scholarly journals A Comprehensive Review on the Interaction of Milk Protein Concentrates with Plant-Based Polyphenolics

2021 ◽  
Vol 22 (24) ◽  
pp. 13548
Author(s):  
Mansuri M. Tosif ◽  
Agnieszka Najda ◽  
Aarti Bains ◽  
Thummalacharla Chaitanya Krishna ◽  
Prince Chawla ◽  
...  
Keyword(s):  
Functional Properties ◽  
Milk Protein ◽  
Structural Changes ◽  
Biological Activities ◽  
Structural Characteristics ◽  
Milk Proteins ◽  
Polyphenolic Compounds ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Structural And Functional Properties

Functional properties and biological activities of plant-derived polyphenolic compounds have gained great interest due to their epidemiologically proven health benefits and diverse industrial applications in the food and pharmaceutical industry. Moreover, the food processing conditions and certain chemical reactions such as pigmentation, acylation, hydroxylation, and glycosylation can also cause alteration in the stability, antioxidant activity, and structural characteristics of the polyphenolic compounds. Since the (poly)phenols are highly reactive, to overcome these problems, the formulation of a complex of polyphenolic compounds with natural biopolymers is an effective approach. Besides, to increase the bioavailability and bioaccessibility of polyphenolic compounds, milk proteins such as whey protein concentrate, sodium caseinate, and milk protein concentrate act as natural vehicles, due to their specific structural and functional properties with high nutritional value. Therefore, milk proteins are suitable for the delivery of polyphenols to parts of the gastrointestinal tract. Therefore, this review reports on types of (poly)phenols, methods for the analysis of binding interactions between (poly)phenols–milk proteins, and structural changes that occur during the interaction.

scholarly journals Promising Food Ingredients: Milk Proteins

2021 ◽  
Author(s):  
Roua Lajnaf ◽  
Hamadi Attia ◽  
Mohamed Ali Ayadi
Keyword(s):  
Functional Properties ◽  
Food Industry ◽  
Biological Activities ◽  
Structural Characteristics ◽  
Milk Proteins ◽  
Protein Fractions ◽  
Emulsifying Properties ◽  
Nutritional Properties ◽  
Food Ingredients ◽  
Industrial Relevance

Milk, well known for its nutritional properties, has also good functional properties as foaming, emulsifying and biological activities due to proteins. Milk proteins are then considered as promising food ingredients due to their particular structural characteristics leading to various interesting properties in the industrial field. Thus, the examination of the biological activities and techno-functional properties (foaming and emulsifying properties) of some milk protein fractions revealed interesting ingredients for food industry due to their nutritional value, which is of a great scientific and industrial relevance. This chapter presented an overview of the studied functional properties of some milk proteins.

Determination of Aflatoxin M1 in Liquid Milk, Cheese, and Selected Milk Proteins by Automated Online Immunoaffinity Cleanup with Liquid Chromatography‒Fluorescence Detection

2020 ◽  
Author(s):  
Jackie E Wood ◽  
Brendon D Gill ◽  
Harvey E Indyk ◽  
Ria Rhemrev ◽  
Monika Pazdanska ◽  
...  
Keyword(s):  
Whey Protein ◽  
High Throughput ◽  
Milk Proteins ◽  
Whey Protein Concentrate ◽  
Aflatoxin M1 ◽  
Protein Concentrate ◽  
Compliance Testing ◽  
Liquid Milk ◽  
Hydroxylated Metabolite ◽  
Single Laboratory

Abstract Background Aflatoxins are secondary metabolites produced by a number of species of Aspergillus fungi. Aflatoxin M1 (AFM1) is a hydroxylated metabolite of aflatoxin B1 and is found in the milk of cows fed with feed spoilt by Aspergillus species. AFM1 is carcinogenic, especially in the liver and kidneys, and mutagenic, and is also an immunosuppressant in humans. Objective A high-throughput method for the quantitative analysis of AFM1 that is applicable to liquid milk, cheese, milk protein concentrate (MPC), whey protein concentrate (WPC), whey protein isolate (WPI), and whey powder (WP) was developed and validated. Method AFM1 in cheese, milk, and protein products is extracted using 1% acetic acid in acetonitrile with citrate salts. The AFM1 in the resulting extract is concentrated using RIDA®CREST/IMMUNOPREP® ONLINE cartridges followed by quantification by HPLC‒fluorescence. Results The method was shown to be accurate for WP, WPC, WPI, MPC, liquid milk, and cheese, with acceptable recovery (81–112%) from spiked samples. Acceptable precision for WP, WPC, WPI, MPC, liquid milk, and cheese was confirmed, with repeatabilities of 4–12% RSD and intermediate precisions of 5–13% RSD. Method detection limit and ruggedness experiments further demonstrated the suitability of this method for routine compliance testing. An international proficiency scheme (FAPAS) cheese sample showed that this method gave results that were comparable with those from other methods. Conclusions A method for high-throughput, routine testing of AFM1 is described. The method was subjected to single-laboratory validation and was found to be accurate, precise, and fit-for-purpose. Highlights An automated online immunoaffinity cleanup HPLC‒fluorescence method for milk proteins, cheese, and milk was developed and single-laboratory validated. It allows for high-throughput analysis of AFM1 and can be used for the analysis of AFM1 in whey protein products.

