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Modifications and Interactions of Milk Proteins in Different Processes and...
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Modifications and Interactions of Milk Proteins in Different Processes and Products

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

Deadline for manuscript submissions: 15 October 2024 | Viewed by 9261

Special Issue Editors

Dr. Maneesha S. Mohan

E-Mail Website
Guest Editor
Department of Dairy and Food Science, South Dakota State University, Brookings, SD 57007, USA
Interests: product structure and rheology; high pressure processing; nanobubble technology; supercritical fluid processing; functional products and ingredients; dairy processing and value addition; delivery systems and release kinetics
Dr. Bongkosh Vardhanabhuti

E-Mail Website
Guest Editor
Food Science Program, College of Agriculture, Food and Natural Resources, University of Missouri, Columbia, MO 65211, USA
Interests: physical chemistry of dairy foods; dairy ingredients; milk protein; functional properties; delivery; digestion properties; milk protein-polysaccharide interactions

Special Issue Information

Dear Colleagues,

The dairy industry has been capitalizing on diversified milk protein ingredients in the past couple of decades, enabling them to create economy and profit even from byproducts. Milk proteins are a main component in many dairy products and are used as an ingredient in other foods, supplements, and pharmaceutical products. Apart from their high nutritional quality, milk proteins also have functional properties including foaming, emulsification, binding, gelling, and delivery properties. Several processes involving thermal treatment, non-thermal technologies, mechanical forces, chemical reactions, enzymatic reactions, fermentation, and separation technology may affect the protein quality and physicochemical and rheological properties. The modifications and interactions of milk proteins with other ingredients and components in products and different processes lead to changes in the structural, nutritional, chemical, biological, and technological properties of milk proteins, which affect their end applications and utilization. Some of the intermolecular and intramolecular interactions that can affect these properties of milk proteins include adsorption, conjugation, complexation, and encapsulation. There are several applications of milk proteins in products and processes that on the one hand utilize modifications in milk proteins and on the other find the modification-induced changes unacceptable. Hence, it is important to identify, characterize, and quantify, at micro- and macromolecular levels, the effect of modifications of milk proteins induced by different forces, interactions, and reactions, in their resultant products and applications.

Overall, the main goal of this Special Issue is to present the latest research on:

  • Understanding milk protein modification and interactions that occur during different processes and in the presence of different ingredients and components;
  • Approaches and achievements in modification and interactions of milk proteins to other biomolecules;
  • Changes in the nutritional quality, physicochemical properties, digestion and bioavailability, techno-functionality, delivery properties, texture and rheology, as well as sensory properties of milk proteins;
  • Processes and products that affect the different beneficial properties of milk proteins.

Dr. Maneesha S. Mohan
Dr. Bongkosh Vardhanabhuti
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Foods is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • dairy
  • milk proteins
  • processing
  • techno-functionality
  • bioavailability
  • rheology
  • sensory
  • ingredient interaction (or biopolymer interaction)
  • digestion properties

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Published Papers (7 papers)

