8: Food Proteins Flashcards

1
Q

Explain the composition of milk

A

Made up of fat; casein; whey protein; lactose, etc. etc.

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2
Q

What is casein?

A

Composed of alpha, beta (phosphoproteins) & K-caseins (glycoproteins)
- Caseins self assemble into protein packets called casein micelles (a/b caseins are held together inside by hydrophobic interactions, whereas K-caseins remain at the surface to allow suspension in milk)
- Micelles are in close association with calcium phosphate, giving milk white appearance

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3
Q

Explain the importance of casein in the food industry

A
  • casein is the most dominant protein in bovine milk
  • the caseins are dispersed in water solvent and carry a significant amount of calcium
  • the dairy industry is able to separate these proteins = wide array of functional ingredients
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4
Q

How is the separation of casein from skimmed milk achieved?

A

Using a centrifuge. Separate cream from skim milk (plasma phase)

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5
Q

What are the casein-based ingredients that are obtained by methods that separate caseins?

A
  • skimmed milk powder (SMP
  • acid casein
  • rennet casein
  • caseinate
  • milk protein concentrates (MPC)
  • phosphocasein
    (all obtained as powder)
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6
Q

Skimmed milk powder (SMP) is the major milk derived ingredient. Describe the method by which it is obtained

A
  • requires no major separation processes except removing fat component by centrifugation
  • skimmed milk is then pasteurised = heat induced denaturation in whey protein, which attach to the casein micelle
  • samples are then evaporated and subjected to spray drying, producing a powder
  • SMP is soluble following reconstitution & can be used for further processing e.g. UHT
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7
Q

How is acid casein produced?

A

(preliminary step in the production of yoghurt)
- caseins self aggregate by changing the pH of skimmed milk from 6.7 (natural pH) to 4.6 (isoelectric point)
- pH is reduced by using hydrochloric acid; sulphuric acid & lactobacillus sp.
- allows for concentration of caseins & elimination of lactose, whey proteins & minerals as these are soluble at low pH
- water washing facilitates casein concentration before being pasteurised & dried

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8
Q

How is rennet casein produced?

A

(preliminary step in the production of cheese)
- caseins self aggregate due to the action of rennet, resulting in formation of curd & whey
- calcium is recovered
- subsequent treatment of curd is similar to acid casein manufacture
acid/rennet caseins : very efficient method of producing high casein ingredients but dried protein is insoluble when reconstituted in water

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9
Q

How is caseinate produced?

A

Neutralisation of acid/rennet casein through alkali addition
- this pH change converts insoluble acid caseins into casein dispersions = recovery of functional properties e.g. ability to bind water, rehydrate or dissolve
Reagents used to increase pH = sodium hydroxide, calcium hydroxide, ammonium hydroxide, sodium carbonate
- If pH is adjusted with sodium hydroxide, insoluble acid casein becomes a ‘soluble’ translucent dispersion called sodium caseinate
- if pH is adjusted with calcium hydroxide, resulting caseinate is a white colloidal dispersion called calcium caseinate

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10
Q

How are milk protein concentrates (MPC) produced?

A

Concentration of casein by membrane technology
- contains both casein and whey proteins and low lactose conc.
- if at least 90% of protein (casein and whey), the product is named milk protein isolate
- calcium fraction is in its native micellar form and therefore carried significant quantities of calcium phosphate
- used for nutritional properties: suitable for protein fortified beverages

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11
Q

How is phosphocasein produced?

A

concentration of casein using micro filtration
- only contains micellar casein with calcium phosphate as whey proteins, lactose and soluble salt fractions are eliminated
- following evaporation & drying, a 75-80% protein powder is produced; rehydration possible
- however stability at processing temps is limited : reintroduction of soluble milk salts restore stability
- phospchocasein exhibits a physical-chemical behaviour similar to milk in terms of rennet/acid gelation

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12
Q

What are the uses and application of casein-based ingredients?

A

(Depends on the required end result : liquid or solid)
Ability to be stable to high heating treatments is an important property
* acid gels (sodium/calcium caseinate; phosphocasein & SMP. Control gel behaviours during fermentation by bacterial cultures. e.g. yoghurts and cream cheeses)
* recombined milk products (SMP due to stability at high temps. Stored in cans or UHT treated to ensure long life)
* food emulsions (help with flavour, texture, colour. Sodium caseinate used due to high pressure stability. Both oil in water emulsions e.g. mayo, ice cream; and water in oil emulsions e.g. table spreads)
* cheese analogues (rennet casein used. needs to go through disaggregation by adding calcium salts and then rehydrated in water)
* cream liqueur
* chocolate (composed of SMP and whey powders)
* bakery (SMP and whole milk powder often used)

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13
Q

What are the most abundant whey proteins?

