Four characteristics of protein
large, complex molecules
found in cells of all living things
organic molecule
composed of long chain of amino acids (20)
Amino acid structure
each have the same basic structure
carbon atom (alpha carbon) with:
amino group (NH2)
Carboxylic acid (COOH)
H atom
Side chain (R group)
How are amino acids linked together
peptide bonds
Dipeptide
2 amino acids
Tripeptide
3 amino acids
Polypeptide
more than 3 amino acids
protein
70 or more amino acids
What is protein denaturation
proteins uncoil and lose their shape
protein function is lost (shape=function)
what causes protein denaturation
temperature
pH
enzymes
alcohol
Essential amino acids
cannot be produced in sufficient quantities to meet physiological needs
must be obtained from food
total of 9 essential amino acids
support normal body growth-maintenance repair
Non-essential amino acids
can be synthesized by the body in sufficient quantities
Total of 11 non-essential amino acids
Conditionally essential amino acids
non-essential amino acid become essential in the diet
phylketonuria (PKU): tryosine becomes a conditionally essential amino acid
Transamination
transfer amine group (NH2) from essential amino acid to a different acid group and R group
used to make nonessential amino acids
How do we determine protein quality ?
determine how well a protein from food matches the body’s requirements and, therefore, how useful the protein is for our body
amino acid composition
protein digestibility
Amino acid composition: complete proteins
contain all 9 essential amino acids
adequate amounts for growth and maintenance of body tissue
all animal products are complete proteins except gelatin
Amino acid composition: incomplete proteins
lack one or more of the 9 essential amino acids
cannot support either maintenance or growth of body tissues
most of the plant proteins are incomplete
amino acid composition: partially complete protein
contains all 9 essential amino acids, but one or more is limited
limiting amino acid
limits the amount that all amino acids can be used to produce protein
can support maintenance but not growth of tissues
Limiting amino acids
an essential amino acid supplied in less than the amount needed to support protein synthesis
Amino acid composition: complementary protein
combining two incomplete protein sources
amino acids in one food makeup for those lacking in the other food
vegetarian must mix protein-rich plant foods to get amino acid balance, ex.- rice and beans
Protein digestibility
digestibility of a protein varies between foods
amino acids from animal sources are digested more easily
animal proteins: 90-99% digested and absorbed
plant proteins: 70-90% digested and absorbed
Soy and legumes: >90% digested and absorbed
protein quality: reference proteins
a standard against which to measure the quality of other proteins
compares amino acid composition with essential amino acid requirements of preschool-age children
Reference proteins:
highest protein quality and digestibility
sustain maximal growth rates
Protein quality: biological value (BV) (high and low)
nitrogen is retained/ absorbed
high biological value
more nitrogen is retained/ absorbed
generally animal proteins (Ex. eggs)
Low biological value
less nitrogen is retained/ absorbed (more is exerted)
generally plant proteins
Protein function
growth and maintenance
body processes
energy
fluid and electrolyte balance
Protein function: growth and maintenance
involved whenever body is growing, repairing, or replacing tissues
form the building blocks of muscles, blood, and skin
collagen is a structural protein that makes scars, tendons, ligaments, foundations of bones and teeth
replace dead cells → avg. life span of skin cell 30 days and cells of GI tract are replaced every few days
Protein function: body processes
enzymes→ digestion, DNA synthesis
hormones→ messenger molecules that tell something to happen (insulin, glucagon)
antibodies→ large proteins that are produced by your immune system to fight viruses
transport proteins→ brining important substances in and out of your cells, lipoproteins
Protein function: energy
they are sacrificed to provide energy and glucose during times of starvation or insufficient carb intake
tissue proteins are broken down to make amino acids available for energy or glucose production- known as GLUCONEOGENESIS
protein can maintain blood glucose levels, but at the expense of losing lean body tissue
4 kcal per gram
Protein function: fluid and electrolyte balance
protein attracts water, protein in the blood creates an osmotic pressure and keeps fluid from seeping out into extracellular space
during critical illness or protein malnutrition, plasma proteins can leak out of the blood vessels into the spaces between the cells
due to protein attracting water, fluid can accumulate and cause swelling (edema)
also accepts and releases hydrogen ions, thus acting as buffers in the blood- maintaining acid- base balance - pH balance
failure of any part of the fluid balance system causes edema (protein deficiency)
Sickle cell disease
two of hemoglobin’s four polypeptide chains have a normal sequence of amino acids, but the other chains do not
changes shape of hemoglobin
loses its ability to carry oxygen effectively
Protein digestion: where?
stomach: <10% of protein is digested
small intestine: >90% of protein is digested
protein digestion: how?
