PROTEIN INGREDIENT Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

CLASSIFICATION

A

GLOBULAR
FIBROUS
FLEXIBLE

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

GLOBULAR
PROTEINS

A

made up of polypeptide chains that fold into a densely packed shape due to hydrophobic effects, hydrogen bonding, electrostatic forces, van der Waals forces, and disulfide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

why is globular protein good emulsifying and foaming agents

A

due to non-polar regions on their surfaces that promote adsorption to oil–water or air–water interfaces

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

why is globular protein gelling agents

A

when heated, they unfold, exposing non-polar and sulfhydryl groups to the surrounding aqueous phase, causing aggregation via hydrophobic and disulfide bond formation.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Examples of animal-based globular proteins used in the food industry

A
  • Whey (α-lactalbumins, β-lactoglobulins)
  • Albumins (egg white)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Most plant proteins are globular:

A
  • Soy, pea, potato, mung bean, and rice proteins
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Many plant proteins only denature

A

at higher temperature

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Complex hierarchical construction of fibrous protein

A

bundles embedded inside connective tissue formed of triple helices of collagen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Collagen is derived from

A

animal tissues which are made up of
interconnected polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Actin and myosin molecules in muscle tissues are packed into

A

fiber-like structures, which contribute to the textural qualities of foods

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

only glutenin in wheat has cohesive and viscoelastic characteristics,

A

enabling it to form fibrous proteinaceous
networks which are widely utilized in alternative meat products

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Casein has a random coil structure

A

with hydrophobic and hydrophilic patches

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Caseins are highly stable at neutral pH

A

but can coagulate with an acid or enzyme (important in cheese and yogurt production)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Casein has excellent surface-active and stabilizing properties due to (high…)

A

high proportions of prolyl residues conferring open
and flexible conformations

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Casein has excellent surface-active and stabilizing properties due to (random…)

A

random coil shapes that include hydrophobic, hydrophilic regions and phosphate group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Animal-based proteins

A

1) Higher nutritional quality
2) Better technological functionality
3) major sources: dairy proteins (casein and whey) /meat (collagen: gelatin)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Plant-based proteins

A

1) Less complete nutrition
2)technological functionality
3)major sources: wheat/ soy protein/ peas and other legumes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

CASEINS is major component of milk because

A

it constitutes about 80% of milk protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

CASEINS contain

A

all the essential amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

casein is - amphiphilic

A

The hydrophobic, polar and charged residues are not uniformly distributed throughout the molecular sequences but occur as hydrophobic or hydrophilic patches

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

casein very flexible but

A

unstable structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q
  • Whey is the fluid by-product resulting from the
A

precipitation of proteins in milk

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

whey protein fraction of bovine milk contains
four main protein

A
  • β-lactoglobulin (β-Lg, 50%)
  • α-lactalbumin (α-La, 20%)
  • Blood serum albumin (BSA, 10%)
  • Immunoglobulins
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q
  • Whey proteins are the proteins remaining soluble at pH
A

4.6 and 20°C after the removal of caseins from milk

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Major forms of whey protein

A
  • Whey protein concentrate
  • Whey protein isolate
  • Hydrolyzed whey protein
25
Q

Whey protein concentrates (WPC)

A

a low level of fat and cholesterol but, in
general, have higher levels of bioactive compounds, and carbohydrates in the form of lactose

26
Q

Whey protein concentrates (WPC) available in

A

various protein concentration levels such as 34% (WPC34), 50% (WPC50), or 80% (WPC

27
Q

Whey protein isolate (WPI)

A

purest form of whey protein - Contains 90% or greater protein with minimal lactose (<1%)

28
Q

Whey protein isolate (WPI) virtually

A

no fat

29
Q

Whey protein isolate (WPI) are processed to

A

remove the fat and lactose, but are usually lower in bioactive compound

30
Q

Hydrolyzed whey protein

A

Predigested, partially hydrolyzed whey proteins - > easily absorbed

31
Q

Hydrolyzed whey protein maybe

A

Highly hydrolyzed whey may be less allergenic than other forms of
whey

32
Q

uses of caseins in food products

A

To modifying the physical properties of food product
To provide nutritional supplementation

33
Q

Casein micelles bind large amount of water due to

A
  • Mechanical entrapment of water in the micellar matrix
  • k-casein ‘hairs’ (having carbohydrate moiety) that protrude from the surface of the micelle
34
Q

Advantages of binding large amount of water

A
  • modify the texture of dough or baked products
  • serve as the matrix former in cheese-type products
  • increase the consistency of solutions such as soups
  • meats and sausages
35
Q

Acid and rennet casein are

A

insoluble in water

36
Q

High solution viscosity of casein is a result

A

of the very open, nearly random structures of casein molecules.