A

Beta-lactoglobulin
alpha-lactalbumin
Glycomacropeptides

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14
Q

What are the 3 whey-protein based ingredients?

A
  1. whey protein concentrates = obtained by ultrafiltration to remove water, lactose & minerals. Loss of a-lactalbumin may happen
  2. whey protein isolates = obtained by ion exchange separation; wash out lactose, minerals & caseinomacropeptide
  3. Whey hydrolysates = protein hydrolysis by incubating with proteolytic enzymes at elevated temp. (37-40 degrees)

Whey proteins are normally supplied as dry powders

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15
Q

What considerations need to be made as a result of the manufacturing process?

A

a) effect of heat treatments : pasteurisation & drying. Denaturation of immunoglobulins and serum albumin
b) changes during storage of dry powder : whey proteins can undergo “dry” Maillard reactions
c) flavour of whey protein hydrolysates : presence of hydrophobic peptides with characteristic bitter flavours

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16
Q

what are the functional properties of whey protein ingredients?

A
  1. solubilisers (clear sports drink folmulation)
  2. gelation (when heated at conc. over 10%)
  3. foaming (formation of aerated foods e.g. meringues)
  4. emulsification (in simple oil in water emulsion systems, comparable with sodium caseinate)
17
Q

what are the nutritional properties of whey protein ingredients?

A
  1. infant formulations (hydrolysates : hydrolysis breaks down possible allergenic proteins such as B-lactoglobulin)
  2. sports nutrition (high levels of branches chain amino acids, which are preferentially metabolised by muscle rather than in the liver. Sports drinks & nutrition bars)
18
Q

Describe the nutritional value of meat

A
  • high biological value (composition close to human proteins)
  • contains essential amino acids (e.g. leucine, lysine, valine, etc.)
  • source of vitamins & minerals e.g. vit A/B, Fe, Cu, Zn, Se
  • high in saturated fatty acids
18
Q

What are the health concerns about eating meat?

A
  • energy dense diet low in fibre: increased fat consumption
  • chronic diseases: CVD, cancer
  • nitrites used in producing cured meats = potential carcinogen
  • food safety (salmonella, E. coli, Campylobacter)
  • bacterial resistance to antibiotics
19
Q

Explain the classifications of meat protein

A
  1. STROMAL PROTEINS - CONNECTIVE TISSUES 10-15% (collagen, elastin, reticulin)
  2. MYOFIBRILLAR PROTEINS 55% (actin, myosin)
  3. SARCOPLASMIC PROTEINS 30% (water soluble proteins : haemoglobin, myoglobin)
20
Q

Describe the structure and functional uses of collagen

A
  • has a triple helix structure
  • non polar, non charged
  • not valuable in processed meats (little binding ability), but chopped, ground, powdered collagen is useful as a gel (sausage casing, contact lenses, Pharmaceuticals)
  • degrades to gelatin at 65-80 degrees C -> is used as a food ingredient in many food products e.g. jams & jellies
21
Q

Explain how enzymes and pigments (sarcoplasmic proteins) impact meat

A

Enzymes e.g. calpain = tenderisation, flavour contribution
Pigments e.g. myoglobin (stores O2 in muscles); haemoglobin (transports O2 in blood) = responsible for colour variations in meat

22
Q

Describe the stages in post-mortem acidification

A
  1. animal dies, oxygen levels fall
  2. supply of oxygen to the muscles stops, respiration stops
  3. ATP is generated from glycogen: anaerobic glycolysis
  4. lactic acid accumulates and the muscle acidifies (from 7.2 to 5.5 pH)
23
Q

Why is acidification important?

A
  • Muscle proteins denature as pH falls
  • myosin & actin reach their isoelectric point: no electrical charge
  • loss of biological activity : water holding capacity and solubility
  • exudation of water from muscle fibres
  • light scattering properties of contractile elements increase
  • meat changes from dark and translucent to pale and opaque
24
What happens in tenderisation and conditioning of meat?
Tenderisation = muscles soften as myofibrils become fragmented; rate depends on species & temp Conditioning = continuation of tenderisation; myofibrils weaken; changes in connective tissue; calpins = flavour; better results above freezing point (1 degree)