MIDTERM 1 REVIEW Flashcards
objective vs sensory evaluation
objective: quantitative, unbiased, uses instruments
sensory: subjective, human experience, qualitative
objective measurements
physical measurements:
- mass (g), volume, (L), density (g/L), specific gravity
- moisture: pressing, wettability
- texture: tensile strength, puncture strength, torque % sag
- color: standardized systems
chemical measurements:
- pH, nutrient analysis, sugar concentration, saltiness
physiology of sensory evaluations
olfactory receptor neurons (10 mil)
- volatile/aromatic compounds
taste receptors (10 thous)
- sweet, salty, sour, bitter, umami
- umami: amino acid, savory
other flavors
- astringency, coolness, heat, glucosinolates
subthreshold levels
affect of salt, acid, sugar
salt
- inc sweetness
- dec sourness
acid
- increase saltiness
sugar
- decrease saltiness
- decrease bitterness
types of sensory tests
- single sample (acceptability)
- descriptive (scoring of attributes)
- affective (preference)
- difference test
a. paired comparison which has greater amt of characteristic
b. duo-trio (which sample of two is diff from control)
c. triangle test (3 samples, which is diff)
proteins in food
foam, thickening, structure
protein stcuture
contains amino group (NH3), carboxyl group (COOH… carbonyl + OH + R); held together by peptide bonds
- primary: sequence of a chain of AA
- secondary: sequence of AA linked by hydrogen bonds (pleated sheets; alpha helix)
- tertiary: attractions present between alpha helices and pleated sheets
- quaternary: protein consisting of more than one AA chain
***secondary protein structure:
- necessary for function
- lowers thermodynamic state
- prevents aggregation
types of proteins
globular protein (varying solubility)
- enzymes
- hormones
- transport proteins
fibrous proteins (insoluble in water)
- structural proteins (ex: collagen)
conjugated proteins
- bound to lipids
- carbs
- metals
- phosphorous
- (ex: lipoprotein)
*** what type of protein would you expect rennin to be?
denaturation & coagulation in food science
1) heating/beating leads to denaturation
- tertiary structure lost
- inc viscosity, dec solubility
- dec water holding capacity
- inactivate enzymes
- (continued) heating/beating leads to coagulation
- R groups: crosslink: aggregation
coagulation: isoelectric point
- point at which protein carries no electrical charge
- protein is least soluble at isoelectric point
*** (1) a positive charge on each molecule keeps them apart (2) when molecule loses charge they clump together
hydrolysis
- heat of pH to break peptide bonds
- inc solubility
- dec thickening
- meat tenderizing
egg structure
- yolk, germinal disc, vitelline membrane
- chalaza, air cell
- thick albumen, thin albumen
- inner membrane, outer membrane, cuticula
egg formation
- development of ovum in ovary
- possible fertilization
- egg white develops as it moves through oviduct
- shell forms in oviduct
- bloom (cuticula) forms
- intestine merges and egg is laid through same pathway feces are excreted
egg nutrition
white
- *3.2 g protein
- trace amount of fat
yolk
- 2.4 g protein
- *4.6 g fat (half saturated)
*overall
- 186 mg cholesterol in large egg
- fat soluble vitamins
- B12
- minerals
- sometimes omega 3s
proteins in egg albumin
*ovalbumin: 54% of protein
conalbumin: binds metals if uncooked
ovamucoid: inhibits trypsin if uncooked
lysozymes: breakdown bacteria
ovamucin: thick albumin
avinid: binds biotin if uncooked