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Food biochemistry general review mind map
A general review mind map on food biochemistry, including statics, human biology, proteins, vitamins and coenzymes, etc. Suitable for review materials of biochemistry in the food field.
Edited at 2023-11-09 17:39:59
- bacteria
This is a mind map about bacteria, and its main contents include: overview, morphology, types, structure, reproduction, distribution, application, and expansion. The summary is comprehensive and meticulous, suitable as review materials.
- Plant asexual reproduction
This is a mind map about plant asexual reproduction, and its main contents include: concept, spore reproduction, vegetative reproduction, tissue culture, and buds. The summary is comprehensive and meticulous, suitable as review materials.
- Reproductive development of animals
This is a mind map about the reproductive development of animals, and its main contents include: insects, frogs, birds, sexual reproduction, and asexual reproduction. The summary is comprehensive and meticulous, suitable as review materials.
Food biochemistry general review mind map
- bacteria
This is a mind map about bacteria, and its main contents include: overview, morphology, types, structure, reproduction, distribution, application, and expansion. The summary is comprehensive and meticulous, suitable as review materials.
- Plant asexual reproduction
This is a mind map about plant asexual reproduction, and its main contents include: concept, spore reproduction, vegetative reproduction, tissue culture, and buds. The summary is comprehensive and meticulous, suitable as review materials.
- Reproductive development of animals
This is a mind map about the reproductive development of animals, and its main contents include: insects, frogs, birds, sexual reproduction, and asexual reproduction. The summary is comprehensive and meticulous, suitable as review materials.
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- Outline
food biochemistry
over
Hormone Review
human hormone system
sensory input
Central Nervous System
hypothalamus
hypothalamic hormone
anterior pituitary gland
One glance
adrenocorticotropic hormone
adrenal cortex
Two eyes
cortisol, adrenaline, aldosterone
many organizations
final goal
thyroid stimulating hormone
thyroid
Thyroid hormone, triiodothyronine
muscle, liver
follicle-stimulating hormone, luteinizing hormone
ovaries/testicles
Progesterone, Estradiol/Testosterone
reproductive organs
growth hormone
🈳
liver, bone
prolactin
🈳
mammary gland
posterior pituitary gland
Oxytocin
🈳
Smooth muscle, breast
Vasopressin (antidiuretic hormone)
arterioles, kidneys
adrenal medulla
adrenaline
liver muscle heart
blood sugar level
islet cell pancreas
Insulin, glucagon, somatostatin
liver, muscle
Different hormones go through different levels and have different effects on time.
hormone
Hormone definition
A class of trace organic compounds secreted by living cells (special tissues or glands) that have special agonistic effects on certain target cells (regulating and controlling the metabolism or physiological functions of various substances).
animal hormones
definition
All hormones secreted by animal glandular cells (glandular hormones) and non-glandular tissue cells (tissue hormones)
five endocrine glands
Thyroid, adrenal glands, pancreas, gonads, and pituitary gland
There is no excretory tube. It goes directly into the blood or lymph and then into the blood. The circulatory system transports the whole body.
spine
glandular hormones
1. Amino acid derivative hormones
Thyroxine
Increase metabolism
adrenaline
1. Promote hepatic glycogen decomposition and increase blood sugar 2. Constrict capillaries and increase blood pressure
2. Peptide and protein hormones
insulin
Promote glycogen synthesis and glucose utilization, as well as promote protein and lipid anabolism.
glucagon
Promote hepatic glycogen decomposition and increase blood sugar
auxin GH
Promote RNA biosynthesis, thereby promoting protein biosynthesis, allowing organs to grow and develop
thyroid stimulating hormone TSH
Directly stimulates the thyroid gland to secrete thyroxine, and indirectly affects the entire metabolism of the body.
adrenocorticotropic hormone ACTH
Stimulates the development and secretion of the adrenal cortex
Oxytocin, vasopressin (nonapeptide, structurally similar)
Oxytocin causes the smooth muscles of the uterus and breast to contract, and vasopressin causes capillaries to contract.
prolactin
Promote lactation secretion by lactation glands and maintain activity of corpus luteum
Gonadotropin (glycoprotein)
follicle stimulating hormone
Female: Stimulates ovarian maturation, prepares to produce eggs and promotes the secretion of estradiol Male: Stimulates testicular development, produces sperm
luteinizing hormone
Female: stimulates ovulation, produces corpus luteum and secretes progesterone. Male: stimulates the development of Leydig cells in the testicles and secretes male hormones.
3. Steroid hormones
Adrenocorticotropic hormone
Function: Regulates sugar metabolism and water and salt metabolism. Those with hyperactive functions can cause obesity and precocious puberty in adolescents
Cortisone and hydrocortisone: increase gluconeogenesis and have anti-inflammatory effects. They are often used in medicine to relieve inflammation of the eyes, nose and rheumatoid arthritis.
sex hormones
androgens
Stimulates the development of male sexual organs, promotes sperm production and male secondary sexual characteristics.
Estrogen
1. Follicle hormone (estradiol, estrone, promotes the development of female sexual organs and ovulation) 2. Progesterone (progesterone, stimulates the uterus to prepare for conception and promotes mammary gland development, inhibits ovulation, stops menstruation, inhibits estrus and reduces uterine contractions etc.).
4. Aliphatic hormones
Prostaglandin PG
There are many kinds, with different structures and different functions.
