New Strategies to Improve the Functionality of Meat and Meat Products

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Meat".

Deadline for manuscript submissions: closed (30 April 2020) | Viewed by 12636

Special Issue Editor

Department of Animal Science, Chonnam National University, Gwangju 500757, South Korea
Interests: meat products; meat science; meat science and technology; food processing; meat; meat quality

Special Issue Information

Dear Colleagues,

Meat and meat products have been highly associated with human health since they contain many necessary components which are useful in maintaining a good health. To improve the functionality of meat and meat products, there are many new emerging ingredients and processing techniques.

Functionality is defined as the ability to promote health with bioactive compounds which might improve the antioxidant and antimicrobial activity, antihypertension, etc. As a result, the occurrence of chronic diseases, such as cardiovascular disease, high blood pressure, and certain types of cancer, might be delayed or avoided altogether.

Reducing the nonmeat ingredients and adding functional ingredients for functional meat products to create a ‘clean label’is of great interest for consumers. Furthermore, meat and meat products using new ingredients or technology could improve the product functionality of meat and meat products, making them healthier.

This Special Issue will discuss the product functionality of meat and meat products using new ingredients and technologies as compared to the previous ones and suggest how these affect the functional properties in meat and meat products.

Prof. Dr. Koo Bok Chin
Guest Editor

Manuscript Submission Information

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Keywords

  • Meat
  • Meat products
  • Functional meat products
  • New emerging ingredients and processing techniques
  • Meat nutrients
  • Bioactive compounds
  • Antioxidant
  • Antihypertension
  • Antimicrobial activity
  • Function foods
  • Meat science
  • Meat science and technology
  • Meat
  • Meat quality

Published Papers (4 papers)

