Milk protein structure—what can it tell the dairy industry (original) (raw)
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Erratum to:“Milk protein structure—what can it tell the dairy industry
2002
This paper describes the possible usefulness of knowledge of the three-dimensional structure of milk proteins to dairy scientists. After a brief introduction of the available methodology and the structures of milk proteins that are already available, the structure of bovine b-lactoglobulin is used to illustrate the possible applications of the structure to understanding the problems to which the protein contributes during milk processing. r
‘New views’ on structure–function relationships in milk proteins
Trends in Food Science & Technology, 2001
The molten globule state has been regarded as a major intermediate in protein folding. It is characterized by nativelike secondary structure with a compact molecular size but little specific tertiary structure. -lactalbumin under various denaturing conditions has been considered a paradigm of the classical molten globule state. It has been shown that caseins share many of the same properties and may therefore exist naturally in a molten globule-like state with defined secondary structure and limited fluctuating tertiary structure, which lead to their propensity for polymerization. The architectural concepts of tensegrity may be used to describe, in part, the structure of casein polymers. #
Milk Proteins - From Structure to Biological Properties and Health Aspects
InTech eBooks, 2016
Mammalian milk is a complex fluid mixture of various proteins, minerals, and lipids, which play an important role in providing nutrition and immunity to the newborn. Casein proteins, which form about 80% of the bovine milk proteins, form large colloidal particles with calcium phosphate to form casein micelles, which for many years have been an important subject of interest. Casein micelles are composed of four main types of proteins: α S1-casein, α S2-casein, β-casein, and k-casein. These constituent casein proteins lack well-defined secondary and tertiary structure due to large amount of propyl residues. These micelles are being extensively studied because of their importance in functional behavior of milk and various milk products. However, the exact structure and nature of these casein micelles are still under debate. These different casein proteins possess different functional properties due to their primary amino acid sequence.
beta-Lactoglobulin - a three-dimensional perspective
International Journal of Food Science and Technology, 1999
Bovine -lactoglobulin has been the subject of intense study over the past 60 years by, effectively, every available physicochemical technique, of which one of the most powerful is X-ray crystallography. We present a short review of the X-ray crystallographic work on milk protein together with an overview of the properties as they are seen from the current state of crystallographic analyses. At the present time, structural analyses do not provide any further insights into the possible function of the protein.
Nomenclature of the proteins of cows' milk--sixth revision
Journal of dairy science, 2004
This report of the American Dairy Science Association Committee on the Nomenclature, Classification, and Methodology of Milk Proteins reviews changes in the nomenclature of milk proteins necessitated by recent advances of our knowledge of milk proteins. Identification of major caseins and whey proteins continues to be based upon their primary structures. Nomenclature of the immunoglobulins consistent with new international standards has been developed, and all bovine immunoglobulins have been characterized at the molecular level. Other significant findings related to nomenclature and protein methodology are elucidation of several new genetic variants of the major milk proteins, establishment by sequencing techniques and sequence alignment of the bovine caseins and whey proteins as the reference point for the nomenclature of all homologous milk proteins, completion of crystallographic studies for major whey proteins, and advances in the study of lactoferrin, allowing it to be added t...
2020
Processing milk into dairy products leaves a large portion of milk protein, which can be used in many ways. Milk protein is<br> composed of casein and whey protein. Casein is predominate bovine milk protein, which forms large colloidal particles and present in the<br> form of casein micelles. Whey is liquid by products in chess manufacturing or liquid obtained from remove fat and casein from milk.<br> Generally, protein, especially milk protein, has multiple functions in food, such as emulsification, foam formation and stability.<br> Condensed milk protein is a high quality protein that is found naturally in the milk. These milk powders provide powerful and nutritious<br> multifunctional nutrients for the global food and beverage industry due to their high protein content. Milk Protein also consider high<br> quality protein and provide various nutritional benefits, which should be included into the diets. The objective of this review is to<br&g...
Covalent Structure of the Minor Monomeric β-Lactoglobulin II Component from Donkey Milk
Biological Chemistry Hoppe-Seyler, 1990
The complete primary structure of the minor /3-lactoglobulin II component from donkey milk is presented. It has been established by aminoacid sequencing and mass-spectrometry analysis of intact protein and peptides obtained after enzymatic and chemical cleavages. The molecular mass and the pi of the protein are calculated to be 18 261 Da and 4.5 respectively. Despite the close structural similarity of the donkey and horse major/3-lactoglobulin I components , their minor /3-lactoglobulin II components show substantial differences in sequence. Most observed exchanges are clustered at residues 78-106 where only 6 amino-acid residues are conserved.The primary structure of donkey /3-lactoglobulin II reveals some unusual features of minor /3-lactoglobulins II and gives new light to the evolution of /3-lactoglobulins and other lipocalins involved in retinol binding or reproductive functions. Primarstruktur der monomer en ß-Lactoglobulin-II-Nebenkomponente aus Eselsmilch Zusammenfassung: Die vollständige Primärstruktur der /3-Lactoglobulin-II-Nebenkomponente aus Eselsmilch wird präsentiert. Sie wurde mit Hilfe von Aminosäuresequenzierung und Massenspektrometrie des intakten Proteins sowie enzymatischer und chemischer Spaltpeptide gefunden. Die molekulare Masse beträgt 18261 Da und der p/-Wert 4.5. Im Gegensatz zur großen Ähnlichkeit zwischen den Hauptkomponenten (/3-Lactoglobulin I) von Esel und Pferd zeigen ihre Nebenkomponenten (/3-Lactoglobulin II) sub-stantielle Unterschiede. Die meisten der Aminosäure-Austausche treten gehäuft im Bereich von Position 78-106 auf. Diese Bereiche stimmen nur in 6 Aminosäureresten überein. Die Primärstruktur des /3-Lactoglobulins II vom Esel zeigt einige ungewöhnliche Eigenschaften dieser Lactoglobulin-Nebenkomponenten und wirft neues Licht auf die Frage der Evolution von /3-Lactoglobulinen und anderen Lipocalinen, die an der Retinolbindung beteiligt sind oder Funktionen bei der Reproduktion haben.
Journal of dairy science, 2002
Recent advances in the field of protein chemistry have significantly enhanced our understanding of the possible intermediates that may occur during protein folding and unfolding. In particular, studies on alpha-lactalbumin have led to the theory that the molten globule state may be a possible intermediate in the folding of many proteins. The molten globule state is characterized by a somewhat compact structure, a higher degree of hydration and side chain flexibility, a significant amount of native secondary structure but little tertiary folds, and the ability to react with chaperones. Purified alpha(s1)- and kappa-caseins share many of these same properties; these caseins may thus occur naturally in a molten globule-like state with defined, persistent structures. The caseins appear to have defined secondary structures and to proceed to quaternary structures without tertiary folds. This process may be explained, in part, by comparison with the architectural concepts of tensegrity. By...
Ovine β-lactoglobulin at atomic resolution
Acta crystallographica. Section F, Structural biology communications, 2014
The crystal structure of the triclinic form of the milk protein β-lactoglobulin from sheep (Ovis aries) at 1.1 Å resolution is described together with a comparison of the triclinic structures of the low-pH bovine and high-pH ovine proteins. All three structures are remarkably similar, despite the well known pH-dependent conformational transition described for the bovine and porcine proteins that occurs in solution. The high resolution of the present structure determination has allowed a more accurate description of the protein than has hitherto been possible, but it is still not clear whether flexibility changes in the external loops can compensate for the presence of a significant void in the unliganded interior of the structure.