Functional properties of native and cheese whey protein concentrate powders

2007 ◽  
Vol 60 (4) ◽  
pp. 277-285 ◽  
Author(s):  
ANTTI T HEINO ◽  
JANNE O UUSI-RAUVA ◽  
PIRJO R RANTAMÄKI ◽  
OLLI TOSSAVAINEN
Keyword(s):  
Whey Protein ◽  
Functional Properties ◽  
Cheese Whey ◽  
Whey Protein Concentrate ◽  
Protein Concentrate

Study of Whey Protein Concentrate Fortification in Cookies Variety Biscuits

2011 ◽  
Vol 7 (2) ◽  
Author(s):  
Vishal R. Parate ◽  
Dilip K Kawadkar ◽  
Shriram S. Sonawane
Keyword(s):  
Nutritional Status ◽  
Whey Protein ◽  
Sensory Evaluation ◽  
Functional Properties ◽  
Percent Level ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Spread Ratio ◽  
Ratio Spread ◽  
Spread Factor

Whey protein concentrate is one of the most cheaply available rich sources of quality proteins offering many health benefits, and it has the ability to improve the food products due to its various functional properties. In improving the nutritional status of biscuits, the incorporation of whey protein concentrate has proved its ideality. The objective of present study was to explore the possibility of fortifying the whey protein concentrate in the formulation of biscuits. Biscuits were prepared from the blend (wheat flour and whey protein concentrate) containing various wt% levels of whey protein concentrate (0, 20, 25, 30, 35 and 40 percent) using traditional creaming method. Prepared biscuits were then evaluated for chemical, physical and sensory properties. It was observed that the thickness of whey protein concentrate fortified biscuits increased with increasing wt% level of whey protein concentrate, whereas diameter, spread ratio, spread factor and weight decreased with increasing wt% level of incorporation. The sensory evaluation supported incorporation of maximum 25 percent level of whey protein concentrate.

Utilization of milk proteins as starting materials for other foodstuffs

1979 ◽  
Vol 46 (2) ◽  
pp. 369-376 ◽  
Author(s):  
Charles V. Morr
Keyword(s):  
Functional Properties ◽  
Food Processing ◽  
Milk Protein ◽  
Milk Proteins ◽  
Food Processing Industry ◽  
Processing Industry ◽  
Whey Protein Concentrates ◽  
Wide Range ◽  
Utilization Of Protein ◽  
The Subject

SUMMARYThe modern food-processing industry is placing more and more emphasis upon the utilization of protein ingredients to provide specific functional properties to a wide range of formulated foods. Isolated milk protein products represent an important and valuable source of protein ingredients due to their recognized superior nutritional, organoleptic and functional properties. This paper provides up-to-date information on the quantities, production processes, composition, general properties, and specific functional properties of the major milk protein products, e.g. caseinates, co-precipitates, lactalbumin, whey protein concentrates and milk blends. The subject of chemical and enzymic modification to improve certain functional properties of milk proteins is considered briefly.

Comparison of heat and pressure treatments of skim milk, fortified with whey protein concentrate, for set yogurt preparation: effects on milk proteins and gel structure

2000 ◽  
Vol 67 (3) ◽  
pp. 329-348 ◽  
Author(s):  
ERIC C. NEEDS ◽  
MARTA CAPELLAS ◽  
A. PATRICIA BLAND ◽  
PRETIMA MANOJ ◽  
DOUGLAS MACDOUGAL ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Whey Protein ◽  
Skim Milk ◽  
Milk Proteins ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Casein Micelles ◽  
Micelle Structure ◽  
Dynamic Structures ◽  
Β Lactoglobulin

Heat (85 °C for 20 min) and pressure (600 MPa for 15 min) treatments were applied to skim milk fortified by addition of whey protein concentrate. Both treatments caused > 90% denaturation of β-lactoglobulin. During heat treatment this denaturation took place in the presence of intact casein micelles; during pressure treatment it occurred while the micelles were in a highly dissociated state. As a result micelle structure and the distribution of β-lactoglobulin were different in the two milks. Electron microscopy and immunolabelling techniques were used to examine the milks after processing and during their transition to yogurt gels. The disruption of micelles by high pressure caused a significant change in the appearance of the milk which was quantified by measurement of the colour values L*, a* and b*. Heat treatment also affected these characteristics. Casein micelles are dynamic structures, influenced by changes to their environment. This was clearly demonstrated by the transition from the clusters of small irregularly shaped micelle fragments present in cold pressure-treated milk to round, separate and compact micelles formed on warming the milk to 43 °C. The effect of this transition was observed as significant changes in the colour indicators. During yogurt gel formation, further changes in micelle structure, occurring in both pressure and heat-treated samples, resulted in a convergence of colour values. However, the microstructure of the gels and their rheological properties were very different. Pressure-treated milk yogurt had a much higher storage modulus but yielded more readily to large deformation than the heated milk yogurt. These changes in micelle structure during processing and yogurt preparation are discussed in terms of a recently published micelle model.

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