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Research

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20 pages, 3330 KiB  
Article
The Impact of Varying Lactose-to-Maltodextrin Ratios on the Physicochemical and Structural Characteristics of Pasteurized and Concentrated Skim and Whole Milk–Tea Blends
by Dilema Wijegunawardhana, Isuru Wijesekara, Rumesh Liyanage, Tuyen Truong, Mayumi Silva and Jayani Chandrapala
Foods 2024, 13(18), 3016; https://doi.org/10.3390/foods13183016 (registering DOI) - 23 Sep 2024
Abstract
This study investigates the impact of substituting lactose with maltodextrin in milk–tea formulations to enhance their physicochemical and structural properties. Various lactose-to-maltodextrin ratios (100:0, 90:10, 85:15, 80:20, 75:25) were evaluated in both post-pasteurized and concentrated skim milk–tea (SM-T) and whole milk–tea (WM-T) formulations. [...] Read more.
This study investigates the impact of substituting lactose with maltodextrin in milk–tea formulations to enhance their physicochemical and structural properties. Various lactose-to-maltodextrin ratios (100:0, 90:10, 85:15, 80:20, 75:25) were evaluated in both post-pasteurized and concentrated skim milk–tea (SM-T) and whole milk–tea (WM-T) formulations. Concentration significantly improved the zeta potential, pH, and browning index in both SM-T and WM-T compared to pasteurization. L:M ratios of 90:10 and 75:25 in WM-T and 90:10 and 80:20 in SM-T showed higher phenolic preservation after concentration due to structural changes resulting from the addition of maltodextrin and water removal during prolonged heating. The preservation effect of phenolic components in both WM-T and SM-T is governed by many mechanisms including pH stabilization, zeta potential modulation, protein interactions, complex formation, and encapsulation effects. Therefore, optimizing milk–tea stability and phenolic preservation through L:M ratio adjustments provides a promising approach for enhancing milk–tea properties. Full article
(This article belongs to the Special Issue Modifications and Interactions of Milk Proteins in Different Processes and Products)
16 pages, 824 KiB  
Article
Transglutaminase Crosslinked Milk Protein Concentrate and Micellar Casein Concentrate: Impact on the Functionality of Imitation Mozzarella Cheese Manufactured on a Small Scale Using a Rapid Visco Analyzer
by Prafulla Salunke and Lloyd E. Metzger
Foods 2024, 13(17), 2720; https://doi.org/10.3390/foods13172720 - 27 Aug 2024
Viewed by 393
Abstract
In dairy-based imitation mozzarella cheese (IMC) formulations, intact casein is critical and imparts IMC with a firm and elastic, stringy, melted texture. Rennet casein (RCN) is the desired ingredient to provide intact casein in IMC and is preferred over milk protein concentrate (MPC) [...] Read more.
In dairy-based imitation mozzarella cheese (IMC) formulations, intact casein is critical and imparts IMC with a firm and elastic, stringy, melted texture. Rennet casein (RCN) is the desired ingredient to provide intact casein in IMC and is preferred over milk protein concentrate (MPC) and micellar casein concentrate (MCC). Transglutaminase (TGase), a crosslinking enzyme, alters the physical properties of MPC or MCC and may change IMC functionality. The objective of this study was to determine the effect of TGase-crosslinked MPC and MCC powders on the functionality of IMCs. The TGase treatment included TGase at 0.3 (L) and 3.0 (H) units/g of protein and a control (C) with no TGase addition. Each IMC formulation was balanced for constituents and was produced in a Rapid Visco Analyzer (RVA). The MCC or MPC powder with high TGase enzyme in IMC formulation did not form an emulsion. The IMC containing TGase-treated powders had a significantly (p ≤ 0.05) higher RVA-viscosity during manufacture and transition temperature (TT), and a significantly (p ≤ 0.05) lower Schreiber melt test area. The IMC made from MPC (with or without TGase) had lower TT values and Schreiber melt test area as compared with that made from MCC. The TGase-treated MPC and MCC, when used for IMC manufacture, were comparable to IMC manufactured with RCN in texture and some measured melted characteristics. In conclusion, TGase treatment alters the melt characteristics of MCC and MPC in IMC applications. Full article
(This article belongs to the Special Issue Modifications and Interactions of Milk Proteins in Different Processes and Products)
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15 pages, 2408 KiB  
Article
The Influence of pH on the Emulsification Properties of Heated Whey Protein–Pectin Complexes
by Yeyang Wang and Bongkosh Vardhanabhuti
Foods 2024, 13(14), 2295; https://doi.org/10.3390/foods13142295 - 21 Jul 2024
Viewed by 781
Abstract
Interactions between proteins and polysaccharides could improve protein functional properties. Most studies focus on the formation of complex coacervates at pHs < pI. Much less attention has been given to the interactions at pHs > pI, especially when the mixtures are heated. The [...] Read more.
Interactions between proteins and polysaccharides could improve protein functional properties. Most studies focus on the formation of complex coacervates at pHs < pI. Much less attention has been given to the interactions at pHs > pI, especially when the mixtures are heated. The objective of this study was to investigate the emulsification properties of heated whey protein isolate (WPI) and pectin complexes formed at near neutral pHs. Heated soluble complexes (Cpxs) were formed by heating mixed WPI (3 wt% protein) and pectin (0 to 0.60 wt%) at pH 6.0, 6.5, or 7.0 at 85 °C for 30 min. Emulsions (5 wt% oil, 0.5 wt% protein, and pH 5.5) were characterized by measuring droplet size, zeta potential, rheological properties, and creaming stability. The results showed that, regardless of heating pH, Cpxs formed more stable emulsions with significantly smaller droplet sizes, higher negative charges, and less shear-thinning behavior in comparison to emulsions stabilized by heated WPI (p < 0.05). At fixed pectin concentrations, the emulsions stabilized by Cpx formed at pH 7.0 were the most stable. Increasing pectin concentrations led to a decrease in mean droplet sizes and an increase in negative charge. Maximum stability was achieved with the emulsion stabilized by Cpx formed with 0.60 wt% pectin at pH 7.0. The formation of Cpxs under proper conditions will allow for the utilization of WPI in a wider range of applications and fulfill the consumer need for clean label food products. Full article
(This article belongs to the Special Issue Modifications and Interactions of Milk Proteins in Different Processes and Products)
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13 pages, 247 KiB  
Article
The Influence of Sodium Hexametaphosphate Chain Length on the Physicochemical Properties of High-Milk Protein Dispersions