The seminal vesicles have stronger synthetic capacity, followed by the kidneys, lungs and gastrointestinal tract
tissue hormone
Invertebrate
crustacean hormone
insect hormones
Plant hormone
definition
Phytohormones, also known as plant growth regulatory substances, are a class of trace active substances that promote or inhibit the physiological processes of plants.
Auxins
Indoleacetic acid (IAA). Auxin is present in the vigorous parts of plants and is responsible for the growth of plant cells.
Gibberellins
Synthetic site: in young leaves, fruits and root tips. Function: Promote plant growth and morphology, break seed dormancy, induce fruit growth, form parthenocarpy, etc.
Beer malt: use gibberellin to increase the content of α-amylase in malt.
Cytokinins
Promote cell division and differentiation, promote cell lateral thickening, break dormancy, promote fruit setting and other physiological activities.
abscisic acid
Plant growth inhibitor, which can promote the maturation of plant abscission layer cells and cause organ shedding
Ethylene
A product of normal metabolism in higher plants. Function: 1. Reduce growth rate. 2. Promote fruit ripening, promote cell radial growth and inhibit longitudinal growth, induce seed germination 3. Promote organ shedding and other effects.
Mechanism
Hormones and receptors
Hormone receptor definition
Special proteins that bind tightly to hormones with high specificity
Only affects target cells (which have corresponding receptors)
receptor site
on target cell membrane
Water-soluble, insulin, epinephrine glucagon
within target cells
Lipid-soluble, adrenocortical hormones, sex hormones, steroids
Mechanism
Acts via cyclic nucleotides
Acts through phosphoinositide enzymes. Acts via tyrosine kinase.
induced enzyme synthesis
human biology
digestive system
1.Basic functions (1) Digestion and absorption function (2) Endocrine function; digestive juice 6-10L/d (3) Immune function
2. How food is digested (1) Mechanical digestion (2) Chemical digestion.
organ size
1. Kidney, three fingers together 2. Heart, make a fist with the right hand and insert the thumb inside 3. Uterus, one-half of the heart 4. Duodenum, five fingers together, stack three 5. The stomach can be big or small. 50-100ml on an empty stomach, 1200-1600ml on a normal meal, 4000ml on a large meal
digestion time
1. Oral cavity 8s (eating quickly, cardia injury, people getting fat or thin) 2. Stomach 3 hours 3. Small intestine 25min-6 hours (longer for girls)
digestive tract
oral cavity
beginning of digestive tube
saliva 1. Function: Moisturize food to facilitate digestion, hydrolyze starch, sterilize, and excrete. 2. Saliva secretion is regulated by nerves. 3. Saliva physical properties: colorless, odorless, moderately acidic (pH 6.6-7.1); amount (L/d): 1.0-1.5
Chewing function: 1. Chop food. 2. Make food fully exposed to salivary amylase 3. Can reflexively cause increased activity of the stomach, pancreas, liver, gallbladder, etc. Strong to prepare for further digestion and absorption.
pharynx
The only way the digestive tube passes from the mouth to the esophagus
esophagus
Stomach
1. Its main function is to store food and perform preliminary digestion of food. 2. The stomach is not the main site of absorption. 3. Gastric juice components: (1) Hydrochloric acid (2) Pepsin (3) Mucus (4) Intrinsic factor Gastric juice physical properties: colorless, odorless, acidic (pH 0.9-1.5); amount (L/d): 1.5-2.5 4 .Gastric motility gastric receptive relaxation definition: Food stimulates the receptors in the mouth and pharynx, which reflexively causes gastric smooth muscle to relax and increase gastric volume. The meaning of gastric receptive relaxation: a large amount of food is taken in while the intragastric pressure remains unchanged. Gastric motility: pushing food from the middle of the stomach into the duodenum
small intestine
It can be divided into three parts: duodenum, jejunum and ileum, which are the most important parts for absorbing nutrients. (Females are longer than men)
the large intestine
The large intestine is divided into three parts: cecum, colon and rectum. (Female’s colon is longer than Nan’s)
Large intestine movement: Small intestine movement is small and slow, which is beneficial to the storage of feces in the large intestine. Features: bag-like reciprocating motion; segmented or multi-bag propulsive motion and peristalsis
anus
digestive glands
Salivary glands: There are three pairs, parotid glands, sublingual glands, and submandibular glands
Liver: The largest gland that secretes bile and stores it in the gallbladder Bile is alkaline, has no digestive enzymes, and contains emulsified fat. The role of fat.
Bile promotes fat digestion and absorption 1.. Emulsifiers (bile salts, cholesterol and lecithin) 2. Delivery vehicle (bile salts participate in the formation of micelles) 3. Promote the absorption of fat-soluble vitamins (vitamins A, D, E, K) 4. Neutralize gastric acid (bile salts) and promote self-secretion of bile
Pancreas: secretes pancreatic juice, which is alkaline and contains digestive proteins enzymes of quality, iodine powder and fat.
Regulation of pancreatic juice secretion neuromodulation Body fluid regulation: secretin, cholecystokinin
Intestinal glands: tiny glands located in the mucosa of the small intestine that secrete intestinal The liquid is alkaline.
Gastric glands: are invaginations of the gastric wall mucosa that can produce hydrochloric acid, Mucus, pepsin.