stomach: pepsin and HCl (acid)
small intestine: chymotrypsin and trypsin
Protein digestion
protein foods denatured by stomach acids (HCl)
enzymes from stomach, pancreas, and small intestine digest proteins
free amino acids are formed
Protein absorption
amino acids absorbed by villi
delivered to cells via blood
amino acids rebuilt as needed into new protein in the cells
Protein balance
balance of protein output and protein intake
nitrogen balance: the amount of nitrogen consumed compared to the amount of excreted in a given time period
equilibrium or nitrogen balance: intake = output
positive nitrogen balance: intake > output
Negative nitrogen balance: intake < output
protein balance: positive nitrogen balance
growth (infant and children)
pregnancy and lactation
recovery from illness
athletes
protein balance: negative nitrogen balance
when muscles or other protein tissue breaks down and is lost (illness
inadequate protein intake (fasting)
inadequate energy intake
deficiency in essential amino acids
RDA protein requirement
0.8 grams per kg healthy body weight
AMDR protein requirement
10-35% total kcals
Kwashiorkor
protein malnutrition, disease resulting from low protein intake
occurs often when child taken off breast milk and fed starchy liquid
usually develops rapidly
will cause symptoms of EDEMA→ swollen belly
Marasmus
protein-energy malnutrition
extreme starvation; occurs during famine, especially in infants
resulting from chronic underfeeding, both inadequate energy as well as protein
symptoms:
weakening of the muscles
stunted brain development and learning
depressed metabolism
stunted physical growth
growth ceases
death
Excessive protein intake
often associated with obesity
high cholesterol and heart disease
contribution to bone loss
kidney disease
Triglycerides (TG)
fats and oils
90-95% lipids in food
phospholipids
2-3% lipids in food
sterols
2-7% lipids in food
types of lipids
triglycerides
phospholipids
sterols
Triglycerides basic structure
glycerol backbone
3 fatty acids
Fatty acid structure
C-H chain
COOH (acid group)
CH3 (methyl group)
fatty acid differences
length of carbon chain
number of double bonds
location of double bonds
Fatty acid differences: length of carbon chain
most contain even number of carbons- up to 24
long chain fatty acids
12-24 carbons
meats, seafood, vegetable oils
most common in diet
Medium- chain fatty acids
6-10 carbons
Short-chain fatty acids
less than 6 carbons
medium and short primarily in dairy products
Fatty acids differences: number of double bonds→ saturated fatty acids
carbon is “saturated” with hydrogens
no double bond
solid at room temp
primarily from animal sources
some plant sources
associated with health risks
Fatty acids differences: number of double bonds→ unsaturated fatty acids
carbon lacks hydrogen atoms
at least one double bond between carbons
point of unsaturation
liquid at room temperature (oils)
primarily from plant sources
double bonds are “reactive”
Monounsaturated fatty acids
one double bond
“cis” formation
sources: olive, peanut, canola oils
mediterranean diet
usually omega-9 group
only double bond 9 carbons from methyl end
oleic acid (18 carbons, omega 9)
polyunsaturated fatty acids
two or more double bonds
“cis” formation
two basic forms
Linoleic acid→ Omega 6
Linolenic acid→ Omega 3
polyunsaturated fatty acid: omega-6
omega 6= linoleic acid
18 carbon chain
two double bonds
essential in our diet
sources: vegetable oils, nuts, poultry
polyunsaturated fatty acid: omega-3
omega 3= linolenic acid
18 carbon chain
three double bonds
EPA (food form, essential)
may lower cholesterol and decrease risk of heart disease, HTN, cancer, arthritis
reduce inflammation, blood clotting, plasma TG
sources: vegetable oils, nuts, poultry
Fatty acids differences: location of double bonds
identified by closest double bond to methyl end of the carbon chain
characteristics of fats
lipids that are solid at room temperature
most saturated animal fats
characteristics of oils
lipids that are liquid at room temperature
most unsaturated plant fats
cocoa butter, palm oil, palm kernel oil, coconut oil have higher saturated fat content
characteristics of fats and oils: degree of unsaturated affects stability
spoiled (rancid) when exposed to oxygen
polyunsaturated fats spoil most readily- double bonds are unstable
saturated fats least likely to turn rancid
characteristics of fats and oils: manufacturers protect fat-containing products
air-tight containers, protected from light, refrigerated
antioxidant additives
hydrogenation-cis→ trans fatty acids
hydrogenation
the process of adding hydrogen to double bonds
converts double bonds → single bonds
may be partially or fully hydrogenated
makes oils more solid and more saturated
improves shelf life
increases risk of cardiovascular disease
hydrogenation pros
decrease food spoilage
can use oils as solid fats
better cooking qualities
hydrogenation cons
increase saturation of fats
produce trans fats
“unnatural” reaction
triglycerides and condensation reaction
few fatty acids occur free in foods or in the body
most are incorporated into triglycerides
most contain a mixture of more than one type of fatty acid