37
Q

The combination of sodium caseinate and certain other thickening agents

A

can greatly improve its thickening performance

38
Q

CASEIN SURFACE ACTIVE PROPERTIES &EMULSION PROPERTIES IMPORTANT IN?

A

Important in functional applications such as foaming and emulsification

39
Q

The caseins

A
  • small size migrate quickly to air/water or oil/water interfaces
  • open conformations allow them to spread readily at interfaces
40
Q

How casein is used as emulsifying agents

A

Used in as emulsifying agent - e.g. coffee cream

41
Q

casein have Excellent surfactant property

A

so is responsible for its use in whipped toppings, cake mixes, and ice-cream

41
Q

WHEY PROTEIN role in controlling the texture of food product

A
  • Highly soluble over a wide range of pH, especially acid pH
  • Able to produce firm gels on heating
  • Exhibit good fat and water binding properties
  • Good aerating agents
42
Q

Proteins are least soluble at the isoelectric point but whey proteins are soluble

A

over a wide range of pH values - desirable for use in beverage

43
Q

WPC & WPI - Have good dispersibility

A

dissolve quickly and without an excessive amount of agitation)

44
Q

Whey proteins have both hydrophilic and hydrophobic groups, which allow the proteins to

A

adsorb and unfold rapidly at the oil- water interface and form a layer that stabilizes the oil droplets and prevents flocculation and/or coalescence

44
Q

Whey proteins form irreversible gels by

A

restructuring into extended three- dimensional networks that have the capability to entrap fat and water

44
Q

in whey protein, A strong gel network helps hold this water and prevents moisture loss,

A

which assists in controlling syneresis.

45
Q

whey protein Heating increases the foaming properties

A

because heat unfolds protein molecules, to expose buried and alter their effective hydrophobic–hydrophilic balance

46
Q

whey protein in MEAT & MEAT PRODUCT

A
  • Water binding capacity
  • Viscosity
  • Emulsification
  • Addition of whey proteins affects the taste and improves the gelation
47
Q

whey protein in PRODUCTS WITH REDUCED
FAT CONTENt

A

Partially replace egg in cake (provide body & viscosity to cake batters - entrap air)

48
Q

how whey protein replace eggs

A

. 100 g fresh whole eggs = 15 g WPC80 + 75 g water
. 100 g fresh whole eggs = 35 g WPC34 + 75 g water

49
Q

addition of WPC 34 IN DAIRY PRODUCTS (YOGURT)

A

Addition of WPC34 at the level 0.7–2.0% or WPC80 at 0.5–0.8% is sufficient in the case of mixed yoghurt

50
Q

whey protein Replacing skimmed in yogurt

A

increased gel strength in solid
yoghurt,
increasing the viscosity of mixed yoghurt,
reduces the risk of syneresis in both types of yogurt

51
Q

Addition of whey protein gives yoghurt a

A

smooth and creamy texture & increases nutritional value

52
Q

soy protein in meat

A

enhance and stabilize fat emulsion, improve
viscosity, impart texture upon gelation following cooking and improve moisture retention and overall yields in comminuted meats (sausage, bologna, luncheon meats

53
Q

Soy proteins with good solubility will produce

A

better beverage mouthfeel and suspension stability

54
Q
  • The capacity of proteins to form stable foams with gas by forming impervious protein film
A

important property in some food applications including angel and sponge cakes

55
Q

Good foam stability properties of soy protein

A

can be used as whipping agents in combination with egg albumen or whole eggs in confectionery products and desserts

56
Q

Soy protein isolate is the preferred ingredient in infant formula due to

A
  • bland taste,
  • absence of flatus-producing sugars
  • negligible fibre content