What type of bonds do amylases hydrolyze in starch?
→ α(1 → 4) glycosidic bonds
What are the products of starch digestion by amylases?
→ Maltose, maltotriose, and dextrins
What enzyme breaks down maltose at the brush border?
→ Maltase
What two enzymes are combined in sucrase-isomaltase?
→ Sucrase and isomaltase
What enzyme deficiency causes lactose intolerance?
→ Lactase deficiency
How are glucose and galactose absorbed in the intestine?
→ Sodium-dependent transport by SGLT1
How is fructose absorbed in the intestine?
→ Carrier-mediated diffusion (GLUT)
What happens when large amounts of fructose or sugar alcohols remain unabsorbed in the intestine?
→ Osmotic diarrhea
What happens to lactase activity in most humans after weaning?
→ It declines
Which populations retain lactase activity into adulthood?
→ Northern Europeans and nomadic African/Arab tribes
What are the major lipids in the diet?
→ Triacylglycerols (main), phospholipids (minor)
Why must lipids be emulsified before absorption?
→ Lipids are hydrophobic and need to be broken into small droplets (micelles) to be absorbed in a watery environment.
What are the end products of pancreatic lipase digestion?
→ 2-monoacylglycerols and free fatty acids
How do bile salts aid lipid absorption?
→ They emulsify fats into micelles for transport through the watery intestinal environment.
Where are bile salts reabsorbed?
→ Ileum (enterohepatic circulation)
What enzyme requires colipase for activation?
→ Pancreatic lipase
How do plant sterols lower cholesterol levels?
→ They compete with cholesterol for esterification, leading to increased excretion of unesterified cholesterol.
Where are long-chain fatty acids absorbed?
→ Repackaged into chylomicrons → absorbed into lymphatics
What inhibits pancreatic lipase and is used to treat obesity?
→ Orlistat
What happens to short- and medium-chain fatty acids after absorption?
→ Absorbed directly into the hepatic portal vein
What are the two main classes of proteolytic enzymes?
→ Endopeptidases (cut within the protein chain) and Exopeptidases (cut at the ends of the protein chain).
How is pepsinogen activated into pepsin?
→ By gastric acid and active pepsin in the stomach.
What enzyme activates trypsinogen into trypsin?
→ Enteropeptidase (secreted by duodenal epithelial cells).
What is the role of chymotrypsin in protein digestion?
→ Hydrolyzes peptide bonds next to aromatic amino acids.
How are free amino acids absorbed in the intestine?
→ By sodium-dependent active transport.
What enzyme hydrolyzes small peptides at the amino-terminal end?
→ Aminopeptidase.
What type of amino acids does elastase target?
→ Small neutral aliphatic amino acids (e.g., alanine, serine).
What is the role of dipeptidases and tripeptidases?
→ Hydrolyze di- and tripeptides into free amino acids.
What are zymogens, and why are they important?
→ Inactive precursors of proteases; they prevent self-digestion.
What condition results from defective amino acid transporters?
→ Cystinuria — leads to increased excretion of amino acids in urine.
What are the two types of vitamins based on their absorption mechanism?
→ Fat-soluble (via micelles) and water-soluble (via active transport or diffusion)
How is vitamin B12 absorbed in the intestine?
→ Requires intrinsic factor secreted by gastric parietal cells
What role does vitamin D play in calcium absorption?
→ Increases calbindin synthesis and recruits calcium transporters
What compound enhances iron absorption by reducing Fe³⁺ to Fe²⁺?
→ Vitamin C
What protein regulates iron absorption by blocking ferroportin?
→ Hepcidin
Why can high fat intake impair calcium absorption?
→ Forms insoluble calcium soaps with fatty acids
What dietary factors reduce calcium absorption?
→ Phytic acid and oxalates
What happens to iron that is not transported into the bloodstream?
→ Stored in mucosal cells bound to ferritin and lost when cells are shed
Why is iron absorption from meat better than from plants?
→ Heme iron is absorbed separately and more efficiently
How does hypoxia affect iron absorption?
→ Reduces hepcidin production, increasing iron absorption
What is the primary source of energy for the body?
→ Carbohydrates, fats, and proteins
What is the formula for BMI?
→ BMI = weight (kg) ÷ height² (m²)
What is the significance of the respiratory quotient (RQ)?
→ RQ indicates the type of metabolic fuel being used (1.0 = carbs, 0.7 = fats, 0.8 = proteins).
What happens to BMR with age?
→ Decreases due to loss of muscle and increase in fat.
What are the key differences between marasmus and kwashiorkor?
→ Marasmus = calorie deficiency, muscle + fat loss; Kwashiorkor = protein deficiency, edema + fatty liver.
What is diet-induced thermogenesis?
→ Energy used for digestion, absorption, and nutrient storage (~10% of meal energy).
What causes increased energy expenditure in cachexia?
→ Increased protein catabolism, anaerobic glycolysis, and futile lipid cycling.
What is nitrogen balance and how is it calculated?
→ Nitrogen balance = dietary nitrogen intake – nitrogen excretion (mainly in urea).
What are the three states of nitrogen balance?
→ Positive nitrogen balance (intake > output), negative nitrogen balance (intake < output), nitrogen equilibrium (intake = output).
What conditions lead to positive nitrogen balance?
→ Growth, pregnancy, recovery from illness.
What conditions lead to negative nitrogen balance?
→ Trauma, infection, starvation, inadequate protein intake.
How is protein intake calculated from nitrogen intake?
→ mg protein = mg nitrogen × 6.25 (since nitrogen is 16% of protein).
What is the average daily protein requirement for adults?
→ 0.66 g/kg body weight; recommended = 0.825 g/kg body weight (~55 g/day).
Why do athletes not need very high protein intake?
→ Increased energy needs are more important than increased protein intake.
How does high protein intake affect protein turnover?
→ Increases both protein synthesis and protein catabolism, leading to increased diet-induced thermogenesis.
Why do children have higher protein requirements than adults?
→ Due to increased muscle and tissue growth during development.
What is the main form of nitrogen excretion?
→ Urea (via urine).
What are the main hormones involved in protein catabolism after trauma?
→ Cytokines (e.g., IL-1, TNF) and glucocorticoids (e.g., cortisol)
Why does protein breakdown increase after trauma or infection?
→ Increased demand for threonine and cysteine for acute-phase protein synthesis and hormonal response
How much total body protein can be lost in 10 days after severe trauma?
→ 6–7%
What type of nitrogen balance occurs during recovery from trauma?
→ Positive nitrogen balance
Why can't the body maintain protein synthesis if even one essential amino acid is missing?
→ Protein synthesis requires all essential amino acids in the correct proportion
Which two amino acids are synthesized from essential amino acids?
→ Cysteine (from methionine) and tyrosine (from phenylalanine)
What are the three truly dispensable amino acids?
→ Alanine, Aspartate, Glutamate
Why do athletes and bodybuilders not need a high-protein diet?
→ A normal diet providing 14% of energy from protein is enough for muscle synthesis
What happens to protein turnover with a high-protein diet?
→ Both protein synthesis and catabolism increase, maintaining nitrogen balance
Why might some non-essential amino acids become essential during stress or trauma?
→ The body’s ability to synthesize them may be insufficient under stress