Antioxidant Activity of Food Proteins and Food Protein Hydrolysates
Food proteins (2)
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Food proteins Chapter: 1. General (physicochemical) properties of proteins and Main sources of food proteins By Tahseen Fatima Miano
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Transcript of Food proteins (2)
Food proteins
Chapter: 1. General (physicochemical) properties of proteins and Main sources of food proteins
ByTahseen Fatima Miano
Outline
1. Physico Chemical Properties Of Proteins
a) Chemical composition of amino acidb) Classification of amino acid based on phc) Ionization behavior of amino acidd) Peptides, oligopeptides, polypeptides, proteinse) Protein structuref) Electrostatic interactions van der waals interactions
2.Sources of Protein
g) Major types of soybean protein productsh) Defatted cottonseed floursi) Mycoprotein productsj) Leaf-protein concentratek) Microbial-biomass proteinl) Conclusion
PHYSICO CHEMICAL PROPERTIES OF PROTEINS:
Amino acids
Basic structural unit
Building block of proteins.
20 amino acids
Coded genetically
Make food proteins.
CHEMICAL COMPOSITION OF AMINO ACIDConsists of a hydrogen (H), Amine (NH2)group, Carboxyl (COOH) group, Side group (R) which are covalently linked to a central α-carbon.
The structures of amino acids differ only in the different structure of their side group (R).
Proline Side chain are covalently linked to the central α-carbon and to the nitrogen of the amine group forming a cyclic structure.
Group (R) determines, Size,Net charge, Solubility, Chemical reactivity Hydrogen bonding ability
The Joint Commission of Biochemical Nomenclature (JCBN)
International Union of Pure and Applied chemistry (IUPAC)-International Union of Biochemistry (IUB)
established standardsymbols and nomenclature for amino acids and peptides.
Glycine, single hydrogen as its R group. Based on their side group R,
CLASSIFICATION OF AMINO ACID BASED ON pH
1. Positively charged or basic amino acids include Arg, His, Lys,
2. Negatively charged or acidic are Aspartame, Glutamate.
3. Polar uncharged amino acids include Asparagine, Glutamine, Serine, Threonine,Cysteine.
4. Aliphatic and nonpolar are Alanine, Isoleucine, Leucine, Valine, Glycine Proline, Methionine.
5. Aromatic and nonpolar include Phe, Tyr, Trp.
Few of the amino acids particularly Gly, His, and Cys do not fit into a particular group
Physicochemical properties of the 20 amino acids
Molecular weights of amino acids range from 75.1 to 204.2 daltons.
The MW of an amino acid residue is calculated by subtracting the MW of water, 18 daltons.
Hydrophobicity (or hydrophilicity) of the side groups of amino acids that make up the protein influences protein folding and thus the physical properties of that protein.
Range amino acids vary in their degree of hydrophobicity depending on the constituents
Amino acids display ionization behavior and can serve as hydrogen donors or acceptors,
Behave as acids and bases.
IONIZATION BEHAVIOR OF AMINO ACID
• Hydrogen donors or acceptors,• Behave acids and bases.
The isoelectric point (pI) of an amino acid pH at which the amino acid has no net charge. pH values above their pI (pH > pI) amino acids will be negatively
charged. At pH values below their pI (pH < pI) amino acids will be
positively charged. The pI for amino acids with no acidic or basic side chains range
from 5.0 to 6.3. Dissociation of α-carboxyl group provides pKa values of 1.8–2.7. At neutral pH molecule is a dipolar ion or a zwitterion amino acids
(Arg, Asp,Cys, Glu, His, Lys, Tyr) have ionizable side group
Aspartic acid and glutamic acid are acidic amino acids containing ionizable carboxyl side chains with pKa of 3.9–4.0 and 4.3–4.5,
Arginine, lysine, and histidine contain ionizable side groups withpKa values of 12.0, 10.4–11.1, and 6.0–7.0
Tyrosine and cysteine also have ionizable side chains with pKa of 9.7 and 9.0–9.5 for the phenolic hydroxyl and the thiol groups, respectively.
The total charge of an amino acid will be the sum of the charges.
Derived amino acids and conjugated proteins
Derivatives of primary amino acids.
Derived amino acids have covalently or non covalently bound moieties or maybe cross-linked.
The proteins that contain derived amino acids are called conjugated proteins.
Covalently bound groups may include phosphate or carbohydrate moieties, as in the case of phosphoproteins and glycoproteins.
Noncovalent groups may include lipids or nucleic acids as with lipoproteins, and nucleoproteins.
Cysteine is a common cross-linked amino acid found in foods, others include desmosine, isodesmosine, and di- and trityrosine.
Several simple derivatives of amino acids are found in several proteins.
