Nutrients, Enzymes, and Digestive System Flashcards

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1
Q

Carbohydrates Basics

A
  • primary source of energy for cells (fast source of energy)
  • structural material of plant cell walls (cellulose)
  • potatoes (complex carb), bread (simple carb), corn, rice, fruit (simple sugar)
  • athletes consume large amounts of carbohydrates the day before an event called pasta loading
  • will be stored as fat if consumed in excess
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2
Q

Polymer

A

A molecule consisting of three or more subunits

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3
Q

Carbohydrate Composition

A
  • either a singular unit or a polymer
  • single units are made of carbon, hydrogen, and oxygen in a 1:2:1 ratio
  • names end in ‘ose’
  • ring like structures
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4
Q

Monosaccharides

A
  • contains a single sugar unit
  • glucose, fructose, galactose (all C₆H₁₂O₆)
  • hexose (6 carbons), pentose (5 carbons)
  • deoxyribose, ribose: genetic sugars
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5
Q

Isomer

A

Groups of chemicals that have the same chemical but differ in their arrangement of atoms

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6
Q

Dissacharides

A
  • combination of two monosaccharides
  • sucrose (glucose and fructose)
  • maltose (two glucose)
  • lactose (glucose and galactose)
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7
Q

Dehydration Synthesis

A

Formation of a large molecule through the removal of water from two smaller molecules

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8
Q

Hydrolysis

A

The splitting of a large molecule into two smaller molecules through the addition of water

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9
Q

Polysaccharides

A
  • formed from the union of many monosaccharides
  • starch (multiple glucose units): energy storage for plants
  • glycogen (multiple glucose units): energy storage (muscle and liver) for animals
  • cellulose (multiple glucose units): plant cell walls, forms sheets held by hydroxyl groups
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10
Q

Benedict’s Test

A
  • detects reducing sugars (monosaccharides and some disaccharides)
  • ranges from blue (none) to orange/red (lots) depeding on the concentration of reducing sugars
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11
Q

Starch Test (Iodine)

A
  • detects complex carbohydrates
  • iodine turns blue-black in the presence of complex carbohydrates
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12
Q

Lipids Basics

A
  • energy storage compounds
  • structural componenent of cell membranes
  • are non-polar (can’t dissolve in water)
  • contain twice the amount of energy as carbohydrates but are hard to break down
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13
Q

Lipids Composition

A
  • made of glycerol (multiple glucose units, always the same) and fatty acids (carbon chain, will differ)
  • carbon, hydrogen, and oxygen
  • forms by dehydration synthesis
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14
Q

Triglycerides

A
  • three fatty acids
  • fat: triglyceride that’s solid in room tempurature, animal
  • oil: triglyceride that’s liquid in room tempurature, plant
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15
Q

Monoglycerides and Diglycerides

A
  • one (mono), two (di) fatty acids
  • forms when tryglycerides are exposed to heat, digestive enzymes, or are formed naturally in certain oils
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16
Q

Saturated Fat

A
  • only single bonds between hydrogen and carbon atoms in the carbon group
  • will hold as many hydrogen atoms as the molecule can hold
  • solid at room tempurature
  • hard to digest
  • increases risk of heart failure and clogging of arteries
  • comes from animal products
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17
Q

Unsaturated Fat

A
  • one or more double bond between hydrogen and carbon atoms in the carbon group
  • will be able to hold more hydrogen atoms
  • liquid at room tempurate
  • easier to break down
  • comes from plant products
  • one double bond: monounsaturated
  • two or more double bonds: polyunsaturated
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18
Q

Phospholipids

A
  • phosphate group bonded to glycerols
  • has a polar and non-polar end
  • forms the cell membrane
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19
Q

Waxes

A

Long-chain fatty acids bonded to long-chain alchohols or carbon rings

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20
Q

Translucence Test

A
  • lipids will cause paper to become translucent
  • lipids will fill in the gaps within the fibres paper therefore allowing light pass through
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21
Q

Sudan IV Test

A

Lipids dissolve in the Sudan IV turning it from black to pink or red

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22
Q

Protein Basics

A
  • forms the structural components of a cell
  • assists the immune system
  • large role in muscle development
  • enzymes
  • can be used for energy
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23
Q

Protein Composition

A
  • made of amino acids
  • carbon, hydrogen, oxygen, nitrogen
  • dehydration synthesis between two animo acids form a peptide bond
  • polypeptides are made of three or more amino acids
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24
Q