Summary of differences between male and female digestive systems
1. Small stomach. 2. Long intestinal tract: long retention time in the body and sufficient absorption; hemorrhoids; bloating; pain; excessive farts; and more difficulty in losing weight.
human skeleton
central axis
skull spine thoracic
appendages
Upper limbs(64)
Lower limbs(62)
dynamic
carbohydrate
Glycolysis
Ten-step reaction, the first five steps are energy consumption, the second five steps are production capacity
Three speed limits (three irreversible) (G6P, F162P, pyruvate)
place
Other sugar metabolism pathways: fructose incomplete, galactose and glucose complete
physiological significance
1. Main mode of hypoxia energy supply 2. Source of energy supply for a few cells (red blood cells, white blood cells and tumor cells) 3. Provide other metabolic raw materials
Definition: 1 glucose → 2 pyruvate 2NADH, 2ATP
Pyruvate outlet: aerobic: tricarboxylic acid cycle carbon dioxide energy anaerobic: lactic acid ethanol acetic acid
gluconeogenesis
Definition: Synthesis of glucose from non-sugar substances
Pyruvate, lactic acid, glycogenic amino acids, glycerol, tricarboxylic acid cycle intermediates
tricarboxylic acid cycle
8 steps 8 enzymes
physiological significance
Common oxidation pathways of three major nutrients
biological significance
1. Ubiquitous 2. The most effective for energy acquisition 3. Transformation hub 4. Fermented products (citric acid, glutamic acid)
Lipids
Classification
Fats Lipids (cholesterol/cholesterol esters, glycolipids, phospholipids)
Lipids are digested and absorbed in the body
Main place: small intestine
Fat A small amount of phospholipids and cholesterol → chylomicron Through the small intestinal mucosal cells → intercellular fluid → lymphatic system → blood.
Cholesterol or cholesteryl ester: absorption requires the assistance of bile salts and lipoprotein binding.
fatty acid
Fatty acid synthesis
1. Saturated fatty acids
2C Acetyl CoA→→→→16C Palmitic Acid (Place: Cytoplasm)
Carbon chain elongation Location: mitochondria, endoplasmic reticulum
Acetyl CoA transport
fatty acid synthase system
6 enzymes 1 protein
fatty acid catabolism
1.Beta oxidation
generate energy
One round, activation consumes 2ATP and produces 1 FADH2 (2ATP), 1 NADH (3ATP), and 1 acetyl CoA (12ATP)
Even-numbered carbon example: fifteen-carbon palmitate (C15H31COOH), 7*2 7*3 12*8-2=129ATP
A complete citric acid cycle: 2 molecules of CO2, 3 molecules of NADH, 1 molecule of FADH2, 1 molecule of GTP or ATP
unsaturated, odd number
Unsaturated: equivalent to dehydrogenation once, cis → trans → hydroxyacyl CoA, the same as the following
The final product of odd-numbered fatty acids is propionyl CoA → → → succinic acid, etc., which enters the tricarboxylic acid cycle
Fatty acid beta oxidation site: mitochondria, mainly liver cell mitochondria, Cβ reaction 1 round less 2C
Pathway: Fatty acid activation → fatty acyl-CoA dehydrogenation → enoyl-CoA hydration → hydroxyacyl-CoA dehydrogenation → ketoacyl-CoA thiolysis → produce 1 acetyl CoA and less 2C fatty acyl-CoA Repeat β-oxidation → the final product is acetyl CoA
2.ω oxidation
Oxidized to carboxyl
Ketone body production and utilization (fatty acid beta oxidation → acetyl CoA tricarboxylic acid cycle → ketone body)
Ketone bodies are an important form of energy export from the liver to extrahepatic tissues. Ketone bodies are produced in the liver and utilized extrahepatic
Location: Liver Utilization: Rapid synthesis of acetyl CoA
cholesterol
conversion steroids
Physiological functions:
Fat
1. Energy storage and supply 2. Prevent heat loss 3. Protect the body
lipids
1. Maintain the structure and function of biofilms 2. Promote the absorption and transportation of fat and fat-soluble vitamins 3. Cholesterol can be converted into a variety of steroid hormones and active vitamin D. Bile acids, etc.
Lipids 4. Constitute body tissues and important biologically active substances
protein
Amino acid synthesis
Carbon frame source
Krebs cycle, glycolysis, pentose phosphate pathway, amino acid breakdown pathway
Amino source
It starts from inorganic nitrogen, that is, inorganic nitrogen is first converted into ammonia, and then Transformed into nitrogen-containing organic compounds.
protein synthesis
Activation Start Prolongation Termination
protein degradation
The final route of oxidative decomposition of amino acids: tricarboxylic acid cycle, amines
uric acid
Normal: Eliminate free radicals, protect liver and kidney vascular endothelial cells, and improve immunity
Too high: pro-oxidant, arteriosclerotic cardiovascular disease, gout
Two types of peptidases (end) and proteases (end)
Deamination Transamination Combined Decarboxylation
nutritional value
content
Quality (amino acid type quantity)
effectiveness
Six factors that affect effectiveness: conformation, binding, inhibitors, surface area, processing, and physiology
Eight essential amino acids
Suppose you come to borrow a book or two
protein digestion and absorption
static
water
Function
1. Main components 2. Good solvent for metabolites 3. Mediator of biochemical reactions 4. Strengthen the connection of physiological functions of various organs 5. Regulate and stabilize human body temperature 6. Lubricant
adjust
neurohormone chemistry
way
supply
Eating food, drinking water, and nutrient metabolism
discharge
Four channels of urination, defecation, sweating and breathing
carbohydrate
sugar definition
definition
General term for polyhydroxy aldehydes or polyhydroxy ketones and their polymers and derivatives
composition
Mainly composed of C, H, O
Molecular formula
(CH2O)n
1⃣If it conforms to the general formula, it is not necessarily a sugar, such as CH3COOH (acetic acid), CH2O (formaldehyde), C3H6O3 (lactic acid) 2⃣If it does not conform to the general formula, it is not necessarily a sugar
Biological effects of sugar
energy substances
structural matter
Provide carbon source
Cellulose, hemicellulose and pectin in plants, peptidoglycan in bacterial cell walls, chitosan in shrimps and crabs, etc.