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Research

14 pages, 2956 KiB  
Article
Effect of Interaction between Mealworm Protein and Myofibrillar Protein on the Rheological Properties and Thermal Stability of the Prepared Emulsion Systems
by Tae-Kyung Kim, Min Hyeock Lee, Hae In Yong, Samooel Jung, Hyun-Dong Paik, Hae Won Jang and Yun-Sang Choi
Foods 2020, 9(10), 1443; https://doi.org/10.3390/foods9101443 - 12 Oct 2020
Cited by 23 | Viewed by 3211
Abstract
In this study, we investigated the effect of replacing myofibrillar protein (pork ham) with edible insect proteins (Tenebrio molitor L.) in meat emulsion systems and examined the interaction between the two types of proteins. We also evaluated the rheological properties and thermal [...] Read more.
In this study, we investigated the effect of replacing myofibrillar protein (pork ham) with edible insect proteins (Tenebrio molitor L.) in meat emulsion systems and examined the interaction between the two types of proteins. We also evaluated the rheological properties and thermal stability of these meat emulsions. The replacement ratios of myofibrillar protein and edible insect protein were as follows: 100:0 (EI0), 80:20 (EI20), 60:40 (EI40), 40:60 (EI60), 20:80 (EI80), and 0:100 (EI100). The pH, redness, and yellowness of the emulsion systems, after replacing myofibrillar protein with T. molitor protein, significantly increased with T. molitor protein concentrations. In contrast, the lightness, hardness, cohesiveness, gumminess, chewiness, apparent viscosity, and differential scanning calorimetry (DSC) of the emulsion systems decreased significantly with increasing T. molitor protein concentrations. The backscattering values of EI0, EI20, and EI40 decreased evenly in all spots of the dispersions as the storage time increased. Thus, up to 40% of pork myofibrillar protein could be replaced with T. molitor protein in meat emulsion systems. The results also suggest that the interaction between edible insect protein and myofibrillar protein degrades the rheological properties and thermal stability of the meat emulsion systems. Full article
(This article belongs to the Special Issue New Strategies to Improve the Functionality of Meat and Meat Products)
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13 pages, 1634 KiB  
Article
Evaluation of NaCl and KCl Salting Effects on Technological Properties of Pre- and Post-Rigor Chicken Breasts at Various Ionic Strengths
by Dong-Heon Song, Youn-Kyung Ham, Sin-Woo Noh, Koo Bok Chin and Hyun-Wook Kim
Foods 2020, 9(6), 721; https://doi.org/10.3390/foods9060721 - 02 Jun 2020
Cited by 5 | Viewed by 2554
Abstract
The objective of this study is to evaluate the effects of NaCl and KCl salting on technological properties of pre- and post-rigor chicken breasts at various ionic strengths. The following factorial arrangement was used: 2 salt types (NaCl and KCl) × 2 rigor [...] Read more.
The objective of this study is to evaluate the effects of NaCl and KCl salting on technological properties of pre- and post-rigor chicken breasts at various ionic strengths. The following factorial arrangement was used: 2 salt types (NaCl and KCl) × 2 rigor statuses (pre- and post-rigor) × 4 ionic strengths (0.086, 0.171, 0.257, and 0.342). Hot-boned and ground chicken breasts were salted within 30 min postmortem after slaughter (pre-rigor salting) or 24 h postmortem (post-rigor salting) with varying concentrations of NaCl (0.50%, 1.00%, 1.50%, and 2.00%) or KCl (0.64%, 1.28%, 1.91%, and 2.55%) corresponding to the four ionic strengths. KCl caused higher pH value in salted chicken breasts than NaCl (p < 0.05). However, KCl decreased total and myofibrillar protein solubilities in post-rigor salted chicken breasts compared to NaCl (p < 0.05), but those were similar to pre-rigor chicken breasts, regardless of the salt type (p > 0.05). Different salt types had no significant impact on cooking loss and textural properties. This study shows that NaCl and KCl had similar effects on technological properties at the same ionic strength (within 0.342), but the use of KCl may have the possibility to decrease protein solubility, depending on rigor status of raw meat at the different salting time. Full article
(This article belongs to the Special Issue New Strategies to Improve the Functionality of Meat and Meat Products)
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11 pages, 2246 KiB  
Article
Physical Properties and Structural Changes of Myofibrillar Protein Gels Prepared with Basil Seed Gum at Different Salt Levels and Application to Sausages
by Chang Hoon Lee and Koo Bok Chin
Foods 2020, 9(6), 702; https://doi.org/10.3390/foods9060702 - 01 Jun 2020
Cited by 14 | Viewed by 2600
Abstract
The objective of this study was to evaluate physical properties and structural changes of myofibrillar protein gels with basil seed gum (BSG) at different salt levels and develop the low-salt sausages with BSG. Myofibrillar protein (MP) gels were prepared with or without BSG [...] Read more.
The objective of this study was to evaluate physical properties and structural changes of myofibrillar protein gels with basil seed gum (BSG) at different salt levels and develop the low-salt sausages with BSG. Myofibrillar protein (MP) gels were prepared with or without BSG at different salt concentrations (0.15, 0.30, and 0.45 M). Cooking yield (CY, %), gel strength (GS, gf), viscosity, sulfhydryl contents, protein surface hydrophobicity, scanning electron microscopy (SEM), and Fourier transform infrared spectroscopy (FTIR) of MP were measured. Pork sausages were manufactured with 1% BSG at both low-salt (1.0%) and regular-salt (1.5%) levels. pH, color, expressible moisture (EM, %), CY, textural profile analyses, FTIR, sulfhydryl group, and protein surface hydrophobicity (μg) were measured for analyzing the properties of sausages. The addition of 1% BSG to MP gels increased CY and shear stress. Among treatments with different salt concentrations, MP at 0.30 M salt level with 1% BSG had higher GS than that at 0.15 M salt level with BSG. In microstructure, swollen structures were shown in MP gels with BSG. Although CY of sausage at the low-salt concentration (1.0%) decreased, regardless of the BSG addition, hardness values of sausages with regular-salt level increased with the addition of 1% BSG was added. Protein surface hydrophobicity and sulfhydryl contents of sausages increased with the addition of 1% BSG, resulting in higher hardness and lower springiness than those without BSG. These results suggest that BSG could be used as a water-binding and gelling agent in processed meats. Full article
(This article belongs to the Special Issue New Strategies to Improve the Functionality of Meat and Meat Products)
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11 pages, 1275 KiB  
Article
Functional Properties of Extracted Protein from Edible Insect Larvae and Their Interaction with Transglutaminase
by Tae-Kyung Kim, Hae In Yong, Hae Won Jang, Young-Boong Kim and Yun-Sang Choi
Foods 2020, 9(5), 591; https://doi.org/10.3390/foods9050591 - 06 May 2020
Cited by 20 | Viewed by 3948
Abstract
Global concern about food supply shortage has increased interest on novel food sources. Among them, edible insects have been studied as a potential major food source. This study aimed to improve the functional properties of protein solutions extracted from Protaetia brevitarsis (PB) by [...] Read more.
Global concern about food supply shortage has increased interest on novel food sources. Among them, edible insects have been studied as a potential major food source. This study aimed to improve the functional properties of protein solutions extracted from Protaetia brevitarsis (PB) by use of transglutaminase (TG) as a cross-linking agent. After various incubation times (10, 20, 30, 60, and 90 min) with TG, the protein solutions were assessed with regard to their amino acid composition, protein nutritional quality, pH, color (yellowness), molecular weight distribution, thermal stability, foam ability (capacity and stability), and emulsion ability (capacity and stability). Incubation with TG changed the amino acid composition of the proteins and shifted the molecular weight distribution towards higher values, while improving the rest of the aforementioned properties. Since the incubation time for 90 min decreased the protein functionality, the optimum incubation time for cross-linking PB-derived protein with TG is 60 min. The application of TG to edible insect proteins ultimately increases its functionality and allows for the development of novel insect processing technology. Full article
(This article belongs to the Special Issue New Strategies to Improve the Functionality of Meat and Meat Products)
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