Macro nutrients Flashcards
What are macro nutrients?
Macronutrients are large families of molecules that makes up the food we eat. and are required in relatively large amounts to maintain the health and funciton of the body. Macronutrients include carbohydrates, proteins, and fats.
What are carbohydrates?
Carbohydrates are macronutrients made up of long chains of smaller units called saccharides, or sugars and are composed of carbon, hydrogen, and oxygen arranged into chains of sugar molecules.
Depending on their structure, they can be classified as simple or complex.
Simple carbohydrate molecules (aka simple sugars) have a basic ring structure of carbons and hydrogens.
• One ring is called a monosaccharide (mono = one).
• Two rings joined is a disaccharide (di = two).
• A few rings joined are called oligosaccharides (oligo =
few).
As carbohydrates link together in more intricate structures (hence the term “complex carbohydrates”), they become glycogen, starches, and various types of
soluble and insoluble fibers. We often call these polysaccharides (poly = many).
In order for the body to use carbohydrates they need to first be broken down into simple sugars.
What is the difference between simple and complex carbohydrates?
Simple carbohydrates (simple sugars) contain one or two sugar molecules (monosaccharides and disaccharides, respectively), while complex carbohydrates are composed of a number of monosaccharide molecules (three or more) linked together
Name two monosaccharides as well as their sources
Glucose: Honey, syrup, root vegetables
fructose: honey, syrup, fruit
Name two disaccharides
Lactose: cow, sheep and goat’s milk,
Sucrose (common sugar): Mainly from Cane sugar and beet
Which enzyme is required to digest lactose?
Lactase
How is lactase related to lactose intolerance?
Lactase production declines as we age and so when people do not have enough lactase, they cannot properly digest lactase, which results in lactose intolerance
What are oligosaccharides?
Oligosaccharides are comprised of three to nine monosaccharide units linked together The two main oligosaccharides are fructo-oligosaccharides (FOS) and galacto-oligosaccharides (GOS).
What are the benefits of oligosaccharides?
Both fructo-oligosaccharides and galacto-oligosaccharides pass through the upper digestive system undigested and ferment when they reach the large intestine, exerting a prebiotic effect that promotes beneficial bacteria in the gut. However, this fermentation may cause flatulence and can be problematic for those with irritable bowel syndrome
Which plants are rich in oligosaccharides?
fructooligosaccharides: Jerusalem artichokes, alliums (leeks, onions, and garlic), asparagus, banana, burdock root, and chicory root
Galactooligosaccharides (GOS) are found in pulses such as lentils, chickpeas, and beans
name three different kinds of polysacharides and where each is found
starch: Vegetables such as corn, potatoes, beans
pectin: Mainly fruit, some vegetables, pectin in apples
used as a gelling agent
musolage: Found in demulcent herbs and plants like comfrey, slippery elm etc.
which macro nutrient is commonly used as a thickener or gelling agent?
pollysacharides
Which macro nutrient is commonly found in immuno modulating herbs?
pollysacharides
Protein are broken down into …
Amino Acids
Carbohydrates are broken down into…
Sacherides like glucose
Fats are broken down into …
fatty acids
What are the macros ratios of a balanced meal?
30% Protein
40 % Carbs
30% Fat
What happens when we change the macros ratio?
It changes the physiological outcomes
Why is it important to understand macros?
To discover the energy intake as well as the optimal ratio of protein, carbohydrate, and fat that will help you (or your clients) look, operate, perform, and recover as well as possible.
Why is only looking at macros not suffienct when planning a diet?
It doesn’t tell us exactly:
- what types of macronutrient molecules are in it; nor
- the quality of that diet.
What is an energy balance?
energy balance measures the amount of energy in vs the amount of energy out.
Why should we consider the energy balance when planning meals?
Energy balance strongly affects our health, body composition,and performance.
How does energy balance affect weight?
More in than out -weight gain
More out than in -weight loss
Same in as out -Weight stays the same
What does the abreviation CICO stand for
Calories in/Caloreis out
What is the primary criticism of CICO?
These critics say it doesn’t account for hormone imbalances, insulin resistance, polycystic ovary syndrome (PCOS), and other health problems that affect metabolism. They often claim certain diets and foods provide a “metabolic advantage,” helping you lose weight without worrying about CICO.
Which variable can change body weight independend from energy balance?
water
What is meant by Body stores
Body stores refers to all the tissues available for breakdown, such as fat, muscle, organ, and bone
What is the energy balance equation?
