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The Protein BridgeLinking Protein Structure to Function and Application
Julie Emsing MannMay 6, 2015
Overview
• Protein Selection• Structure Determines Functionality• Functionality Determines Application• Application Examples• Overview of Current and Emerging Protein Sources
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Protein Selection
• Protein concentration• Protein functionality desired• Protein fortification desired• Protein quality (PDCAAS)• Protein sourcing/availability• Clean label production• GMO status• Sustainability • Consumer Acceptability• Allergenicity• Kosher requirements• Price/lb
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Protein Selection
Protein Primary Functionalities Limiting Attributes
Dairy Emulsification, Gelation Cost volatility, Lactose
Soy Emulsification, Structure Soy flavor
Gelatin/Collagen Gelation, Water-binding Pork/beef derivation
Peanut Flavor, Texture Aflatoxin concerns
Almond Flavor, Texture Cost
Wheat Film Formation, Structure Gluten presence
Egg Aeration Unstable to heat
Muscle Binder, Gelation Meat processing/Safety
Bean Binder, Viscosity Bean flavor
Algal Gelation, Emulsification Consumer Perception Unknown
Canola Binder Consumer Perception Unknown
Pea Emulsification, Binder Pea flavor
Rice Bran Film Formation, Binder Consumer Perception Unknown
Traditional
Emerging
Protein Structure Dictates Function in Food and Beverage
Amino acid Basic unit
•Differ by their side chains •Charged
PeptideShort chain of AA’s
•Joined by peptide bond
ProteinPolymers that fold into a 3D structure
http://www.chemicalconnection.org.uk/chemistry/topics/view.php?topic=5&headingno=3
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Peptide bonds
Bond type
H-Bonds
Hydrophobic,Di-sulfideIonic
Hydrophobic
http://www.ucl.ac.uk/~sjjgsca/ProteinStructure.html
Protein Denaturation Affects Structure
DENATURED STATE
• Loss of native conformation• Altered secondary, tertiary or quaternary
structure• May be reversible or irreversible, partial
or complete
• Results• Decrease solubility• Increase viscosity• Altered functional properties• Loss of enzymatic activity
NATIVE STATE
• Usually most stable and soluble• Polar groups usually on the
outside• Hydrophobic groups on inside
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Denaturing Agents
Temperaure pH Shear
High Pressure Processing
Organic Solvents Salts
Oxidizing and Reducing
Agents
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Beyond the Specification Sheet
• Basic spec sheet information is not sufficient to understand protein ingredients.
• Ask suppliers if they can provide you information on:• How the protein was processed
• Heat• Filtration
• Degree of denaturation through processing
Protein Structure Functionality
Knowing the structure and degree of denaturation in selected protein source is fundamental to predicting its functionality. The environment plays a role as well.
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Protein Structure is Highly Dependent on Environment
pH Temperature
Dielectric constant
Ionic strength
Other Molecules Air
Fat Denaturing Agents
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Proteins Strive to Achieve Lowest State of Free Energy
Hydrophillic
Hydrophobic
Protein in Aqueous Solution (Native)
Isolated Protein
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Protein Ingredient Functionality in Food
Water Binding Viscosity Gelation
Foaming Emulsification Browning
Flavor/texture Protein fortification/nutrition
Protein Functionality Importance
• Shorten development time• Aid scale-up efficiency• Save $$$• Ensure stable products through-
out shelf life• Provide unique function leading
to novel products
Understanding protein
selection and functionality for specific
projects can:
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Interactions Effecting Food Protein Function
1) Protein/Water interactions• Hydration of protein
• Solubility, water absorption, wettability, viscosity
2) Protein/Protein interactions• Within or between proteins
• Network building, precipitation, gelation
3) Protein/Other interactions• Air, fat, carbohydrates
• Surface tension, emulsification, foaming/aeration, film forming
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Protein Solubility
• Functional properties of proteins depend on their solubility
• Charged amino acids have primary role in protein solubility• The proteins are least soluble at their
isoelectric point
• The proteins become increasingly soluble as pH is increased or decreased
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Critical Parameters to Understand Functionality
