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Meat emulsions - batters– Frankfurters are the best example
-produced with unique technology that is highly protein
dependent
-failures, i.e. “broken” emulsions are a dramatic mess
(fat caps where separated fat rises to upper ends of the
frankfurters as they hang on smoketrucks during
cooking, then solidifies into solid fat when chilled)
-successful, i.e. stable emulsion/batter is the result of 3
factors:
Emulsion/batter stability is determined by:
1. Meat quality
– meaning - myofibrillar protein content and functionality
– quality problems like PSE pork can result in emulsion/batter problems
– WHC and fat binding
2. Handling knowledge and technology
– meaning - appropriate use of salt, temperature, added water and chopping to properly manage soluble protein and dispersed fat
3. Additional binders to help stabilize emulsion/batters and control physical properties
Before we cover specifics --- some definitions
emulsion - stable dispersion of one immiscible liquid in another
– i.e. water-in-oil (mayonnaise, butter)
oil-in-water - frankfurters
– 30% fat is well-hidden
true emulsion
– dispersed particle size is 0.1µ or less
meat emulsion - particle size is typically 1.0 µ or more therefore often called a “batter”
What is “fat binding”?
1. Fat cell walls
– intact cells retain fat
– dried cells i.e. “salted” can be very stable due to collagen/cell wall rigidity and impermeability
2. Emulsification membranes
– myofibrillar proteins
– hydrophobic portion fat
– hydrophilic portion water
fat
protein
water
fat
Proteins rearrange somewhat and consequently lose some water binding ability (know this)
Therefore there are three necessary components for every emulsion/batter
– internal phase
i.e. fat
– external phase
i.e. water
– emulsifier
i.e. protein
“Membranes” are critical to raw emulsion/batters -- but cooking then
results in:
3. Heat-set gelation - crosslinking proteins to form a 3 dimensional matrix
– semi-rigid “trap” for fat and water
– critical to cooked stability, texture, slicing, appearance
More definitions
– Emulsion/batter capacity
– maximum amount of fat or oil stabilized by a given amount of protein
– measured by oil-in-water dispersion with clear blender jar, colored oil, protein solution
– model system comparisons
– emulsion/batter stability– amount of fat or oil retained (or separated) after stressing, usually
with heat, a formed emulsion/batter
– practical comparisons
– affected by process technology and non-meat ingredients
Factors affecting stability can be found in Stokes Law:
D = diameter of fat globules
de = density of external phase
di = density of internal phase
k = constant
vis = viscosity
V = D2(de-di) k vis
– smaller fat globules are more stable (also require more protein)
– greater viscosity (protein solubility, protein quality, temperature, non-meat ingredients, salt concentration) is more stable
Practically: V = D2
vis
Processing parameters
1. Start with lean meat plus salt
– best at 4-5% (brine strength)
plus ice/cold water– temperature control
– increased protein solubility and swelling
– can chop or mix (extract) longer
– low temperature increases viscosity
2. Chopping/mixing
– two effectsa. dissolves (1-5%) and swells (remainder) of myofibrillar
protein
b. breaks fat cells and subdivides fat into small globules
– chopping needs to be extensive enough to achieve small fat globules with solubilized protein membrane coatings
– over chopping will destroy the protein membranes and “break” the emulsion/batter
– usually chop lean, salt, water to about 40oF
Critical considerations:
– chopper speed
– sharp knives
– bowl/knife clearance
– temperature control and monitoring
– add fat meat at 40oF and chop to 55oF (pork fat), 65oF (beef fat)
3. pH is critical
– Protein “functionality” is closely related to the pH - WHC curve / relationship– therefore increasing pH increases emulsion stability
– pre-rigor meat is 50% - 100% more effective than post-rigor– phosphates are important
– pre-blends (lean meat + salt + 1/2 nitrite) are very effective (and advantageous for cured color as well)
4. Collagen
– High collagen meat sources are a potential problem– high capacity, low stability
– forms membranes but converts to gelatin when heated
– however, ground/powdered collagen appears to be effective probably depending on adequate dispersion followed by gelatin formation
5. Other emulsifier proteins
– myofibrillar proteins might be best “saved” for WHC and gelation– “pre-emulsions” --- use another protein to coat fat
globules --- then add “pre-emulsion” as fat to meat mixture
– soy and caseinate
– skin / collagen is sometimes used
6. Vacuum processing
– Chopping/mixing under vacuum can increase capacity and stability
6. Vacuum processing
– microscopic observations show air “bubbles” probably surrounded by protein thus consuming some protein functionality– air competes with fat for the emulsifier making the
emulsion/batter less stable– more critical for round globular sarcoplasmic proteins than
for filamentous, long myofibrillar proteins
6. Vacuum processing
– product density and diameter will differ with vacuum– can contribute “plumpness”
– major effects on cured color development – with about 50 ppm in going nitrite vacuum will give good
cooked color while non-vacuum will give gray cooked color
– absence of air also will decrease likelihood of rancidity development– not as much an issue in cured meats as for fresh products
(i.e. pork sausage)
7. Stuffing
– Pressure flow of product, proper casing diameter
– minimize smear/separation of fat and breaking emulsion membranes prior to heating
8. Heating / cooking
– humidity– important to yields, thus is kept high --- only risk is
high collagen content
– heating rate– critical to proper protein gelation
– protein unfolding crosslinking gel formation
Remember:
– “Bind” values listed for calculating formulations with different meat ingredients reflect water and fat binding ability
Ex. Bull meat 17.0Pork picnics 16.050 pork trim 4.1Liver 1.25Beef hearts 0.3