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5) Food Product Development > Technical Challenges (1) > Flashcards

Technical Challenges (1) Flashcards

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1
Q

what 2 main categories can food ingredients be divided into? what does each consist of?

A
  1. macrocomponents: water, protein, CHO, lipids

2. microcomponents: vitamins, colorings, flavorings, preservatives, emulsifiers, etc…

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2
Q

define a food additive

A
  • any chemical substance that is added to food during prep or storage
  • either becomes part of the food or affects its characteristics for the purpose of achieving a particular technical effect
  • eg: substances used to enhance appearance, texture, keeping qualities of a food
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3
Q

according to the canadian food and drug regulations, what do food additives not include?

A
  • food ingredients such as salt, sugar, starch
  • vitamins, minerals, AAs (other than ascorbic acid and dicalcium phosphate)
  • spices, seasonings, flavoring
  • agricultural chemicals
  • vet drugs
  • food packaging materials
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4
Q

what should a food additive not be?

A

should not

  • mask faulty manufacturing processes
  • conceal damage or spoilage
  • be used to deceive the consumer
  • be used to obtain desirable results that should be obtained through GMP
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5
Q

how are food processing aids different than food additives?

A

food processing aids have no regulatory definition/requirements

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6
Q

what are main interactions of ingredients in food systems which occurs?

A
  1. among macrocomponents
  2. between microcomponents
  3. between micro and macro components
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7
Q

what is the goal of manipulating ingredient interactions?

A

to enhance desirable attributes of foods while minimizing or eliminating undesirable attributes

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8
Q

what are the thermodynamic similarities of formulated foods due to?

A

common behavior features of structure forming food macromolecules

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9
Q

interactions between macrocomponents may favor what phenoma? (examples)

A
  • thermodynamic incompatibility
  • interbiopolymer complexing
  • protective colloids
  • bridging
  • flocculation
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10
Q

describe functionality

A

property of a food ingredient that affects utilization, except its nutritional value

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11
Q

what are some examples of functional properties of proteins?

A
  • coagulation
  • gelation
  • structure formation
  • emulsification
  • water holding capacity
  • foam formation
  • fiber formation
  • fat absorption
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12
Q

what do the properties of protein (eg. AA composition, ionization state of AA, ionic strength, pH) effect?

A
  • electrostatic interactions b/w charged amino and carboxyl groups
  • H bonding b/w OH and carboxyl groups
  • hydrophobic interactions b/w two non-polar residues
  • covalent disulfide linkages between cysteine residues
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13
Q

how does isoelectric points affect functional properties of proteins?

A

at IE point, functional properties are mostly at max or min levels

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14
Q

how does pH affect elastic type wheat proteins?

A
  • pH at isoelectric point gives the greatest amount of strength
  • pH away from isoelectric point has greatest extensible properties (higher tenderness)
  • can use this to influence the ratio of elasticity and extensibility
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15
Q

how can proteins be denatured?

A

by altering H bonds, hydrophobic interactions and salt linkages

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16
Q

what are 2 types of protein denaturing agents? what are examples of each?

A

physical (heat, shaking, high pressures, UV light)

chemical (pH, salts, synthetic detergents)

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17
Q

define a gel

A

continuous 3D, solid like, cross liked network of protein molecules in an aqueous solvent

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18
Q

protein gelation is responsible for what characteristics?

A
  • viscoelasticity and texture
  • juiciness
  • viscosity
  • adhesiveness
  • water retention
  • stability of emulsions and foams
  • stimulation of mouthfeel of lipids
  • retention of sugars and flavors
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19
Q

what rheological properties can vary between different gels?

A

cohesiveness
hardness
stickiness
adhesiveness

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20
Q

what three events occur in protein gelation? describe each step

A
  1. denaturation: partial unfolding of proteins with changes in secondary structure by heating or treatment with acid, alkali and urea
  2. aggregation: polymer-polymer and polymer-solvent interactions are balanced
  3. crosslinking: provides fluidity, elasticity and flow behavior gels with high strength and stability
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21
Q

what three treatments can cause denaturation of proteins?

A

acid
alkali
urea

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22
Q

crosslinking provides what during protein gelation?

A

fluidity
elasticity
flow behavior

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23
Q

the gelling ability of proteins is influenced by what?

A
  • protein concentration
  • AA composition
  • molecular wt
  • hydrophobicity of proteins
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24
Q

the development of the 3D network during gel formation is influenced by what?

A
  • method of protein prep
  • processing conditions
  • environmental factors (pH and ionic strength)
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25
Q

describe the gels formed at the isoelectric pH of proteins. why is this?

A
  • less hydrated and less firm
  • structure of gels will be more aggregated instead of ordered
  • translucent or turbid

b/c of lack of repulsive forces

26
Q

at isoelectric pH of proteins, repulsive forces are ____ (incr/decr) and aggregation/precipitation is (incr/decr)

A

decreased repulsive forces

increases aggregation and precipitation

27
Q

define WHC

A

water holding capacity

ability to hold its own and added water during the formulation and the application of forces, pressing, centrifugation or heating

28
Q

what interactions are important for the water holding capacity of proteins?

A

protein-water interactions

29
Q

WHC plays a major role in what?

A

formation of some food texture, taste and tenderness

30
Q

why is understanding the WHC important?