converted into other biological macromolecules
Amino acids, nucleotides, and fatty acids provide the carbon skeleton.
bioactive substances
Oligosaccharides
Prebiotics
polysaccharide
For example, Ganoderma lucidum polysaccharides and fungal polysaccharides have the effects of improving immunity and preventing cancer.
Information molecules recognized by cells
Classification of sugar
number
Monosaccharide
Can no longer be hydrolyzed, basic structural unit
Triose
Glyceraldehyde and dihydroxyacetone
tetraose
D-erythrose
Pentose
Ribose
hexose
glucose
galactose
Mannose
fructose
Heptose
Oligosaccharides
Can hydrolyze 2-10 monosaccharide molecules
disaccharide
Some disaccharides are reducing
sucrose
maltose
lactose
trisaccharide
marshmallow
polysaccharide
Starch, cellulose, glycogen
Some have a colloidal structure in water, and some are insoluble in water.
No flavoring, no reducing properties
Optically active, no mutarotation
Carbonyl type
aldose
Ketose
Carbon chain type
pyranose
Furanose
important polysaccharides
starch
Amylose
α-1.4 glycosidic bond
Not fully straight, left-handed spiral
iodine solution
Starch (blue or purple)--red dextrin--colorless dextrin--maltose--glucose
Amylopectin
α-1.4 glycosidic bond
branch
α-1.6 glycosidic bond
iodine solution
Purple red
glycogen
Composed of glucose residues, more branches, similar structure to amylopectin
Cellulose
β-1.4 glycosidic bond
Ruminants contain enzymes that can be used by the normal flora in the human intestine to promote defecation.
pectic substance
1. Pectic acid: The main component of pectic acid is polygalacturonic acid, which produces galacturonic acid after hydrolysis.
2. Pectin ester acid: Pectin ester acid shows varying degrees of methyl esterification, with the esterification range ranging from 0 to 35%. generally Those with a very low degree of esterification (less than about 5%) are called pectic acid, and those with a high degree of esterification are called pectic acid.
3. Protopectin: insoluble in water, mainly present in primary cell walls, especially parenchyma cells and meristems cell wall.
In addition to polygalacturonic acid, pectin substances also contain small amounts of sugars, such as L-arabinose, D-galactose, L-rhamnose, and D-glucose.
chemical properties of simple sugars
The effect of acid
molish reaction
In case of furfural or hydroxymethylfurfural, purple
alpha-naphthol
seliwawoff reaction
Ketose is red, aldose is very light
Resorcinol and hydrochloric acid
esterification reaction
The alcoholic hydroxyl group of acid and sugar condenses and loses water to form ester
Sucrose fatty acid ester commonly used emulsifier
Effect of base (isomerization)
Glycoside reaction
The hemiacetal hydroxyl group reacts with the alcohol or phenolic hydroxyl group and loses water to form an acetal derivative, glycoside
Reducing property (detection of monosaccharides)
Aldehyde group
Sugars that can be oxidized by alkaline weak oxidants are usually called reducing sugars, and sugars that are not oxidized are called non-reducing sugars.
Monosaccharides are all reducing sugars, sucrose is a non-reducing sugar, maltose and lactose are reducing sugars
D-glucuronic acid combines with poisons to form glycosides and is excreted from the body for detoxification.
Fehling's reagent
Potassium Sodium Tartrate NAOH CUSO4
reduction
Aldose or ketose can be reduced to sugar alcohols by sodium borocyanide or sodium amalgam.
The formation of
Different sugars form crystals with different shapes and melting points, which can be used to identify different sugars.
amination reaction
The hydroxyl groups in monosaccharide molecules (mainly -OH on 2C and 3C) can be replaced by -NH2 to produce amino sugars, also called sugar amines.
In nature, amino sugars mostly exist in the form of acetyl amino sugars, of which the most important three are: N-acetyl-D-glucosamine (NAG), acetylmuramic acid (NAM), and acetylneuraminic acid (NAN). The first two are responsible for the formation of bacterial cell walls, bacterial capsules, crustacean shells, and insect shells. The main component of insect shells; the latter is also called sialic acid.
deoxygenation
When the hydroxyl group on a monosaccharide loses oxygen, deoxysugar can be generated. For example, deoxyribose is generated through deoxygenation of ribose.
Lipids
Overview
definition
A large class of biomolecules that are insoluble in water in biological cells and tissues, but soluble in non-polar solvents such as ethanol, and are mainly composed of hydrocarbons.
