Impacts of Different Pea Protein Isolate Levels on Functional, Instrumental and Textural Quality Parameters of Duck Meat Batters

by Xueshen Zhu, Beibei Tan, Ke Li, Shaohua Liu, Ying Gu, Tianlan Xia, Yun Bai, Peng Wang and Renlei Wang

Foods 2022, 11(11), 1620; https://doi.org/10.3390/foods11111620 - 30 May 2022

Cited by 7 | Viewed by 2415

Abstract

This study aimed to investigate the effect of pea protein isolate (PPI) on the functional, instrumental and textural quality parameters of duck meat batters (DMB). Ground duck breast meat was mixed with different concentrations of PPI (0%, 3%, 6% or 9%, w/w) to prepare DMB. The color, cooking yield, water-holding capacity, water distribution and migration, rheological properties and texture profile of the DMB were evaluated. The results showed that the L* value of the gel decreased and the b* value increased with the increasing pea protein addition. The cooking yield and water-holding capacity showed a gradual increase, but the difference was not significant (p > 0.05). Compared with the control, the storage modulus (G′) and loss modulus (G″) were higher at the beginning and at the end and increased with the addition of pea protein, which was in accordance with the Fourier series relationship. The hardness, chewiness and gumminess of the gels gradually increased; on the contrary, the springiness and cohesiveness first increased and then decreased, respectively, reaching a maximum value of 0.96 and 0.81 when the addition amount reached 6%. Adding pea protein to the gels not only increased the area of immobilized water but also decreased the area of free water, thus improving the water-holding capacity of the batters. Therefore, pea protein can promote the formation of a stable and elastic network structure of duck meat batters. Full article

(This article belongs to the Special Issue Meat Proteins: Processing Functionality, Structure-Function Relationships and Interactions)

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14 pages, 45515 KiB

Open AccessArticle

Effects of Tea Polyphenol Palmitate Existing in the Oil Phase on the Stability of Myofibrillar Protein O/W Emulsion

by Jianchao Li, Zongyun Yang, Zhen Li, Ling Wu, Juan Shen, Jinhua Wang and Peng Wang

Foods 2022, 11(9), 1326; https://doi.org/10.3390/foods11091326 - 2 May 2022

Cited by 4 | Viewed by 2143

Abstract

This study aimed to explore the effect of adding different concentrations (0, 0.01%, 0.03%, and 0.05% (w/w)) of tea polyphenol palmitate (TPP) in the oil phase on the emulsifying properties of 5 and 10 mg/mL myofibrillar protein (MP). Particle size results revealed that the flocculation of droplets increased as TPP concentration increased and that droplets in 5 mg/mL MP emulsions (25–34 μm) were larger than in 10 mg/mL MP emulsions (14–22 μm). The emulsifying activity index of 5 mg/mL MP emulsions decreased with increasing TPP concentration. The micrographs showed that the droplets of MP emulsions exhibited extensive flocculation at TPP concentrations >0.03%. Compared with 5 mg/mL MP emulsions, 10 mg/mL MP emulsions showed better physical stability and reduced flocculation degree, which coincided with lower delta backscattering intensity (ΔBS) and Turbiscan stability index values. The flow properties of emulsions can be successfully depicted by Ostwald–de Waele models (R² > 0.99). The concentrations of TPP and protein affect the K values of emulsions (p < 0.05). Altogether, increased protein concentration in the continuous phase could improve emulsion stability by increasing viscosity, offsetting the adverse effects of TPP to a certain extent. This study is expected to promote the rational application of TPP in protein emulsion products of high quality and acceptability. Full article

(This article belongs to the Special Issue Meat Proteins: Processing Functionality, Structure-Function Relationships and Interactions)

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14 pages, 2545 KiB

Open AccessArticle

Relationship between Molecular Structure and Heat-Induced Gel Properties of Duck Myofibrillar Proteins Affected by the Addition of Pea Protein Isolate

by Xueshen Zhu, Jiaxin Zhang, Shaohua Liu, Ying Gu, Xiaobo Yu, Feng Gao and Renlei Wang