[Energy in] – [Energy out] = Changes in body stores
What regulates the internal and environmental factor of energy balance?
The brain
What factors influence “energy in”?
Appetite : influenced by hormones that regulate hunger
and satiety
Food Consumed: influenced by Palitibillity, Energy
density, Socio-Economic status,
Education and culture
Calories absorbed: influenced by Macro nutrient intake,
age, food prep, microbiome, health
and energy status
Psycological factors: Stress, mindset, self-control, self
esteem, sleep quality
What factors influence “energy out”?
Energy burned at rest: influence by age, hormonal status, dieting history, genetic factors, health status, sleep
quality
Energy burned during exercise: influenced by abillity, type, frequency, duration, intensity, environment, sleep
quality and hormonal status
Energy burned by non exercise activity: influenced by occupation, leisure activities, hormonal status, health
status, energy levels, genetic factors
Energy burned by metabolizing food: influenced by macronutrient makeup and by how processed teh food
is.
Why is “eat less, move more” a big oversimplification?
Because it does not account for the factors, such as hormones and metabolism, that influence both intake and output
What are some of the problems with estimating the “exact” amount of calories in?
We don’t absorb all of the calories we consume. And
Calorie information on Food lables are not always correct and can be off by as much as 20%
Calorie information in Restuarants can be of by as much as 100 to 300%
absorption rates vary across food types. (Example: We absorb more calories than estimated from fiber-rich foods, and less calories than estimated from nuts and seeds.)
We all absorb calories uniquely based on our individual gut bacteria.
Food prep, such as Cooking, blending, or chopping food generally makes more calories available for absorption than may appear on a nutrition label.
what is the problem with using calory calculators to calculate calories out?
They provide an output based on averages, and can be off by as much as 20-30 percent in normal, young, healthy people. They may vary even more in older, clinical, or obese populations.
What are two alternative approaches to calorie counting?
hand portions and intuitive approaches
What are some common hormonal issues that impact energy balance and weight gain?
Menopause, Diabetes, Hypothyrodism, insulin resitance, Polycistic Ovary syndrome
Are results diet dependent or are they behavior dependent?
Maintaining a healthy body (including a healthy body weight) is about developing consistent, sustainable daily habits that help you positively impact “energy in” and “energy out.”
What is body composition?
the ratio of lean muscle vs body fat
What influences body composition?
Body composition is influenced by factors such as our:
• hormones (such as testosterone, estrogen, or growth
hormone);
• exercise (e.g., how often, how intensely, how long,
what type of exercise,and so on);
• age;
• medication use;
• genetic predisposition; ,
• macronutrient intake (especially protein).
How does energy balance affect physiological function, performance and recovery?
• Hormonal health and balance can be disrupted by
either too much or too little energy, especially over a
long period of time.
• If we don’t eat enough energy, our physical and mental
performance may decline.
• People recovering from surgery or major injuries (such
as broken bones) may need more energy than healthy
people, as energy is going to tissue repair
and rebuilding.
The body regulates the energy balance via the hypothalamus and a complex network of feedback loops: What happens when energy intake is consistently too low?
• If energy intake is consistently too low for a person’s needs, that person may eventually start to:
- struggle with hunger, appetite, and food cravings.
- They may also feel cold or have sluggish digestion. —–
- Their bodies are slowing metabolic rate and increasing
- the desire to eat, in order to compensate.
The body regulates the energy balance via the hypothalamus and a complex network of feedback loops: What happens when energy intake is consistently too high?
• If energy intake is consistently too high for a person’s needs, that person will likely store the extra energy as fat. However, depending on the person, excess energy can also be used for recovery, repair, and growth (for instance, in building muscle); or thrown off as heat.
What is the difference between Calories and Joules?
Calories are a measure of heat, while joules (J) are a measure of work.
How much energy is released by each macronutrient when burned in a lab, as measured by a bomb calorimeter?
- 1 gram of fat = 9.44 kcal
- 1 gram of starch = 4.18 kcal
- 1 gram of sucrose or glucose = 3.94 kcal
- 1 gram of protein = 5.65 kcal
- 1 gram of alcohol = 7.09 kcal
what are four important considerations when planning a macros diet?
weight/composition goals
physical activity
recovery
metabolic health
how many calories in one pound of body weight?
3500
What are predicitive equations?
equations that attempt to predict a client’s future energy requirements?
What is the margin of error when predicting energy requirements?