Classification
simple, compound, derived
Biological effects
1. Structural components of biological membranes (glycerophospholipids and sphingomyelins, cholesterol, glycolipids 2. Energy storage form (triglycerides) 3. Precursors of hormones, vitamins and pigments (terpenes, sterols, i.e. lipids) 4. Growth factors 5. Antioxidants 6. Chemical signals 7. Participate in signal recognition and immunity (glycolipids) 8. The fat tissue of animals has protective functions such as thermal insulation and mechanical pressure resistance.
fatty acid
definition
4-36C hydrocarbon chain carboxylic acid
Classification
length
1. Short chain 4-5 2. Medium chain 6-10 3. Long chain 12-26
unsaturated bond
1. Saturated (palmitic acid, stearic acid) 2. Unsaturated (oleic acid, linoleic acid) both are straight chain
Necessary for synthesis
1. Essential fatty acids (linoleic acid, linolenic acid, arachidonic acid) 2. Non-essential fatty acids
unsaturated fatty acid
1. Cis 2. Trans (more stable)
name
Customary nomenclature (linoleic acid), systematic nomenclature (octadeca-9,12-dienoic acid (cis, cis), abbreviation 18:2△⁹,¹²
Triacylglycerol
definition
An ester formed by dehydration and condensation of 3 hydroxyl groups of glycerol and 3 fatty acid molecules, accounting for about 90% of lipids. Molecular structure
physical properties
1. Melting point (the longer ↑, the more unsaturated bonds ↓)
2. Oiliness (liquid grease lubricating film) and viscosity (side attraction of acylglycerol molecules), plasticity (solid fat’s strain resistance)
3. Colorless, odorless thick liquid or waxy solid. The density is less than 1g/cm3, insoluble in water, easily soluble in non-polar organic solvents such as ether, and can be emulsified by emulsifiers. no clear melting point
chemical properties
1. Hydrolysis (acid or alkali or lipolytic enzyme, product glycerol fatty acid) and saponification (alkaline hydrolysis irreversible). Saponification value: the number of koh mg required for saponification of 1g triglyceride
2. Acid ester substitution and alcohol transesterification
Lower the melting point of oils and prepare emulsifiers
3. Oxidation
In rancidity, free fatty acids are oxidized and broken down to form aldehydes and ketones low molecular weight fatty acids, producing a foul odor. Acid value neutralization 1g of free fatty acids consumes koh mg
4.Hydrogenation
When saturated, the liquid becomes solid and prevents rancidity. Margarine, vegetable cream
5. Halogenation
Iodine value measurement
Phospholipids
Phospholipid definition
Complex lipids containing phosphoric acid
The most important types of phosphoglycerides
Glyceryl phosphate
definition
The third hydroxyl group of glycerol is phosphorylated, and the other two hydroxyl groups are esterified with fatty acids.
The phosphate group continues to esterify with the hydroxyl group to form various glycerophospholipids. 1. Esterification of phosphoric acid and choline, lecithin (biofilm component). 2. Phosphoric acid and ethanolamine, cephalin (component of cerebral cortex) 3. Phosphoric acid and serine, serine phospholipid (prothrombinase activator) 3. Inositol esterification, inositol phospholipid (heart, brain)
Sphingomyelin
Ingredients: Sphingosine, fatty acids and phosphatidylcholine
Ceramide is formed from sphingosine nh2 linked to fatty acids
nature
1. Fat-soluble 2. Unsaturated fatty acids are easily oxidized 3. Can be hydrolyzed 4. Hydrophilic and lipophilic
Binding lipids
lipoprotein
Definition: A complex of lipids and proteins bound by non-covalent bonds, mainly found in plasma, also known as plasma lipoproteins
density classification
chylomicrons very low density lipoprotein VLDI intermediate density lipoprotein IDL low density lipoprotein LDL HDL
LDL transports cholesterol to the peripheral blood; HDL transports cholesterol lipoproteins to the liver to maintain cholesterol balance
High LDL and low HDL signal cardiovascular disease
Glycolipids
simple lipids
Terpenes
Definition: The carbon skeleton is composed of two or more isoprene connected.
C10 monoterpene, c15 sesquiterpene, c20 diterpene (vitamin A), beta carotene is a tetraterpene (vitamin A precursor)
Steroid
Definition: Based on the structure of cyclopentane polyhydrophenanthrene
cholesterol
Definition: C17 profile is C8
sterol derivatives
Bile acids (main metabolites of cholesterol, main components of bile, emulsified fats, helpful for intestinal absorption)
Cholesterol can be converted into androgens, estrogens, glucocorticoids, mineralocorticoids, and vitamin D
Phytosterols
Definition: C17 profile is C10
reduce cholesterol
nucleic acid
definition
Polynucleotide polymer composed of bases, pentose sugars and phosphates
biological functions
1. DNA is the storage and carrier of genetic information and the main genetic material of living things.
2.RNA is mainly involved in the transmission and expression of genetic information.
RNA has a catalytic function
nucleoside
Definition: It is formed by condensation of pentose sugar and base and connected by glycosidic bond.