Amino Acids

A
  • animo group (NH₂)
  • R group (varies on the amino acid)
  • carboxyl group (COOH)
  • 20 different types
  • proteins with all 20 types are called complete
  • proteins with without all types are called incomplete
  • the body can create all amino acids but 8 (essential amino acids) which has to be ingested to prevent protein deficiency and disease
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25
Q

Protein Structures

A
  • primary structure: unique sequence of amino acids
  • secondary structure: hydrogen bonding between amino acids causes coils and sheets
  • tertiary structure: interactions between R groups of amino acids causes more folding
  • quaternary structure: clustering of multiple tertiary polypeptides
26
Q

Denaturation

A
  • changes in configuration of a protein (shape, physical properties, biological activity)
  • caused by excess heat, radiation, or change in pH
  • protein will turn to normal once factors have been removed
27
Q

Coagulation

A

Permanent change in the protein’s shape

28
Q

Buiret Test

A

Protein’s turn the buiret reagent from blue to pink (little) to purple (lots)

29
Q

Nucleic Acid

A
  • nucleotide
  • made of carbon, hydrogen, oxygen, nitrogen, and phosphorous
  • form the genetic material of cells
  • make up ATP energy molecules
30
Q

Enzymes

A
  • proteins catalysts that reduce the activication energy needed on a chemical reaction
  • binds with substrates on the active site to form enzyme-substrate complexes
31
Q

Cofactors

A
  • inorganic molecules that assist enzymes to bind to substrate molecules
  • minerals such as iron, zinc, potassium
32
Q

Coenzymes

A
  • organic molecules that assist enzymes to bind to substrate molecules
  • vitamins
33
Q

Factors Affecting Enzyme Reactions

A

pH - enzymes in environments that are too acidic or basic for them will start to denature, an excess of hydrogen or hydroxide ions will affect the hydrogen bonds within the protein structure
Substrate Concentration - the higher the amount of substrate the higher the reaction speed until the enzymes have been saturated with substrate
Tempurature - molecules gain kinetic energy allowing reactions to occur faster until the enzyme starts to denature

34
Q

Competitive Inhibitor

A
  • molecules with a similar shape to an enzyme’s substrate molecule
  • will bind to the active site and prevent substrate molecules from binding to the enzyme
35
Q

Noncompetitive Inhibitor

A
  • molecules that will bind to the regulatory site of an enzyme
  • substrate molecules can still bind to the enzyme but won’t react
36
Q

Feedback Inhibition

A
  • the inhibition of an enzyme in a metabolic pathway by the final product of that pathway
  • binds to the regulatory site and changes the active site so that it won’t function properly
  • prevents the accumulation of final product
37
Q

Precursor Activity

A
  • the activation of an enzyme in a metabolic pathway by the initial reactant of that pathway
  • binds to the regulatory site and changes the active site to make to improve the fit of the enzyme-substrate complex
  • prevents the accumulation of initial reactant
38
Q

Digestive Process

A
  1. ingestion - taking in of nutrients
  2. digestion - breakdown of complex organic molecules into enzymes by enzymes
  3. absorbtion - transport of digested nutrients to the cells of the body
    4 - egestion - removal of food waste from the body
39
Q

Roles of the Digestive System

A
  • breakdown of molecules and energy is released (catabolic reaction)
  • formation of molecules and energy is used (anabolic reaction)
40
Q

Salivary Glands

A
  • produces saliva which contains amylase (breaks down complex carbohydrates to simple carbohydrates / breaks down starch into maltose)
  • dissolves food (polar) particles
  • makes it possible to taste the food
  • lubricates the food to facilitate swallowing
41
Q

Teeth

A
  • incisors are in the front and specialize in cutting
  • canines surround the incisors and specialize in tearing
  • premolars are behind the canines and specialize in grinding
  • molars are at the very back and specialize in crushing
42
Q

Esophagus

A

Once the food (bolus) is swallowed it stimulates the walls of the esophagus causing a series of rhythmic muscle contractions that push the food down (peristalsis)

43
Q

Stomach Sphincters

A
  • lower esophageal sphincter (LES) or cardiac sphincter contracts to prevent stomach contents froms entering the esophagus and relaxes to let food from the esophagus fall into the stomach
  • pyloric sphincter controls the movement of digested food into the small intestine
44
Q