The Protein1. Protein type/structure
Solubility: Hydrophillic and hydrophobic exposure
2. Protein concentrationMore protein = more water uptake, molecules closer together
3. Protein denaturationHow much protein is denatured pre-process?
The Food/Bev System1. pH
• Acidic, neutral or basic
2. Interactions with other compounds:
• Proteins• Carbohydrates• Salts/Minerals
The Process
1. Heat treatment
2. Shear
3. Pressure
Solubility- Beverage Example
• Primary proteins utilized: • Dairy, Soy
• Production• Hydration of protein and hydrocolloid, other
ingredients• Heat treatment• Homogenization• Filling
• Chemistry• Stabilization of protein with hydrocolloid
interaction• Homogenization reduces particle size
Gelation- Gummy Bear Example
• Primary Proteins Utilized: • Gelatin
• Production:• Boiling of sugar/corn syrups, addition of
gelatin, removal of water, cooling and forming/depositing in starch molds to remove surface moisture.
• Chemistry:• Collagen molecules are mobile in hot
water, as cooling occurs, they are restricted
• Junction zones form and bond the molecules together, forming a gel network
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Gummy Bear Sample Formula
Ingredients %
Gelatin-Type A 9.00
Water 15.00
Sucrose 32.00
Corn Syrup (43 DE) 42.00
Citric Acid Solution 1.00
Flavor 0.50
Color 0.50
Total 100.00
Procedure: (1) Hydrate gelatin in hot water, cool to form gelatin plug, cut into pieces(2) Combine and boil sucrose, corn syrup to reach X solids (temp)(3) Add pieces of gelatin to cooked syrup, mix well(4) Add remaining flavor, color, acid(5) Deposit into starch molds
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Foaming-Marshmallow Example
• Primary Proteins Utilized: • Egg albumen, gelatin, hydrolyzed soy
or milk• Production
• Frappe produced: aerated/whipped• Syrup produced, cooked, added to
frappe• Gentle mixing, slab or deposit
• Chemistry • Hydrophobic amino acids orient
towards gas phase• Viscous protein solutions create more
stable final foams
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Protein Evolution
Dairy Soy Egg
Wheat
Pea
Canola
Potato
Pulses
AlgaeLemna
RuBisCoInsectsWolffia
Knowledge Building
Dairy
Pros:• Whole food perception• Mixture of casein and
whey• Complete protein• 40-90% protein content• Excellent functionality• Long history of usage
Cons:• Cost volatility• Animal derivation• Consumer concerns
over antibiotics and hormones in milk
Soy
Pros:• Plant derived• Complete protein• Predominately glycinin and β- conglycinin
• 40-90% protein content• Excellent functionality• Heart health claim• Long history of usage
Cons:• Anti-nutritionals• Off-notes/beany• Perception of
hormone/estrogenic
Gelatin
Pros:• Pure protein• Unique gelling
properties• Heat Stable• Intact or hydrolyzed• Health Linkages:
• Joint health linkage• Beauty from within
• Gluten free
Cons:• Animal source• Not Kosher• Not a complete
protein
Pulses
Cons:• Newer science and
technology• Not complete proteins
Pros:• Plant derived whole
food• Contains fiber and
protein• Sustainable• Many regions of world
already rely on this in their diet
Wheat Protein
Cons:• Not a complete protein
• Low lysine
• Gluten sensitivity
Pros:• Unique functionality
from gliaden and glutenin
• Elastic properties can not be duplicated with other proteins
• Bland flavor profile• Low cost
Emerging Protein SourcesSource Forms Available Maximum
ProteinSupply Sufficiency
Algae Flours: high protein or high lipid
55% Medium
Canola Flour, isolate, hydrolysate 90% Small/Medium
Oats Flour, concentrate 55% Small/Medium
Flax Meal, concentrate, crisps 50% Med/Lg
Hemp Seed, flours, concentrates 50% Small
Quinoa Seed, crisps, flours 65% Small
Rice Flour, concentrates, crips 80% Medium
Sunflower Flour, concentrate 70% Small
Lemna Flour, concentrate 65% Small
• Contain highly functional and nutritional protein.• Consumption areas are predominantly outside of the US.
Live Crickets Dried Crickets Live Meal WormsDried Meal
WormsMoisture, % 69 8 61 6Fat, % 5 15 13 22Protein, % 20 60 20 60Fiber, % 3 8 2 10Ash 2 8 2 1Ca, ppm 345 No data available 133 283P, ppm 4238 No data available 3345 2161
Insect protein
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