Functional Characteristics of Milk Protein Concentrates and Their Modification

Abstract

A major deterrent to the usage of milk protein concentrate (MPC), a high-protein milk product with increasing demand as a food and sports drink ingredient, has been its poor functional characteristics when compared with other milk protein products such as whey protein concentrate and sodium caseinates. This review discusses the recent research on functional properties of MPC, focusing on factors that may contribute to the poor functional characteristics before, during, and after production. Current research, methods employed, and new understanding on the causes of poor solubility of MPC at mild temperatures (about 20°C) has been presented, including loss of solubility during storage as these areas have received unprecedented attention over the past decade, and also affects other useful functional properties of MPC, such as emulsifying properties, gelation, and foaming. Processing methods, which include heat treatment, high-pressure application, microwave heating, ultrasound application, and enzyme and salts modification, have been used or have potential to modify or improve the functional properties of MPCs. Future research on the effects of these processing methods on the functional properties, including effects of enzyme hydrolysis on bitterness and bioactivity, has also been discussed.

Application of front-face fluorescence spectroscopy as a tool for monitoring changes in milk protein concentrate powders during storage

“…Storing the MPC powders at 40°C resulted in crosslinking networks at the surface of the MPC powders (Anema et al, 2006). These crosslinking networks include interactions between hydrophobic caseins and whey proteins, which hinders the hydration in the MPC powders (Anema et al, 2006;Uluko et al, 2016). As expected, the solubility of MPC has decreased with the increase in the protein content from 70 to 90% and this reduced solubility can be attributed to the reduction in lactose concentration.…”

“…Storing the MPC powders at elevated temperatures such as 40°C resulted in crosslinking networks at the surface of the MPC powders and could be attributed to its poor dissolution characteristics (Anema et al, 2006). The crosslinking networks include interactions between hydrophobic caseins and whey proteins, and thereby hinder the hydration in the MPC powders (Anema et al, 2006;Uluko et al, 2016). As the protein content increased in MPC powders from 70 to 90% (wt/wt), the MPC90 showed more primary particle aggregates and exhibited more resistance to dispersing in water (Crowley et al, 2015).…”

Functional properties and structural characteristics of phosphorylated pea protein isolate

“…At present, various modification methods including chemical, physical and enzymatic modification have been widely studied to enhance the functional properties of protein (Uluko et al , ). Physical modification has a high demand of machinery and equipment, which makes it difficult to carry out in large‐scale industrial production (Day et al , ).…”

Time effect on structural and functional properties of whey protein isolate‐gum acacia conjugates prepared via Maillard reaction

“…Structural changes may cause enhanced functional properties. Many attempts have thus been made to enhance the functionality of proteins, including high‐pressure treatment, ultrasound treatment, heating, glycation, oxidation, hydrolysis, and enzymatic cross‐linking . Of these methods, conjugation of protein with reducing sugar via the Maillard reaction has received great attention recently.…”

“…Many attempts have thus been made to enhance the functionality of proteins, including high-pressure treatment, ultrasound treatment, heating, glycation, oxidation, hydrolysis, and enzymatic cross-linking. 6 Of these methods, conjugation of protein with reducing sugar via the Maillard reaction has received great attention recently. Extensive scientific research has demonstrated that glycation was efficient in enhancing the emulsifying properties, solubility, and thermal stability of proteins.…”