Nucleotide
Definition: A base, a pentose sugar, and a phosphate formed through glycosidic bonds and esterification
nucleic acid
3,5 phosphodiester bond
Physical and chemical properties: Denaturation (the hydrogen bonds are broken and the double helix becomes a single-stranded structure) Renaturation (the single strand restores the double helix) Hybridization (the base pairing region between single-stranded DNA from different sources or between single-stranded DNA and RNA, in the complex can form a local double helix region)
RNA
Classification
mRNA,tRNA,rRNA
effect
Messenger, transporter, assembly catalysis
structure
straight line
DNA
structure
primary structure
straight line circular
secondary structure
double helix, right-handed
Anti-parallel 3'→5' is positive
Maintaining force: hydrogen bonding, ionic bonding, main base stacking force
tertiary structure
Specific conformations formed by twisting and folding: loops and supercoils.
protein
Overview
definition
It is a biological macromolecule with a relatively stable conformation and certain biological functions, which is composed of 20 kinds of L-α-amino acids condensed through amide bonds in a certain sequence.
chemical components
CHONS
Classification
simple protein
definition
Proteins that produce only amino acids when hydrolyzed
Category 7
Albumin (serum protein, whey protein), Globulin (serum globulin divided into superior and inferior globules), Gluten (rice glutenin), prolamin (more proline, amide, more non-polar side chains, in plant seeds, zein, gliadin) Histones, (more histidine and lysine, such as calf thymus histones) Protamine (rich in basic amino acids, salmon protamine) Sclerostin (protective function of animal connective tissue, keratin, collagen, elastin, reticulin)
Insoluble in water
Gluten
prolamins
Nothing, nothing, nothing, nothing
Nothing nothing nothing nothing nothing nothing
hard protein
Insoluble in alcohol
Gluten
Insoluble in water 7.80 soluble
Nothing, nothing, nothing
Nothing nothing nothing nothing nothing nothing
nothing nothing nothing
insoluble in acid
nothing nothing nothing
Nothing, nothing, nothing
Nothing, nothing, nothing, nothing
Nothing nothing nothing nothing nothing nothing
hard protein
insoluble in alkali
nothing nothing nothing
Nothing, nothing, nothing
Histones (dilute ammonia)
Protamine (same as left)
hard protein
insoluble dilute salt
Gluten
Nothing, nothing, nothing
Nothing, nothing, nothing, nothing
Nothing nothing nothing nothing nothing nothing
hard protein
Saturated ammonium sulfate precipitation
Albumin
Semisaturated ammonium sulfate
globulin
binding protein
definition
During hydrolysis, not only amino acids are produced, but also other organic or inorganic compounds and proteins are produced. The non-amino acid part is called a prosthetic group or ligand
Category 7
nucleoprotein
Prosthetic group: nucleic acid
DNA nucleoproteins and ribosomes
lipoprotein
Prosthetic group: lipid
Vitelloglobulin
Glycoproteins and mucins
prosthetic base: Galactose, mannose, hexaminose, hexuronic acid Acid, sialic acid, sulfuric acid or phosphoric acid
Ovalbumin
phosphoprotein
Prosthetic group: phosphate group through ester bond with serine in protein acid or threonine residue side chains.
casein
heme protein
Prosthetic group: heme (porphyrin compound with metal in the center)
Hemoglobin (Fe), chlorophyll (Mg)
flavoprotein
Prosthetic group: flavin adenine dinucleotide
succinate dehydrogenase
metalloprotein
Prosthetic group: a protein that directly binds to a metal
Alcohol dehydrogenase contains zinc
Biological functions 8 points
1.Catalysis
Enzymes, proteins, proteolytic enzymes, alpha salivary amylase
2. Structure
membrane proteins, keratin, collagen
3.Transshipment
outside cell membrane
Hemoglobin (oxygen), serum albumin (fatty acids)
in cell membrane
glucose transporter
4.Storage
Bird embryo ovalbumin, peanut and soybean protein, lactoferrin to store iron
5. Exercise
Contractile protein, swimming protein, motor protein (ATP chemical energy is converted into mechanical energy for movement)
6. Defense against offense
Immunoglobulin defense, blood coagulation protein (thrombin), snake venom, ricin, animal and plant defense
7.Adjustment
1. Regulate the ability of other proteins to perform physiological functions, such as insulin (peptides)
2. Participate in the regulation of gene expression, activating or inhibiting the transcription of genetic information into rma
8. Control cell growth and differentiation
Growth factors (growth hormones - peptides), repressor proteins (terminate transcription).
amino acids
structure
20 kinds of amino acids in living organisms, L type (glycine has no LD)
Rare amino acids (derivatives), non-protein amino acids (not involved in protein composition)
nature
physics
1.Solubility
2. Optical activity
3. Taste (D type is sweet, L type is sweet, bitter and sour)
4. Absorption spectrum
Chemical
1.Acidity and alkalinity
2.Amino reaction
Reacts with nitrous acid - produces nitrogen gas, determines its amount, and determines nitrogen by Van's method; Reaction with aldehydes - the principle of measuring amino acid nitrogen by formaldehyde method; Salt formation - cysteine hydrochloride; Acylation and hydroxylation reactions - Sanger reaction, Edman reaction Carbonyl ammonia reaction – also known as Maillard reaction
3.Carboxyl reaction
Ester-forming and salt-forming reactions - monosodium glutamate, acid chlorination reaction, amide-forming reaction, azide reaction
4. Amino carboxyl groups participate in the reaction together
Reaction of amino acids with ninhydrin
5. Reaction of functional groups on R group
For example: the sulfhydryl group on cysteine is easily oxidized into a disulfide bond to form cystine
Classification
Can the human body synthesize it by itself?
