Abstract
This article continues a series of reviews on the abundance and roles of intrinsic disorder in milk proteins. Besides caseins, which are the major proteinaceous constituents of any milk that can be isolated by isoelectric precipitation, milk contains a set of soluble whey proteins, such as β-lactoglobulin, α-lactalbumin, serum albumin, immunoglobulins, lactoferrin, lactoperoxidase, glycomacropeptide, and proteose peptone (the last two are soluble casein derivatives). Lactoferrin and lactoperoxidase (LPO) are known to possess prominent biocidal activity, serving as efficient antibiotics and antiviral agents against a wide spectrum of bacteria, fungi, and viruses. LPO is a heme-containing peroxidase expressed as preproprotein. The mature protein has a single catalytic domain, structure of which is known for a protein isolated from several species. Functionally, LPO is a crucial component of the LPO system that includes LPO, hydrogen peroxide (H2O2), and thiocyanate (SCN−), being a well-studied, naturally occurring antimicrobial system in milk that is effective against many microorganisms and some viruses. Although various aspects of LPO structure and function are rather well studied and were subjects of several recent reviews, the abundance and potential functional roles of intrinsically disordered regions in this protein have never being addressed as of yet. The major goal of this article is to fill this gap and to show how intrinsic disorder is encoded in the amino acid sequence of LPO, and how intrinsic disorder is related to functions of this important milk protein.
Keywords: Glycosylation, intrinsically disordered protein, lactoperoxidase, milk proteins, phosphorylation, protein-protein interaction, whey.
Current Protein & Peptide Science
Title:Disorder in Milk Proteins: Structure, Functional Disorder, and Biocidal Potentials of Lactoperoxidase
Volume: 16 Issue: 4
Author(s): Hussein A. Almehdar, Esmail M. El-Fakharany, Vladimir N. Uversky and Elrashdy M. Redwan
Affiliation:
Keywords: Glycosylation, intrinsically disordered protein, lactoperoxidase, milk proteins, phosphorylation, protein-protein interaction, whey.
Abstract: This article continues a series of reviews on the abundance and roles of intrinsic disorder in milk proteins. Besides caseins, which are the major proteinaceous constituents of any milk that can be isolated by isoelectric precipitation, milk contains a set of soluble whey proteins, such as β-lactoglobulin, α-lactalbumin, serum albumin, immunoglobulins, lactoferrin, lactoperoxidase, glycomacropeptide, and proteose peptone (the last two are soluble casein derivatives). Lactoferrin and lactoperoxidase (LPO) are known to possess prominent biocidal activity, serving as efficient antibiotics and antiviral agents against a wide spectrum of bacteria, fungi, and viruses. LPO is a heme-containing peroxidase expressed as preproprotein. The mature protein has a single catalytic domain, structure of which is known for a protein isolated from several species. Functionally, LPO is a crucial component of the LPO system that includes LPO, hydrogen peroxide (H2O2), and thiocyanate (SCN−), being a well-studied, naturally occurring antimicrobial system in milk that is effective against many microorganisms and some viruses. Although various aspects of LPO structure and function are rather well studied and were subjects of several recent reviews, the abundance and potential functional roles of intrinsically disordered regions in this protein have never being addressed as of yet. The major goal of this article is to fill this gap and to show how intrinsic disorder is encoded in the amino acid sequence of LPO, and how intrinsic disorder is related to functions of this important milk protein.
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Cite this article as:
A. Almehdar Hussein, El-Fakharany Esmail M., N. Uversky Vladimir and M. Redwan Elrashdy, Disorder in Milk Proteins: Structure, Functional Disorder, and Biocidal Potentials of Lactoperoxidase, Current Protein & Peptide Science 2015; 16 (4) . https://dx.doi.org/10.2174/1389203716666150316114956
DOI https://dx.doi.org/10.2174/1389203716666150316114956 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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