by Baheeja J. Zaitoun and Jayendra K. Amamcharla
Foods 2024, 13(9), 1383; https://doi.org/10.3390/foods13091383 - 30 Apr 2024
Viewed by 1067
Abstract
Protein–protein and protein–mineral interactions can result in defects, such as sedimentation and age gelation, during the storage of high-protein beverages. It is well known that age gelation can be delayed by adding cyclic polyphosphates such as sodium hexametaphosphate (SHMP). This study aims to [...] Read more.
Protein–protein and protein–mineral interactions can result in defects, such as sedimentation and age gelation, during the storage of high-protein beverages. It is well known that age gelation can be delayed by adding cyclic polyphosphates such as sodium hexametaphosphate (SHMP). This study aims to assess the influence of different phosphate chain lengths of SHMP on the physicochemical properties of high-protein dispersions. The effect of adding different SHMP concentrations at 0%, 0.15%, and 0.25% (w/w) before and after heating of 6%, 8%, and 10% (w/w) milk protein concentrate dispersions was studied. The phosphate chain lengths of SHMPs used in this study were 16.47, 13.31, and 9.88, and they were classified as long-, medium-, and short-chain SHMPs, respectively. Apparent viscosity, particle size, heat coagulation time (HCT), color, and turbidity were evaluated. It was observed that the addition of SHMP (0.15% and 0.25%) increased the apparent viscosity of MPC dispersions. However, the chain length and the concentration of the added SHMP had no significant (p > 0.05) effect on the apparent viscosity after heating the dispersions. The HCT of a dispersion containing 6%, 8%, and 10% protein with no SHMP added was 15.28, 15.61, and 11.35 min, respectively. The addition of SHMP at both levels (0.15% and 0.25%) significantly increased the HCT. Protein dispersions (6%, 8%, and 10%) containing 0.25% short-chain SHMP had the highest HCT at 19.29, 19.61, and 16.09 min, respectively. Therefore, the chain length and concentration of added SHMP significantly affected the HCT of unheated protein dispersion (p < 0.05). Full article
(This article belongs to the Special Issue Modifications and Interactions of Milk Proteins in Different Processes and Products)
19 pages, 2904 KiB  
Article
Preferential Binding of Polyphenols in Blackcurrant Extracts with Milk Proteins and the Effects on the Bioaccessibility and Antioxidant Activity of Polyphenols
by Ting Mao, FNU Akshit, Iresha Matiwalage, Subha Sasidharan, Caren Meyn Alvarez, Philip Wescombe and Maneesha S. Mohan
Foods 2024, 13(4), 515; https://doi.org/10.3390/foods13040515 - 7 Feb 2024
Cited by 3 | Viewed by 1988
Abstract
Milk proteins are well-known delivery agents; however, there is no clear understanding of the competitive interactions of milk proteins with polyphenols in mixed complex systems. Here, we investigate the preferential competitive interactions of different polyphenols present in blackcurrant extract with milk proteins by [...] Read more.
Milk proteins are well-known delivery agents; however, there is no clear understanding of the competitive interactions of milk proteins with polyphenols in mixed complex systems. Here, we investigate the preferential competitive interactions of different polyphenols present in blackcurrant extract with milk proteins by quantifying the protein-bound polyphenols and comparing the factors affecting these interactions. In addition, bioaccessibility and antioxidant activity were studied after in vitro gastric digestion. Our results indicated that polyphenols from blackcurrant extracts were preferentially bound to caseins more than whey proteins, with noncovalent interactions causing secondary structural changes in the protein. The hydrophobicity and the charge of the polyphenols were negatively and positively related to the number of polyphenols bound to casein and whey proteins, respectively. Moreover, the bioaccessibility and antioxidant activity of polyphenols were enhanced in the presence of milk proteins in milk-based blackcurrant samples when compared to polyphenol and protein-alone samples in the in vitro gastric phase. These findings underscore the critical role of milk proteins in encapsulating or delivering polyphenols. This will pave the way for boosting the bioavailability of polyphenols by complexing them with milk proteins and formulating functional dairy foods, integrating the beneficial effects of these compounds. Full article
(This article belongs to the Special Issue Modifications and Interactions of Milk Proteins in Different Processes and Products)
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14 pages, 16992 KiB  
Article
Milk Whey Protein Fibrils—Effect of Stirring and Heating Time
by Gunvantsinh Rathod and Jayendra Amamcharla
Foods 2024, 13(3), 466; https://doi.org/10.3390/foods13030466 - 1 Feb 2024
Viewed by 1165
Abstract
Milk whey proteins, which are derived from skim milk through membrane filtration, exhibit valuable functional properties when transformed into a fibrillar form. This conversion enhances their suitability for various applications, including thickening, gelling, emulsification, and foaming. However, reported fibrillation methods have longer heating [...] Read more.
Milk whey proteins, which are derived from skim milk through membrane filtration, exhibit valuable functional properties when transformed into a fibrillar form. This conversion enhances their suitability for various applications, including thickening, gelling, emulsification, and foaming. However, reported fibrillation methods have longer heating times, which may not be economical for the dairy industry. To address these challenges, the current study was undertaken with the objective of reducing the time required for fibril formation. In this study, 2% milk whey protein isolate (mWPI) solution at pH 2 was heated with static and stirring heating conditions at 80 °C for 20 h to convert milk whey proteins into fibrils. Fibrils were observed using the thioflavin T value, transmission electron microscopy, Tricine SDS-PAGE, rheology, and protein oxidation. Results suggest that stirring heating conditions with 14 h heating time produced fibrils with good morphology compared to static heating, showing a 6 h reduction compared to an earlier reported 80 °C for 20 h heating time. Also, stirring heating produced a uniform and homogeneous fibril solution compared to the static heating method. Gentle stirring during heating can also help to scale up fibril production in an industrial setup. The fibrillation method with processing intervention will help to produce fibrils with enhanced functionality at the pilot and industrial scales. Full article
(This article belongs to the Special Issue Modifications and Interactions of Milk Proteins in Different Processes and Products)
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Review