When being very precise there is still a 5% margin of error.
What are the 5 main functions of protein in the body?
production and maintanance of structural proteins: colagen, elastin, kerotin, myosin, actin that maintain the strength and integrity of muscles, connective tissues (ligaments and tendons), hair, skin, and nails
Production of enzymes and hormones: All of the enzymes, which are compounds that catalyze chemical reactions in the body, are made from protein. In addition, the hormones involved in blood sugar regulation (insulin and glucagon), well as the thyroid hormones are synthesized from proteins.
Production of transport proteins: Certain proteins are used by the body to carryvarious substances to body tissues. These transport proteins include hemoglobin (carries oxygen), transferrin (carries iron), ceruloplasmin (carries copper), retinol-binding protein (carries vitamin A), albumin and transthyretin (both carry other proteins).
Lipoproteins participate in the transportation
of fat and cholesterol.
Production of immune cells and antibodies: Antibodies, such as immunoglobin IgA, IgC, IgE, which are proteins, play an important role in the immune system by attaching to antigens (viruses, bacteria, or other foreign invaders), thereby inactivating the antigens and making them more visible to the immune cells (called macrophages) that destroy antigens.
Water regulation: Maintenance of proper fluid balance: Proteins participate in the maintenance of osmotic pressure, which controls the amount of water that is found inside of cells.
What is protein turnover?
The ongoing process of breaking down and building
up proteins in the body
What are amino acids made from?
An amino acid is so named because it has an amino, or nitrogen group (with the chemical formula NH2), on one end of its molecule, and an acidic carboxyl group (COOH) on the other. Amino acids also have what is called an “R group”, or side chain, which can
vary from amino acid to amino acid. Branched-chain amino acids (BCAAs) are so named because they have a branched side chain.
What is protein synthesis?
Protein synthesis is the building of new proteins. Following instructions from our DNA, proteins are built from amino acids into peptides; from peptides into
polypeptides, and from there into increasingly complicated structures, some of which can be incredibly intricate.
This complex sequence, structure and shape determines what a specific protein does, much like a puzzle piece. For instance, one type of protein might become an antibody; another might become a neurotransmitter.
what is protein breakdown?
the opposite of protein synthesis. Breaking proteing down to amino acids
protein -polypeptides -peptides -amino acids
how much nitrogen does protein contain?
16% by weight
How many proteinogenic amino acids are there in the human body?
20
where do amino acids get their names from?
From the foods they were first discovered in
What are the three main catagories of amino acids acording to their role?
Non-essential amino acids: We can make these amino acids in our body, so we don’t need to eat them in our diets (although, of course, we can).
Essential amino acids: We need to get these essential amino acids (aka EAAs) from food. We can’t make these ourselves.
Conditionally essential amino acids: We can make these amino acids ourselves, but not always effectively, particularly when we’re under physical stress (such as from hard athletic training, or when we’re sick). Having
extras around helps us rebuild tissues when those tissues are damaged.
Name the 9 essential amino acids?
Essential amino acids (EAAs): Lysine Methionine Phenylalanine Threonine Tryptophan Histidine1
Branched chain amino acids (BCAAs)
Isoleucine
Leucine
Valine
Name the 4 conditional amino acids?
Arginine
Cysteine
Glutamine
Tyrosine
Name the 7 non essential amino acids?
Alanine Asparagine Aspartic acid Glutamic acid Glycine Proline Serine
What are stereoisomers?
Many molecules, such as amino acids as well as sugars, exist as mirror images of each other, like right and left hands. These molecular mirror images are called stereoisomers.To differentiate between these mirror images, scientists use an L (or a minussign) or D (or a plus sign).
• L stands for laevus (left in Latin).
• D stands for dexter (right in Latin).
Which amino acid isomer is used for nutrition?
The L isomer.
What is an enzyme?
Proteins that facilitate chemical reactions (e.g.,
breaking down molecules)
What is a Chiral Center?
The chemical “middle” of a mirror-image molecule;
an atom that’s bonded to four different chemical
components
What is deamination and why is it nescesary?
The removal of an amino group (nitrogen containing group) from an amino acid molecule in order for it to be metabolized.
What is the toxic byproduct of deamination?
Amonia (NH4)
How does the body remove amonia?
the ornithine or urea cycle, to remove ammonia by converting it into urea ((NH2)2CO). We then excrete the urea in our urine
What is another name for the urea cycle?
ornithine cycle
What is GLUCONEOGENESIS?