A

to prevent:

  1. loss of H2O during cooking or freezing, which may result in a drier and tougher pdt
  2. evaporation and condensation of water on packaging material
  3. syneresis
31
Q

define syneresis

A

contraction of a gel accompanied by the separating out of liquid

32
Q

describe swelling capacity

A
  • enlargement of food systems
  • first step in the solvation of proteins
  • defined as spontaneous uptake of H2O by a protein matrix
33
Q

what does swelling characteristics not include?

A

characteristics of:
soy isolate
Na caseinate
whey protein

34
Q

how does protein ingredients with very high WHC affect other components?

A

can cause dehydration of other components

35
Q

how does WHC of proteins affect other formula components?

A

high WHC proteins can cause dehydration of other components. Thus, this affects the order of dry ingredient incorporation into the formula

36
Q

how does WHC affect the packaging materials?

A

WHC can be used to determine kinds of packaging materials needed to maintain required moisture content of the pdt

37
Q

how can WHC of protein ingredients be predicted?

A
  1. from type (imino and aminocarboxyl groups)

2. number of polar groups in protein polypeptide chain

38
Q

what 3 types of side chains are found in proteins? how many water or AA molecules do each of them bind to?

A
  1. non-polar AA side chains (alanine and valine): binds 1 water or AA
  2. polar side chains: binds 2 or 3 water or AA
  3. ionic side chains (aspartic acid, glutamic acids and lysine): finds 4 to 7 water or AA
39
Q

what are methods of determining WHC of protein ingredients?

A
  1. standard test improved by the AACC

2. absorption isotherm (shows amount of H2O absorbed by the protein as a function of relative water vapor pressure)

40
Q

describe the absorption isotherm graph

A

water content increases fast during Aw = 0 to 0.3 and Aw = 0.8 to 1.0

water content increases slowly during Aw 0.4 to 0.75

”s” shape increase in water content as water activity increases

41
Q

what are factors influencing WHC?

A
  • protein conc
  • pH
  • ionic strength
  • temp
  • presence of other components of foods
  • length of heat treatment and storage conditions
42
Q

what are types of food emulsions?

what are the phases in each? what texture do they have? examples?

A
  1. oil in water (o/w):
    - water is the continuous phase
    - oil is the discontinuous phase
    - creamy texture
    - eg. reconstituted milks
  2. water in oil (w/o):
    - oil is the continuous phase
    - water is the discontinuous phase
    - greasy texture
    - eg. margarines and fatty spreads
43
Q

how does emulsification affect hydrophobic portions of the protein?

A

aligns the hydrophobic portions of the protein with the fat so they can interact

44
Q

how is emulsification and hydrophobicity correlated

A

positive correlation

higher emulsifying capability = higher hydrophobicity of proteins

45
Q

what are 3 characteristics used to describe emulsifying properties of proteins?

describe each.

A
  1. emulsifying capacity (EC): amount of oil (mL) emulsified under specific conditions by 1g protein
  2. emulsifying stability (ES): capacity of emulsion droplets to remain dispersed without separation by creaming, coalescing and flocculation
  3. emulsifying activity index: EA m^2/g
46
Q

what do emulsifying characteristics of proteins depend on?

A
  • source of proteins
  • properties on conditions of emulsification
  • conc
  • pH
  • ionic strength
  • viscosity of system
  • solubility
47
Q

what are the types of emulsion instability?

A
  • coalescence
  • flocculation
  • creaming
  • breaking
48
Q

what is HLB? what is the equation used?

A

hydrophile lipophile balance

HLB = (wt of hydrophilic) / (wt of total) x 100/5

49
Q

how is HLB value and protein hydrophobicity related?

A

[pro hydrophobitiy] = 1- [HLB]

[pro hydrophobicity] = NP residues] / ([NP] + [polar])

50
Q

how are proper emulsifiers chosen?

A

choose an emulsifier with the HLB value which matches required HLB value of the oil or lipid to be emulsified

51
Q

describe the emulsification properties of milk proteins

A
  • good heat stability
  • good emulsification properties
  • works well in retorted beverages in a neutral pH
52
Q

describe the emulsification properties of soy proteins

A
  • good emulsion-stabilizing properties

- functional properties are important in comminuted meat pdt

53
Q

describe the emulsification properties of whey proteins

A
  • favourable for stabilizing emulsions and foams in acid-stable proteins
54
Q

describe the emulsification properties of gelatin

A
  • able to protect colloids
  • inhibit growth of sugar crystals
  • prevents formation of hard, gritty texture and a poor mouthfeel
55
Q

compare using one protein versus combination of proteins

A

combination of multiple proteins is better to achieve desired properties

56
Q

define foaming

A

creation and stabilization of gas bubbles in a liquid

57
Q

what is essential for the formation of protein-based foams?

A
  1. diffusion of protein to the air-water interface to reduce surface tension
  2. partial unfolding of the protein association which leads to an intermolecular cohesive film
58
Q

the foaming properties of proteins encompasses what 2 aspects?

A
  1. ability to produce a large interfacial area

2. ability to form a tenacious interfacial film that can withstand internal and external forces

59
Q

what does “overrun” mean

A

the foaming capacity of the protein

overrun = (vol of foam - vol of initial liquid) / vol of initial liquid x 100

60
Q

how is foam stability expressed?

A

the time required for 50^ of the liquid to drain from a foam

or for a 50% reduction in foam volume

61
Q

what are hydrophobins?

A
  • a unique class of proteins produced by filamentous fungi

- has good interfacial and foam stabilizing properties

62
Q

what is an example of how viscosity is related to gelation and protein-protein interactions?

A

modifications of isolated soy proteins produces low to very high viscosity pdts

5) Food Product Development (12 decks)

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