Essential Amino Acids Let’s borrow a book or two
8 types (tryptophan, phenylalanine, lysine, methionine, threonine, valine, leucine, isoleucine)
non-essential amino acids
Semi-essential amino acids
Synthetic Insufficient Supply in Infants
Arginine, Histidine
R-based structure
aliphatic amino acids
15 types, 5 neutral, 2 hydroxyl-containing, 2 sulfur-containing, 4 acidic and amide, 2 basic
aromatic amino acids
3 types
Heterocyclic amino acids
2 kinds
R base polarity
Be nonpolar or hydrophobic
Polar but uncharged
At pH 7, the R group is negatively charged
At pH 7, the R group is positively charged
protein structure
primary structure
polypeptide chain
The order of amino acids in the peptide chain and the position of disulfide bonds
Free amino N-terminus, free carboxyl C-terminus
secondary structure
The polypeptide chain folds itself
The spatial relationship between amino acid residues that are close to each other in a polypeptide chain due to hydrogen bonding interactions
An arbitrarily arranged polypeptide chain has no biological activity. The biological function comes from a certain conformation. The primary structure of the protein determines its conformation.
alpha helix, beta sheet, beta turn
tertiary structure
The polypeptide chain further folds and bends
The interaction between far apart amino acids in the polypeptide chain causes the polypeptide chain to bend or fold to form a tight and rigid structure. The secondary structure of the polypeptide chain further folds and curls to form a complex globular structure.
Interaction: Mainly non-covalent bonds (hydrogen bonds, ionic bonds, van der Waals forces and hydrophobic bonds, etc.), and occasionally covalent bonds - disulfide bonds.
Quaternary structure
Multiple peptide chain combination
Several peptide chains are linked by non-covalent bonds to form a stable active unit. This peptide chain is called a subunit of the protein.
Protein properties
colloid
Protein aqueous solution gel; cannot pass through semipermeable membrane
precipitation
Such as salting out
Proteins rely on water films and charges to maintain their stability in solutions. Once the water film is removed, Proteins stick together to form larger protein clumps, which eventually precipitate out
Amphiphilic dissociation and isoelectric point
electrophoresis
gel chromatography
protein denaturation
definition
Physical and chemical factors can destroy hydrogen bonds and other weak bonds in the three-dimensional structure of protein molecules, leading to the loss of protein activity.
Reversible denaturation: As long as the denaturation does not exceed the limit, the protein activity can be restored (refolded); Irreversible denaturation: The denaturation is irreversible. Such as: boiled eggs
protein color reaction
Protein color reaction refers to the color change produced by the reaction of protein with specific reagents. Proteins have many functional groups that can react chemically with different reagents to produce different colors. Common protein color reactions include the following:
enzyme
Overview
definition
Enzymes are a type of biological macromolecules with an active center and a certain conformation that are produced by living cells and can catalyze biochemical reactions both in vivo and in vitro.
Enzyme catalytic characteristics
Trace amount, specificity, high efficiency
Enzyme nature
Most proteins and a few RNAs, such as rRNA, catalyze the synthesis of amide bonds
Classification
Molecular characteristics
Monomeric oligomeric multi-enzyme system
composition
simple compound
Enzymatic reaction classification 6 categories
Oxidoreductases Transferases Hydrolases Lysis (lysis) enzymes Isomerases Ligase
name
Habit
Named according to substrate: amylase, protease; Named according to the nature of the reaction catalyzed by the enzyme: transaminase; Naming based on the above two principles: lactate dehydrogenase; Enzyme source or other characteristics of enzyme: pepsin, alkaline protease.
internationality
Lactate dehydrogenase EC 1.1.1.27
enzyme specificity
absolute relative three-dimensional
Enzyme active center
definition
A spatial site that binds to substrates and plays a catalytic role.
functional parts
1. Binding 2. Catalysis
active
Enzyme activity
Reflects the catalytic activity of the enzyme
The catalytic activity of enzymes is related to coenzymes, prosthetic groups and metal ions
Enzyme specific activity
The higher, the purer
enzymatic reaction speed
factor:
1.Substrate concentration 2.Temperature 3.Enzyme concentration 4.ph 4.Activator 6.Inhibitor
Vitamins and coenzymes
Vitamin overview
1. Vitamin definition
It is a type of organic substance necessary to maintain the normal life process of organisms. It is required in very small amounts and cannot be synthesized or synthesized in small amounts by the human body. It needs to be provided by food, but it is very important for maintaining human health.
2. Definition of provitamin
Substances that can be converted into vitamins in humans and animals
3. Definition of vitamins with the same effect
Substances that have a chemical structure similar to vitamins and have vitamin biological activity.
Function
1. Coenzyme components 2. Regulate body metabolism
Vitamin classification (solubility)
1. Water soluble 2. Fat soluble
Vitamin related symptoms
Water-soluble vitamins type 2
1. Vitamin C
Chemical nature: Ascorbic acid, polyhydroxy acidic substance
Properties: Strong reducing ability
Active form:
L-ascorbic acid
Function:
1. Anti-scurvy 2. Hydrogen transfer body 3. Coenzyme of proline hydroxylase 4. Maintain thiolase activity
Deficiency symptoms:
scurvy
2.B vitamins (8 types)
VB1
Chemical nature: anti-neuritis vitamin, thiamine (mainly in the body as thiamine pyrophosphate TPP as its coenzyme form)
nature:
Acid stable. Alkali heating, SO2 is easily destroyed
Function:
1. Decarboxylase coenzyme 2. Move the substrate into (out) the active center of decarboxylase
Deficiency symptoms:
TPP deficiency leads to obstruction of glucose metabolism, accumulation of pyruvate, and elevated levels of pyruvate in the patient's blood, urine, and brain, manifesting as polyneuritis—beriberi.