Derived proteins are not naturally occurring proteins instead they are obtained by further chemical or enzymatic modification, in the cell or derived due to food processing
Peptides, oligopeptides, polypeptides, proteins Linked covalently through α-carboxyl group of one amino acid and
the α-amino group Another amino acid through an amide or peptide bond to form
peptides, oligopeptides, polypeptides, and proteins. Peptides with 10–20 residues are called oligopeptides; more called polypeptides. Polypeptides of more than 50 residues are referred to as proteins The free α-amino group of the first amino acid is the N-terminal,
and The free α-carboxyl of the last amino acid is the C-terminal end of
a peptide or protein.
Peptide bond (Cα – CO-NH-Cα) lie in a single plane.
Polypeptide can be represented as a series of Cα – CO-NH-Cα planes connected by Cα, with only N-Cα and Cα-Cφ and ψ dihedral angles.
Respectively, having rotational freedom. However, the rotations of N-Cα and Cα-C bonds are also restricted due to stearic hindrances from side chain groups. Due to these restrictions, the flexibility of a peptide and protein is also restricted.
When proline is involved in the peptide bond, the peptide bond is normally in a trans configuration.
Peptides, oligopeptides, and proteins only have one free α-amino and α-carboxyl group at either end of the molecule.
Which ionize similar to a free amino acid, and contribute to the acid–base properties of a protein, thus the total charge of the molecule
Protein structure
Primary, secondary, tertiary, and quaternary structure.
Primary structure of a protein is its specific amino acid sequence which in turn determines the secondary, tertiary, and quaternary structures of a protein.
The primary structure is the linear sequence of the amino acids that make-up the peptide or protein.
The primary structure is determined by its genetic code and post-translational covalent modifications.
The primary structure of a protein ultimately determines the physicochemical, and thus the functional properties of that food protein.
The biological function of a protein is determined by its secondary, tertiary, and quaternary structures.
Secondary structure of a protein is the local three-dimensional arrangement of a protein which is determined by the amino acid sequence of the polypeptide.
Secondary structure may result from Aperiodic or periodic structures.
Random coil is an Aperiodic structures and regions in the protein where consecutive amino acids residues possess different sets
HELICAL STRUCTURE: In food proteins, although α-, 310- and β-helix, are found, the right-handed α-helix is the most common and is also the most stable.
Φ AND Ψ
The rotations of the polypeptide backbone around the bonds between N-Cα (called Phi, φ) and Cα-C (called Psi, ψ).
The 310- and β-helix are not so common.
In α-helix each helical rotation has 3.6 amino acid residues.
Hydrogen bonding at N-H and C O groups gives structure.
α-helical structure is due to the helix surface being made up of hydrophobic (or nonpolar) residues as well as hydrophilic (or polar) residues.
Poly peptide chain
Quaternary structure in a protein is determined by the thermodynamics.
stabilized by noncovalent interactions such as hydrogen bonding,
hydrophobic, and electrostatic interactions protein structure.
Higher levels of structures food proteins may be classified as globular or fibrous proteins.
Globular proteins: are those that the polypeptide chain folds to form a globular shape.
Forces involved in stability of proteins
• Three-dimensional structure is complex.
• Intra- and intermolecular interactions.
• Intramolecular interactions forces intrinsic.(i.e., stearic, van der Waals),
• Intermolecular interactions result surrounding solvent (i.e., hydrogen bonding, electrostatic, and hydrophobic interactions).
• During protein folding all the thermodynamically favorable interactions are optimized
• Thermodynamically unfavorable interactions are minimized.
Hydrophobic interactions Thermodynamically unfavorable interaction of nonpolar
groups with water Minimizing their association with water.
Hydropathies
Hydrophobic and hydrophilic tendencies of amino acid residue;
Greater the hydropathy of an amino acid residue interior of the protein molecule.
Hydrophobic interactions are the main reason proteins fold into their tertiary structures,
Hydrophobic free energy provides stability to this structure.
Polar molecule if it has a permanent dipole. A permanent dipole is due to a difference in electronegativity between the atoms involved in a covalent bond.
Non polar molecule
Electrostatic interactions Van der Waals interactions
polarization of the electron neutral atoms in protein molecules. van der Waals interactions are relatively weak
The strength of these forces decreases rapidly, with increase in distance.
Hydrogen bonds are ionic interactions attached electronegative atom such as O, N, or S
Hydrogen bonds are essential to protein structure
Ionic interactions involve negative and a positive charge.
Covalent bonds or chemical cross-links
Covalent cross-linking of side groups found in proteins are disulfide bonds (S S).
Sulfhydryl (thiol) groups of two cysteine molecules Disulfide bonds may be inter- or intramolecular,
Folding of a polypeptide and protein
Stability : Stearic hindrances from side chain atoms.
Interactions: noncovalent and covalent
2.Sources of Protein
1. Animal-protein Products
Egg proteins= methionine bcystine+ lactalbumin Casein, Milk protein isolate, Lactalbumin, Whey-protein concentrate+ lysine and tryptophan Beef, tuna+ Threonine. Chicken and meat products. High In Lysine, Methionineþcystine, Threonine, And Tryptophan
Gelatin Or Collagen Is Animal Protein + Tryptophan
Protein digestibility-corrected amino acid score (PDCAAS)
Vegetable-protein ProductsCodex Committee on Vegetable Proteins (CCVP) has developed an international general standard for vegetable protein products (VPP).