The process of creating glucose from noncarbohydrate sources
What is the difference between glucogenic and ketogenic amino acids?
glucogenic amino acids are transformed into glucose and ketogenic amino acids are transformed into ketones
What are ketone bodies?
Compounds made in the liver from fatty acids (and sometimes protein) when there is not enough carbohydrate for energy.
what are peptides?
A peptide is made of two or more amino acids bonded together
what is ATP?
Our body’s energy currency. Abreviation for adenosine
triphosphate.
Concerning amino acids, what is meant by Primary Structure?
The sequence of amino acids in a peptide
Concerning amino acids, what is meant by Secondary Structure?
Formation of protein helixes or sheets from peptides
What are polypeptides?
Chains of amino acids longer than 25 amino acids; also
known as proteins
What are antibodies?
Immune signalling protein that combats a specific
pathogen such as a virus
What are neurotransmitters?
Nervous system signalling chemical
What is Nitrogen balance?
Ratio between nitrogen consumed and excreted;
a measure of protein adequacy in the body
What is TRANSAMINATION?
Transfer of an amino group from one molecule to another, particularly from an amino acid to a keto acid
What is insulin?
A hormone that helps transport nutrients, particularly glucose, into cells
What is IGF-1?
insulin-like growth factor 1, a hormone similar to insulin that has anabolic effects and promotes growth
What is cell signalling?
Cells’ communication internally, or externally with other cells and their environment
What is translation?
The decoding of genetic information from RNA to protein
What is an isomer?
Molecules that have the same molecular formula, but
different arrangements of the atoms.
What are stereoisomers?
Molecules that are mirror images of eachother
Concerning amino acids, what is meant by Tertiary Structure?
Three-dimensional shape of a structure built from complex peptides (i.e. polypeptides)
Concerning amino acids, what is meant by Quartenary Structure?
Arrangement of many subunits within a large
protein
What are conjucate proteins?
Proteins with non-protein parts
Name three different conjucate proteins?
glycoproteins (carbohydrates + protein),
lipoproteins (fat or cholesterol + protein) and phosphoproteins (phosphate+protein).
What is immunoglobulin?
Antibody glycoproteins in the
immune system such as IgA, IgG, IgE
What is C-reactive protein (CRP)?
A glycoprotein associated with low-level chronic
inflammation and insulin resistance?
What is low density lipo protein (LDL)?
One of five major lipoprotein groups that transport
triglycerides, fatty acids, phospholipids, and cholesterol to the body; sometimes refered to as “bad cholesterol”
Name 4 different kinds of glycoproteins?
Immune sytem: Immunoglobulin like IgA, IgG, IgE
C-reactive protein (CRP) is a well known glycoprotein associated with lowlevel inflammation and insulin resistance.
Hormone stimulating: Thyroid stimulating hormone (TSH), follicle stimulating hormone (FSH) and luteinizing hormone (LH) are hormones that are glycoproteins.
Cholesterol: Low-density lipoprotein (LDL) and high-density lipoprotein (HDL) are themost well-known lipoproteins that allow lipids to move around in a bodythat’s mostly water.
What is High density lipoprotein? (HDL)
One of five major lipoprotein groups that transports
cholesterol to the liver as a part of reverse cholesterol
transport; sometimes referred to as “good cholesterol”
What is Collagen?
Collagen is made up mostly of a repeating primary amino acid sequence of glycine-proline-4-hydroxyproline. This creates a special type of tightly twisted and packed helix structure, which makes collagen very strong. In fact, collagen has more tensile strength than steel wire of comparable size.
Collagen is found in connective tissue like tendons, cartilage, the non-mineral component of bone, and pretty much anywhere you need cells to stick together.
What can you take 1 hour before exercise to help synthesize Collagen in muscle tendons and ligaments?
Gelatine and 48mg of vitamin C
What improves the conversion of proline to hydroxyproline?
Vitamin C
Which amino acids produce creatine?
glycine and arginine
What is creatine?
An amino acid that is a component of phosphocreatine, a compound needed to quickly make more ATP under
intense energy demand.
What is creatine stored as?
Phosphocreatine
What is coline?
An essential nutrient involved in synthesizing and
transporting lipids, as well as methyl group metabolism
Choline is made from serine and is essential for neurotransmitters (such as acetylcholine), cell membrane components (phosphocholine), the myelin sheath, and even epigenetic modifications.
