Metabolism - Lecture Twenty-Three Flashcards
Digestion of Food Molecules
Carbohydrates ➝
Monosaccharides
Protein ➝
Amino acids
Nucleic acids ➝
Nucleotides
Fat ➝
Free fatty acids, monoacylglycerols and cholesterol
Salivary glands
Saliva (neutral pH) contains mucous and amylase which start the digestion of carbohydrates
Stomach
Storage and mixing of food with gastric juices, slowly releases chyme into intestine
What does the stomach secrete?
Acid (0.1M HCl)
Pepsinogen ➝ Pepsin = Protein digestion
Pancreas
Slightly alkaline pH 7 which secretes most of the digestive enzymes including amylase, lipase and several proteases
Liver
Synthesis of bile salts/acids (stored in gall bladder) important for fat digestion
Small intestine
Final phase of digestion and absorption
Digestion: first phase
Hydrolysis of bonds connecting monomer units in food macromolecules
Carbohydrate: Glycosidic bonds - starch → disaccharides
Proteins: Peptide bonds
Fat: Triacylglycerol ester bonds
Digestion: second phase
Absorption of products from gastrointestinal tract into body
Digestion of dietary carbohydrates
Provides 40-50% of energy intake
Dietary carbohydrates
Starch, simple sugars and fibre
Amylopectin
Main component of plant starch
Maltose
Present in honey
Cellobiose and lactose
Are stereoisomers of one another
Cellobiose
Repeating disaccharide unit in cellulose
Lactose
Present in milk
Sucrose hydrolysed to
glucose and fructose
Starch from plants consists mainly of
Amylose
Amylopectin
Glycogen
Glycogen has a similar branched structure to amylopectin and can be present in consumed foods
Glycogen synthesis in animals
From glucose and stored in liver and muscles and then broken down to glucose when required by the body
The breakdown of glycogen
Stored in liver and muscle cells to glucose requires a ‘de-branching enzyme’
The enzyme amylase hydrolyses
Alpha (1➝4) glycosidic bonds
Lactose intolerant
Lactase enzyme deficiency causes bloating, flatulence and diarrhoea due to fermentation of factor by intestinal bacteria
Essential amino acids
Leucine Lysine Threonine Isoleucine Methionine Phenylalanine Valine
Protein digestion
Involves hydrolyses of specific peptide bonds and is performed by several different proteases
Protein digestion: proteases secreted
As inactive forms (zymogens and proenzymes)
Protein digestion: proteases activated
By cleavage of peptides from their structure
How is protease specificity determined?
By adjacent amino acid side chains
Pepsin =
Aromatic i.e. Phe and Tyr
Trypsin =
+ charged i.e. Lys and Arg
Chymotrypsin =
Aromatic i.e. Phe and Tyr
Endopeptidases
Attack peptide bonds within the protein polymer e.g. pepsin, trypsin and chymotrypsin
Exopeptidases
Attack peptide bonds at the end of protein polymer e.g. amino peptidases and carboxypeptidase
Pepsinogen
Inactive zymogen (proenzyme) is activated to pepsin following exposure of pepsinogen to HCl in the stomach
In the stomach acidic environment, part of the pepsinogen protein unfolds
This activates the pepsin protease and results in hydrolysis of part of the pepsinogen protein sequence to generate stably activated pepsin proteases