SOYBEAN-PROTEIN PRODUCTS Dehulled and solvent-extracted remove the oil.
Flakes dried, resulting in defatted soy flakes.
USES• Bakery Products, breakfast cereals, beverages, infant formulas,
dairy, meat, and dairy and meat analogs.
FUNCTIONAL PROPERTIES Including gelling, emulsifying, water-holding, and fat absorbing
properties.
MAJOR TYPES OF SOYBEAN PROTEIN PRODUCTS
Including flour, concentrates, isolates and textured soybean protein.
Soybean flour
Full fat, low-fat and defatted, as well as toasted and textured.
Defatted soybean flour
Produced by grinding the defatted flakes. Protein content of about 50%.
USE : In bakery products.
FULL-FAT SOYBEAN FLOUR
Newer technology Soy milk and tofu
SOYBEAN PROTEIN CONCENTRATE
Aqueous alcohol extraction of defatted soy flakes. Protein content 70% Remaining portion mainly insoluble carbohydrates.
Wheat Gluten
Prepared by the wet extraction from wheat or wheat flours of Certain non-protein constituents (starch and other carbohydrates
Protein content of 80%on a dry-weight basis.
Although high in protein digestibility, Wheat gluten is drastically limiting in lysine,
Other Vegetable-protein Products
Pea protein concentrate 92%.
Cottonseed-protein products 60%.
Sunflower-protein isolate. 94%.
Peanut flour 37% to 50%.
Canola (rapeseed)-protein concentrate
DEFATTED COTTONSEED FLOURS 60% protein, N6.25
Fractionation: cellular proteins during isolate preparation also produces both favorable and unfavorable effects.
Storage protein isolates (99–100% protein) are low in lysine and the sulfur amino acids, low in protein quality.
Non storage protein isolates (76–85% protein)
Fractionation of the seed proteins Quality DFCSP varies physiologically active or ‘free‘ gossypol.
Gossypol is a binaphthyl, dialdehyde, polyhydroxyl pigment which is highly reactive and deleterious to monogastric animals, including humans.
Gossypol in the seed is in discrete extracellular glands.
Chemical structure of gossypol
Mycoprotein Products
Used only since 1985. Protein is made from a type of fungus, Fusarium venenatum
Mycoprotein production steps.
Organism is first grown in an aerobic, axenic, continuous fermentation system.
Using food-grade carbohydrate substrates and other components needed for growth.
The mycelium of the fungus is then heat treated to reduce the ribonucleic acid content to safe levels.
Single-cell protein sources tend to be high in nucleic acids, which can lead to excessive blood uric acid levels.
Binders, flavorings, and other ingredients are added to achieve desired organoleptic and Physical properties.
Considerable toxicity and nutritional testing
Protein quality was evaluated.
Protein quality of mycoprotein is similar to that of soybeans.
Brand name, QuornTM, in the UK and Europe for some 10–15 years and has secured considerable consumer acceptance.
USA Mycoprotein is typically 12% water, 3% fat, 3% available carbohydrates, 6% fiber, and 2% ash. B complex vitamins and mineral nutrients are also present in small amounts.
Leaf-protein Concentrate
Green leaves are protein factories producing good quality protein.
Low concentration, high fiber content, and palatability problems,
vegetables, such as lettuce, spinach, and cabbage. However, some green forage crops produce several times more protein per unit area.
1960s and 1970s many product development
LPC obtained by harvesting leaves by first pressing out the juice.
Heat-coagulated
Serum drained away. Solid material dried and powdered.
‘whole‘ leaf protein concentrate (WLPC),about 45–60% crude protein,
or 34–45% true protein.
There are different types of protein in leaves that can be separated by coagulating at different temperatures.
ALFALFA the protein digestibility of the WLPC is about 88%, WLPC also contains significant amounts of vitamin A precursors, iron, and other nutrients which may bereduced in the white-protein fraction.
Microbial-biomass Protein The term microbial-biomass protein was coined to permit the
inclusion of protein from multicellular fungi.Microbial-biomass protein Possible way to produce useful food Reducing waste products and surplus raw materialsIndustrial and agricultural activities such as pulp mill waste liquor.100 plants producing microbial biomass protein, Economical availability of a suitable substrate,Assurance for safe food materialsTechnology and facilities to produce attractive food products.
Conclusion
Physicochemical properties of food proteins, peptides, and oligopeptides and understanding the forces that contribute to their stability will provide us the tools to better utilize food proteins in food products.
Addition of beef to vegetable protein sources proves significantly the protein quality of soy, pea,peanut, sunflower and wheat-gluten-protein sources.