formed via condensation reactions
H from glycerol + OH from fatty acid → triglyceride + H2O
Diglycerides
two fatty acids +glycerol
generated during digestion of triglycerides
added to foods as an emulsifier
monoglycerides
one fatty acid +glycerol
also generated during digestion and used as emulsifier in foods
Phospholipid structure
glycerol backbone
two fatty acids
phosphorus-containing side group
polar head and nonpolar tail
phospholipids manufactures in our bodies
not essential in our diet
phospholipid functions
major component of cell membranes
important transport forms of lipids in the blood
best known phospholipid
lecithin
phospholipid supplements not needed
can cause GI distress, loss of appetite
liver makes phospholipids for the body
phospholipid food sources
eggs (yolks only), liver, soybean, wheat germ, peanuts
sterol structure
multi-ring structure
most well known sterol
cholesterol
sterols are in foods derived from ____
plants/ animals
plant sterols interfere with cholesterol absorption and lower blood cholesterol levels
cholesterol is in foods derived from ____
animals only
body can make all the cholesterol we need; no dietary requirement
associated with heart disease
Sterol function
bile acids
sex hormones (testosterone, androgen, estrogen)
vitamin D
adrenal hormones (cortisol, cortisone, aldosterone)
cholesterol is structural component of cell membranes
more than 90% of all body’s cholesterol is found in cells
Cholesterol sources
endogenous (made by the liver)→ up to 1500 mg/day
exogenous (from animal food)→ 200-300 mg/day
the role of lipids in diet
energy source
essential fatty acids
carrier of fat-soluble vitamins
palatability
the role of lipids in the body
energy reserve
insulates to prevent loss of body heat
regulates body functions
cell membrane structure and activity
precursor of hormone-like substances (eicosanoids)
Fat absorption: glycerol and short/medium-chain fatty acids
absorbed into blood
go directly to liver
made into VLDL (form of lipoprotein)
Fat absorption: monoglycerides and long-chain fatty acids
form micelles in the small intestine
absorbed into small intestinal cells
repackaged into new TG
packed into chylomicrons
chylomicrons enter lymph
how to differentiate Saturated and unsaturated fatty acids
Saturated will be saturated with hydrogen
unsaturated will have double bonds
Lipoproteins
clusters of lipids, proteins, cholesterol, and triglycerides that act as “transport vehicles” for fats
Four different types of lipids in order from largest and least dense to smallest and most dense
Chylomicrons
Very low density lipoproteins (VLDL)
Low density lipoproteins (LDL)
High density Lipoproteins (HDL)
Chylomicrons
transport dietary lipids (mostly triglycerides) from the small intestine to the rest of the body (via lymph system)
Cells remove triglycerides from chylomicrons as they pass by, so they get smaller and smaller
once TG are depleted, only few remnants of protein, cholesterol, and phospholipids remain
liver removes chylomicron remnants from blood
VLDL
lipids made in the liver and collected from chylomicron remnants are packaged with protein → VLDL
VLDL delivers cholesterol and fatty acids to needy cells
Density increases as fat leaved VLDL
VLDL becomes LDL
LDL
high in cholesterol
circulates through the body delivering triglycerides, cholesterol, and phospholipids to cells
liver removes LDL from circulation
controls blood cholesterol concentrations
HDL
liver makes HDL
removes cholesterol from cells and carries it back to liver for cycling or disposal
can pick up cholesterol from plaques
good cholesterol
HDL
lowers risk of heart disease
anti-inflammatory properties
bad cholesterol
LDL
contributes to plaques when cholesterol “falls off” the LDL and is deposited on artery walls
plaques narrow arteries → increases blood pressure → increases risk of blood clots/ heart attacks
disease associated with lipids
blood pressure
cardiovascular disease
obesity
cancer
diabetes
diets high in saturated fats
decrease removal of LDLs from the blood
increase blood cholesterol levels
formation of plaques that can block arteries
diets high in trans fats
raise LDL as much as saturated fat
abundant in hydrogenated vegetable oils
How to lower LDL-C to reduce risk of CVD
MUFA>PUFA>SFA
reduce cholesterol intake
eliminate trans fats
increase omega-3
increase fiber
physical activity
other lifestyle changes:
normal blood glucose levels
eat throughout day
maintain active lifestyle
maintain healthy body weight
decrease salt intake
How to increase HDL-C
exercise
increase fiber
increase fruit/vegetable consumption
smoking cessation
Mediterranean diet
high in omega-3/omega-6
high in fiber
high in poly/monounsaturated fats
Food sources of fat: visible fats
visible fats
added to foods
Food sources of fat: invisible fats
Invisible fats
hidden within foods
occur naturally or added during processing
Food sources of fat: beneficial fats
omega-3 fatty acids may be low in current diet
add more: fish, walnuts, soy, canola, flaxseed
Food sources of fat: fat replacers
used to lower fat content of foods
found in chips, cakes, cookies
may cause GI side effects in large amounts
example: olestra (olean)