Describe the process by which protein is digested and absorbed
Stomach: Protein digestion really gets started in the acidic environment of the stomach.Hydrochloric acid and the enzyme pepsin (the active form of pepsinogen) begin to break down proteins. Then, the resulting
peptides and single amino acids are passed along to the small intestine.
small intestine: Once in the small intestine, enzymes from the pancreas (such as trypsin, chymotrypsin, arboxypeptidases, aminopeptidases, and collagenase) further break down proteins. Peptides must be short — fewer than 4 amino acids long — to be absorbed. The cells that line the small intestine (enterocytes) break down peptides even further, so that nearly all former proteins enter the bloodstream as single amino acids.
The liver: Most amino acids go to the liver via the portal vein. For every 100 g of amino acids taken in, about 80 g will go to the liver. Of that:
- About 20 g will be used for protein synthesis in the liver.
- About 60 g will be broken down, or catabolized, in the liver.
- About 20 g will be exported by the liver into systemic circulation.
What is protein denaturation?
Denaturation is the change in the threedimensional structure of the protein. Scientists sometimes call this “unfolding” of the protein, becauses key bonds that keep it folded are broken (usually hydrogen and
sulfide bonds).
protein gets denatured in the stomachs acid which has a ph of 2, so that it is easier for the pepsin to break it down.
Explain how the liver metabolizes and uses protein
For every 100g of amino acids consumed, 80% or 80g will go to the liver, only 20% is used for protein synthesis.
- About 20 g will be used for protein synthesis in the liver.
- About 60 g will be broken down, or catabolized, in the liver.
- About 20 g will be exported by the liver into systemic circulation.
Of the 20 g of protein synthesized in the liver:
• 14 g will remain in the liver
• 6 g will be exported to the plasma in the form of
plasma proteins (albumin, globulins, lipoproteins, etc.),
glutathione, carnitine, creatine, and other compounds.
Within the liver, proteins can be turned into enzymes
and nitrogen-containing chemicals for the liver to use.
Of the 60 g of proteins broken down in the liver:
The liver will remove the amino group (NH2) from about 60 g of protein to produce energy, glucose, ketone bodies, or fatty acids. Exactly what happens
here will depend on factors like:
• which amino acid is being broken down (e.g., some amino acids can only be used to make glucose);
• what other nutrients are available;
• how much energy is available (i.e., are we fasted or fed?); and
• what our body needs
of the 20g of Proteins exported from the liver:
Whatever the liver doesn’t use, it sends out to the plasma amino acid pool(i.e., our body’s stores of amino acids) and other cells of the body. Our body’s
cells can then extract amino acids from the plasma for various tasks, such as
synthesizing:
• muscle proteins
• skeletal and connective tissues (e.g., bones, tendons,
ligaments, cartilage)
• neurotransmitters
• enzymes
• immune system chemicals (e.g., immunoglobulins,
antibodies, cytokines)
• transport proteins (e.g., carrier proteins, lipoproteins)
Where new proteins end up depends on:
• genetic signalling;
• which amino acids are involved; and
• how much energy is available in the body.
What is the plasma amino acid pool?
The body’s stores of
available amino acids
circulating in blood
What are some of the consequences of protein deficiency?
Protein deficiency can lead to anemia,physical weakness, edema (water retention and swelling), vascular dysfunction,
and impaired immunity
Why do we need a constant supply of protein?
Because protein turnover is constantly occuring and because…
Proteins are crucial for nearly every aspect of cell function (as enzymes, transporters, and hormones)
and they are the major structural component of all cells in the body.
There are several essential and conditionally essential amino acids that we can’t make ourselves.
We lose some amino acids in various metabolic processes.
When do our protein requirements go up or increase?
• we’re training hard frequently (e.g., as athletes) or have
a heavy physical job;
• we want to gain lean mass and/or strength;
• we’re injured or sick, or are recovering from surgery;
• we’re older (because we digest protein less well, so
we need more to meet requirements);
• we’re losing protein for some other reason (e.g., chronic physical stress).
What are some coditions that require a lower protein intake?
- kidney disease
- certain metabolic diseases (e.g., PKU)
- liver disease
- problems with gastric emptying
- homocystinuria
What is PKU or PHENYLKETONURIA ?
An inherited metabolic disease that causes a
build-up of the amino acid phenylalanine
What is HOMOCYSTINURIA?
An inherited metabolic disease that causes a
buildup of homocysteine and its metabolites