Meat Processing Flashcards
Collagen
Most abundant protein in multicellular animals
Extra-cellular glycol-protein organised into fibres
High tensile strength
Stress and load bearing
Collagen structure
Triple helix
33% glycine
15-30% proline
Sugars are bound to amino acid residues
Collagen synthesis
Polypeptide synthesis Hydroxylation of lysine and proline (Needs vitamins C) Glycolysation Triple helix forms Secrete from cells in soluble form Mature into fibre bundles
Hydroxylation
Peptide chain formation
Glycosylated
Forming a triple helix
Hydroxylysine
Cross link
Collagen Degradation
When heated to 60 degrees collagen fibrils are degraded to constituent molecule
Forms sol in water
Most stable below 30 degrees
Myoglobin
Myoglobin is a haem protein
Absorbs oxygen from blood and stores in muscle
When muscle needs more O2 it released from myoglobin
Myoglobin and cooking
When myoglobin is heated it denatures
Changes texture and colour of muscle
Beef most tender if heated to 65 degrees
Purpose of curing meat
Store meat at ambient temperature
Curing meat process
Immersed in brine
24% NaCl
0.3% NaNO3
0.1% NaNO2
NaCl and curing meat
2-6% in final product
Increases water holding capacity of cells
Reducing water activity
Inhibit microbial growth
NaNo3 and curing meat
Added as additional preservative
When O2 is low it can transfer NO3 to NO2
NaNO2 and curing meat
Active curing agent
Strong oxidant
Inhibits microbial growth of anaerobic bacteria
How does NaNO2 inhibit microbial growth
Oxidises Deoxymyoglobin to make metmyoglobin
Metmyoglobin reacts with nitrite to nitrosyl myoglobin
Nitrite breaks down to produce NO
NO forms with nitrite which may react with non-haem protein to form nitroso derivatives (N-nitrosamines)