Existing form: Thiamine pyrophosphate TPP (active form)
VB2
Chemical nature: Riboflavin
Properties: Stable and heat-resistant in acid; easily destroyed by UV and alkali
Function: : Dehydrogenase coenzyme, transfer H.
Deficiency symptoms: Angular stomatitis, cheilitis, scrotal inflammation, blepharitis, blurred vision
Active form: flavin mononucleotide (FMN), flavin adenine dinucleotide (FAD), (active form)
VB3 (pantothenic acid)
Chemical nature: pantothenic acid, pantothenic acid. Coenzyme A and acyl carrier protein components
Properties: Extremely stable to heat and reducing agents, easily hydrolyzed in alkali
Function: It is a coenzyme of acyltransferase and plays the role of transferring acyl groups in metabolism.
Deficiency symptoms: widespread, generally not deficient
Existing form:
Coenzyme A (CoA-SH)
VB5 (nicotinic acid)
Chemical nature: Niacin, also known as niacin, vitamin PP
Properties: It is not damaged by light, heat and oxygen, and is the most stable vitamin.
Function: Nicotinamide adenine dinucleotide NAD and NADP (active form) are coenzymes of a variety of non-aerobic dehydrogenases and function as hydrogen transmitters.
Deficiency symptoms: Dermatitis, diarrhea, dementia
Existing forms: Niacin, Niacinamide (mainly)
VB6
Chemical nature: Vitamin B6, derivative of pyridine.
Properties: Resistant to heat, acid and alkali, but sensitive to light.
Function: coenzyme of transaminase, amino acid decarboxylase, pyridoxal phosphate and pyridoxamine phosphate (active form)
Deficiency symptoms: vomiting, central nervous system excitement, convulsions, hypochromic anemia
Existing forms: Pyridoxine, pyridoxal and pyridoxamine
VB7 (vitamin H) biotin and decarboxylated biotin
Chemical essence: Parallel ring of thiophene with valeric acid side chain combined with urea.
nature:
Function: Coenzyme of carboxylase, participating in the fixation or decarboxylation reaction of CO2 in the body.
Deficiency symptoms: Dermatitis, hair loss
Existing form: biotin (active form)
VB11 (folic acid)
Chemical essence: Pteroylglutamic acid, composed of pterin, p-aminobenzoic acid and glutamic acid connected.
Function: Hematopoietic vitamin, tetrahydrofolate (active form) is a coenzyme that delivers one-carbon units.
Deficiency symptoms: megaloblastic anemia, leukopenia.
VB12
Chemical nature: cobalamin, corrin formed around cobalt ions
Properties: Vitamin against pernicious anemia; coenzyme involved in propionic acid metabolism, methyl activation and other biochemical reactions
Function: 1. Vitamin against pernicious anemia 2. Participate in propionic acid metabolism and methyl activation coenzyme
Deficiency symptoms: anemia, numbness of hands and feet, etc.
Active form:
common ground
Mainly constitutes the cofactor of enzyme and directly affects the activity of enzyme.
Dependent on food Excreted in urine Rarely stored
Generally non-toxic Deficiency syndrome
4 types of fat-soluble vitamins
1. Vitamin A
Chemical nature: Retinol
Deficiency symptoms: Night blindness
Existing forms: A1 and A2 (one more than 2 =). A1 animal liver blood retina, A2 fish
Precursor β-carotene (decomposed to obtain 2 molecules of A)
2. Vitamin D
Chemical essence: cyclopentane polyhydrophenanthrene compounds.
Properties: Medium, resistant to high temperature and oxidation under alkaline conditions, gradually decomposes under acidic conditions
Function: Promote calcium absorption in the small intestine
Deficiency symptoms: Rickets (children), osteomalacia (adults)
Existing forms: Vitamin D2, D3, D4, D5, D6, D7
3. Vitamin E
Chemical nature: Tocopherol
Properties: Stable in acid and heat, unstable in alkali
Function: Antioxidant
Deficiency symptoms: Infertility
Existing form:
8 kinds
Alpha tocopherol has the highest biological potency
4. Vitamin K
Chemical nature:: A class of derivatives of 2-methyl-l,4-naphthoquinone
Properties: Thermal stable, photo-alkali sensitive oxidative decomposition
Function: Promote prothrombin synthesis
Deficiency symptoms: Slow blood clotting occurs.
Existing form:
K1,K2,K3
common ground
Hydrophobic compound, easily soluble in lipids and organic solvents
It is combined with lipoproteins or specific binding proteins and transported in the blood. It is not easily excreted and is stored in the liver in the body.
Lipid malabsorption and medium- and long-term deficiency of this vitamin can cause deficiency, and excessive intake can cause poisoning.
lipoic acid
Chemical nature:
lipoic acid
nature:
There are oxidized and reduced forms, both water-soluble and fat-soluble.
Function: Coenzyme transfers hydrogen
Deficiency Symptoms: Deficiency has not been identified yet
Storage and processing changes
storage
Enzymatic degradation, photocatalyzed degradation and oxidative degradation
High temperature and excessive water will cause great damage. Low temperature controlled atmosphere storage
processing
Thermal processing, dehydration, grain finishing, chemical factors acid and alkali