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32 pages, 1198 KiB  
Review
Strategies for Exploiting Milk Protein Properties in Making Films and Coatings for Food Packaging: A Review
by Stefano Gerna, Paolo D’Incecco, Sara Limbo, Marta Sindaco and Luisa Pellegrino
Foods 2023, 12(6), 1271; https://doi.org/10.3390/foods12061271 - 16 Mar 2023
Cited by 5 | Viewed by 2847
Abstract
Biopolymers of different natures (carbohydrates, proteins, etc.) recovered from by-products of industrial processes are increasingly being studied to obtain biomaterials as alternatives to conventional plastics, thus contributing to the implementation of a circular economy. The food industry generates huge amounts of by-products and [...] Read more.
Biopolymers of different natures (carbohydrates, proteins, etc.) recovered from by-products of industrial processes are increasingly being studied to obtain biomaterials as alternatives to conventional plastics, thus contributing to the implementation of a circular economy. The food industry generates huge amounts of by-products and waste, including unsold food products that reach the end of their shelf life and are no longer usable in the food chain. Milk proteins can be easily separated from dairy waste and adapted into effective bio-based polymeric materials. Firstly, this review describes the relevant properties of milk proteins and the approaches to modifying them for subsequent use. Then, we provide an overview of recent studies on the development of films and coatings based on milk proteins and, where available, their applications in food packaging. Comparisons among published studies were made based on the formulation as well as production conditions and technologies. The role of different additives and modifiers tested for the performances of films and coatings, such as water vapor permeability, tensile strength, and elongation at break, were reviewed. This review also outlines the limitations of milk-protein-based materials, such as moisture sensitivity and brittleness. Overall, milk proteins hold great potential as a sustainable alternative to petroleum-based polymers. However, their use in food packaging materials at an industrial level remains problematic. Full article
(This article belongs to the Special Issue Modifications and Interactions of Milk Proteins in Different Processes and Products)
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