Foods 2022, 11(7), 1040; https://doi.org/10.3390/foods11071040 - 3 Apr 2022

Cited by 18 | Viewed by 2788

Abstract

This paper investigates the relationship between the molecular structure and thermally induced gel properties of duck myofibrillar protein isolate (DMPI) as influenced by the addition of pea protein isolate (PPI). The results showed that b* value of the gels increased; however, a* value decreased with the increase of PPI content (p < 0.05). The whiteness of the gels decreased significantly with the addition of pea protein compared with 0% vs. 0.5% addition. Nuclear magnetic resonance tests showed the area of immobilized water also increased with increasing PPI addition (0–2%), thus consistent with the increased water-holding capacity (p < 0.05). The penetration force of the gels increased with increasing PPI addition (p < 0.05), while the storage modulus and loss modulus of the gels were also found to increase, accompanied by the transformation of the α-helix structure into β-sheet, resulting in better dynamics of gel formation. These results indicated the gel-forming ability of DMPI, including water retention and textural properties, improves with increasing PPI addition. Principal component analysis verified these interrelationships. Thus, pea protein could improve the properties of duck myofibrillar protein gels to some extent and improve their microstructure, potentially facilitating the transition from a weak to a non-aggregated, rigid structure. Full article

(This article belongs to the Special Issue Meat Proteins: Processing Functionality, Structure-Function Relationships and Interactions)

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12 pages, 1173 KiB

Open AccessArticle

The Solubility and Structures of Porcine Myofibrillar Proteins under Low-Salt Processing Conditions as Affected by the Presence of L-Lysine

by Xiuping Li, Wenhui Wang, Shouyin Wang, Yuqing Shen, Jinfeng Pan, Xiuping Dong and Shengjie Li

Foods 2022, 11(6), 855; https://doi.org/10.3390/foods11060855 - 17 Mar 2022

Cited by 9 | Viewed by 2560

Abstract

This study aimed to investigate the presence of L-lysine (Lys) on the solubility and structures of myofibrillar proteins (MFPs) at different ionic strengths. Porcine MFPs were incubated at 4 °C with various levels of ionic strengths (0.15, 0.3, or 0.6 M NaCl) with or without the presence of 20 or 40 mM Lys. After 24 h of incubation, MFP solubility and turbidity were determined, and the particle size distribution, circular dichroism spectra, and intrinsic tryptophan fluorescence of MFP were analyzed to obtain their secondary and tertiary structure. Results showed that the solubilization effects of Lys on MFPs are dependent on the ionic strength. Particularly, the presence of Lys could improve MFP solubility at 0.3 M, which resembles salt-reducing processing conditions. Concomitantly, the secondary and tertiary structures were observed to change as a result of the varying ionic strengths and the addition of Lys, including myofibril swelling, dissociation of myosin filaments, uncoiling of α-helix, and unfolding of the tertiary structure. The possible mechanisms underlying the solubilization effects of Lys on MFPs at low ionic strengths are discussed from the perspective of protein structural changes. Full article

(This article belongs to the Special Issue Meat Proteins: Processing Functionality, Structure-Function Relationships and Interactions)

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13 pages, 15228 KiB

Open AccessFeature PaperArticle

Nano Filling Effect of Nonmeat Protein Emulsion on the Rheological Property of Myofibrillar Protein Gel

by Ruying Cai, Zongyun Yang, Zhen Li, Peng Wang, Minyi Han and Xinglian Xu

Foods 2022, 11(5), 629; https://doi.org/10.3390/foods11050629 - 22 Feb 2022

Cited by 12 | Viewed by 2865

Abstract

Incorporation of vegetable oils through pre-emulsification has received notable attention for delivering polyunsaturated fatty acids to emulsified-type meat products. The two important influencing factors of the rheological property of composite myofibrillar protein (MP) gel are emulsion droplet size and active or inactive interaction between interface and meat proteins. Incorporation of nonmeat protein emulsion (2% protein (w/w), egg-white protein isolate (EPI), porcine plasma protein (PPP), or sodium caseinate (SC)) with different droplet sizes (nano or macro) to a model of 2% MP gel was investigated in this research. The results of drop size measurement showed that 15,000 psi homogenizing could decrease the diameter of emulsion drop from macro- to nanoscale in the range of 324.4–734.5 nm. Active fillers (PPP and EPI emulsions) with nanodroplet size did not influence the viscosity of emulsion-filled composite cold sols but caused positive filling effects on the MP gel matrix after heating, as evidenced by the density microstructure. PPP and EPI nano-emulsion-filled composite MP had a significant high storage modulus enforcement effect, which reached nearly eight times those of other treatments (p < 0.05). Similarly, the results of thermal scanning rheology and a large-deformation mechanical test showed that PPP and EPI emulsions with nanoscale droplets, other than macroscale, had the highest gel strength of heat-induced emulsion-filled composite MP gel (p < 0.05). Overall, these findings will be helpful for selecting the correct pre-emulsified protein and designing the textural properties of foods. Full article

(This article belongs to the Special Issue Meat Proteins: Processing Functionality, Structure-Function Relationships and Interactions)

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