BIO 169 LAB PRACTICAL 3 Flashcards
four macromolecule
- carbohydrate
- lipids
- proteins
- nucleic acid
what is a enzyme
protein catalysts
increase the rate of a reaction by lowering activation energy
substrate
the reactant in a reaction
product
result of a reaction
active site
location on enzyme where substrate binds
specificity
only substrate compatible with enzyme active site will elicit a reaction
denaturation
anything that changes the molecular shape of the enzyme and renders it nonfunctional
what environment affect enzymes
- temperature
- pH
- salt concentration
- chemical
what temp does the enzyme act optimally
body temp 37 degree C or 98.6 degree F
what does high temp do to enzyme
denature it
catabolic
break down substrate
type of catabolic reaction
hydrolysis
growth/building of substance
anabolic
a type of anabolic reaction
dehydration synthesis
breaking bonds of molecules using water
hydrolysis
monomers bind together to form a larger molecule
dehydration synthesis
primary source of energy for body
carbohydrates
monomers of carbohydrates
saccharides
monosaccharide
simple sugar
what are the monosaccharides?
fructose,glucose, galactose
two monosaccharide bound in a dehydration synthesis reaction
disaccharide
what are the dissacharide?
lactose, maltose, sucrose
long chains of (3+) monosaccharide (complex carbohydrate)
polysaccharide
animal storage form of polysaccharide
glycogen
plant storage form of sugar
starch
enzyme that breaks the carbohydrate into mono- and disaccharide
amylase
two type of amylase
salivary amylase and pancreatic amylase
where is pancreatic amylase release
duodenum after chyme exits the stomach into small intestine
monomers of lipids
glycerol and fatty acid
what are lipids composed of
fatty acid attached to glycerol backbone
the 3 types of lipids
monoglyceride
diglycerides
triglyceride
what type of fat solidify at room temp
saturated fat
what type of lipid stays in liquid form at room temp
unsaturated fat
what’s the difference between saturated fat and unsaturated fat
saturated fat-all carbon are are bonded to hydrogen
unsaturated fat- the carbon atoms at least have one double bond
what enzyme breaks up lipids
lipase
what are the two type of lipase
salivary lipase and pancreatic lipase
monomers of protein
amino acid
what kind of bond does amino acid have
peptide bond
what determine protein structure and function
sequence
how many different amino acid
20
9 are essential and 11 are nonessential (made by body)
protein digestion begin where
stomach
what does chief cells secrete
pepsinogen
what does pepsinogen do
break up peptide bonds into smaller polypeptides
what breaks up protein in small intestine
proteases and peptidases
lugol’s IKI test for what
starch
color change is an indication of presence (carbohydrate polysaccharide)
dark purple/black
benedict’s solution test for what?
glucose (monosaccharide)
color changed with heat
turned yellow
litmus cream
change in color indicated pH change due to fatty acid from lipid
turned pink
biuret’s reagent
color change indicated presence of peptide (protein)
became clear
HCl activate pepsinogen into pepsin to break down peptide bond
macromolecule that our body use for energy production
lipid, protein, and carbohydrate
purpose of 37 degree C
optimal temp for enzyme reaction/body temp. cause the molecules to move more quickly
enzyme for protein
stomach
chief cells release pepsinogen.
parietal cells convert pepsinogen into pepsin (active form)
intestine
protease from pancreas and brush border of small intestine
peptidase from pancreas and brush border of small intestine
what is pH
concentration of H+ ion in a solution
proton donors in a solution
acids
proton acceptor
base (donate OH)