Excretions of the Stomach

A
  • mucus: protects the smoach from the digestive juices
  • hydrocloric acid: kills harmful substances ingested with the food, activates pepsinogen into pepsin
  • pepsinogen/pepsin: breaks down long amino acid chains in proteins into polypeptides
  • rennin: causes milk to curdle preventing the milk from passing through the GI tract too quickly
45
Q

Ulcers

A
  • the mucous lining of the stomach breaks down, the stomach wall is exposed to HCl and pepsin
  • acids irritates blood vessels beneath the stomach wall and cause increased blood flow and acid secretions, causing even more irritation
  • caused by the bacterium, H. pylori
46
Q

Stomach Additions

A
  • alchohol, some drugs, and vitamin B are absorbed into the blood
  • food exiting the stomach is called chyme
  • folds in the stomach lining called rugae
47
Q

Parts of the Small Intestine

A
  • duodenum (majority of digestion)
  • jejunum (absorbtion of majority of nutrients)
  • ileum (continues absorbtion)
48
Q

Small Intestine Digestion

A
  • erepsin breaks down short-chain peptides into individual amino acids
  • disaccharidases break down disaccharides into monosaccharides
  • maltase breaks down maltose into glucose
49
Q

Villi

A
  • small finger-like projections lining the small intestine that increases surface area
  • each cell of the villi has microscopic finger-like projections along the cell membrane
  • each villus contains a capillary, lacteal, and vein
  • monosaccharides and amino acids enter the capillaries
  • fatty acids and glycerol enter the lacteal
  • some nutrients absorbed by active transport
50
Q

Small Intestine Absorbtion

A
  • iron abdorbed in the duodenum
  • vitamin B₁₂ and bile salts absorbed in the terminal ileum
  • water and lipids are absorbed throughout the small intestine
  • sodium bicarbonate absorbed by active transport
  • glucose and amino acids absorbed by co-transport
  • fructose absorbed by facilitated diffusion
51
Q

Pancreas Buffer

A
  • acids entering the small intestine cause prosecretin to be converted into secretin
  • secretin stimulates the release of HCO₃ by the pacreas into the duodenum
  • raises the pH of the chyme and inactivates pepsin
52
Q

Pacreas Digestion

A
  • enterokinase converts trypsinogen into trypsin that breaks down long-chain polypeptides into short-chain peptides
  • erepsin breaks down short-chain polypeptides into individual amino acids
  • amylase enzymes break down intermediate-size carbohydrates into disaccharides / starch into maltose
  • lipase breaks down fat into glycerol and fatty acids
53
Q

Liver and Gallbladder in Digestion

A
  • produces bile which contains bile salts that help in fat digestion (emulsification)
  • stores bile in the gall bladder
  • the presence of fat in the stomach releases CCK (cholecystekone) that trigger the gall bladder to release bile
54
Q

Liver Addition

A
  • stores glycogen, vitamin A, B₁₂, D
  • harmful substances are detoxified by making them soluble to be removed in urine
  • breaks down hemoglobin of red blood cells and stores them in the gallbladder for removal
55
Q

Gallstones

A
  • cholesteral binds to bile salts and forms crystals
  • gallstones obstruct the bile dut inhibiting fat digestion
  • causes jaundice
56
Q

Cirrhosis of the Liver

A
  • nutritional deprivation or infection of the liver
  • caused by overconsumption of alchohol or other harmful agents that destroy liver tissue
  • damages cells are replaced by tissue that is unable to perform liver functions
57
Q

Large Intenstine

A
  • water, vitamins, and minerals are reabsorbed
  • bacteria in the large intestine produce vitamin B and K
  • undigested material collects in the descending colon, rectum
  • a fibrous diet provides bulk to the waste and causes more regular bowel movements which prevents toxic waste from staying in the body
58
Q

Gastrin

A
  • horomone secreted by the stomach
  • released by the presence of food
  • signals the release of HCl
59
Q

Enterogastrone

A
  • horomone secreted by the small intestines
  • released when a fatty meal is injested
  • slows down peristaltic movements and gastric secretions to allow for more fat digestion
60
Q

Pacreas Digestion

A
  • enterokinase converts trypsinogen into trypsin that breaks down long-chain polypeptides into short-chain peptides
  • erepsin breaks down short-chain polypeptides into individual amino acids
  • amylase enzymes