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Download MBBS Biochemistry PPT 61 Ingestion Digestion And Absorption Of Dietary Proteins Lecture Notes

Download MBBS (Bachelor of Medicine, Bachelor of Surgery) 1st year (First Year) Biochemistry ppt lectures Topic 61 Ingestion Digestion And Absorption Of Dietary Proteins Notes. - biochemistry notes pdf, biochemistry mbbs 1st year notes pdf, biochemistry mbbs notes pdf, biochemistry lecture notes, paramedical biochemistry notes, medical biochemistry pdf, biochemistry lecture notes 2022 ppt, biochemistry pdf.

This post was last modified on 05 April 2022

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Department of Biochemistry

Learning Objectives

? Ingestion of Dietary Proteins

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? Digestion of Dietary Proteins
? Absorption of Amino Acids
? Transport of Amino acids
Introduction

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Dietary Protein
? Consists of long chains of amino acids (aa)

? In the digestive process, enzymes in stomach and small

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intestine break down complex protein into polypeptides and

further into individual aa

? aa are absorbed through wall of small intestine, pass into blood

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and further to liver through portal vein

Importance of Dietary Proteins

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? Role of proteins in diet is important for structural component of

cells and tissues.

? Without adequate protein in diet, body cells and tissues not able

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to function.

? Proteins are large, complex molecules made up of smaller aa

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compounds.
Cont--

? Some aa are made by body and are nonessential, but others

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are essential, so we need to get them from diet.

? Therefore, consume protein-rich foods each day, since body

does not have a way to store protein.

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Cont--

? Essential aa: Cannot be

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synthesize in the body so

"essential" to eat them

from dietary food.

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? Non-essential: Body can

synthesize them from

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other proteins so not

essential to eat them

Table 27.1. Harper's Illustrated Biochemistry 30th Edition

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Ingestion of Dietary Proteins

? Ingested dietary proteins is hydrolysed to aa, which are source

of essential aa in blood

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? Absorbed from intestine and utilization of these aa for synthesis

of body proteins ex. Structural proteins, plasma proteins,

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enzymes, milk proteins, hormones

? Also synthesis of necessary non-protein nitrogen compounds

includes urea, uric acid, creatine, creatinine, aa, polypeptides.

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Cont--
? Recommended Dietary allowance (RDA) for both men and

women: 0.8 g of protein/kg body weight/day

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? Dietary proteins: Dietary proteins in our diet are either from

animal source or vegetable source

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? Animal sources: Milk and dairy products, meat, fish, eggs

? Vegetable sources: Cereals, pulses, peas, beans and nuts
Overview of the Digestion of Dietary Proteins

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Marks, Marks and Smith, Medical Biochemistry

Digestion of Dietary Proteins

? Proteins are too large to be absorbed by the intestine, therefore,

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hydrolysed into di- and tripeptides as well as individual aa,

which can be absorbed

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? Proteolytic enzymes responsible for degrading proteins are

produced by three different organs: stomach, pancreas, and

small intestine

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Activation of Gastric and Pancreatic zymogens

? Pepsinogen catalyzes its own

cleavage at the pH of the

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stomach

? Trypsinogen is cleaved by

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enteropeptidase

? Active form of the enzyme

trypsin plays a key role by

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catalysing the cleavage of

other pancreatic zymogens

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Marks, Marks and Smith, Medical Biochemistry

Cont--

Digestion by gastric secretion: Digestion of proteins begins in

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the stomach, which secretes gastric juice, a unique solution

containing hydrochloric acid (HCl) and the proteolytic enzyme

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? Pepsin is a potent proteolytic enzyme and is present in gastric

juices

? It is secreted as inactive zymogen form, pepsinogen.

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Cont--

? It is synthesised in "chief cells" of stomach

? HCl maintains gastric pH at about 1 to 2 and ensures maximum

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pepsin activity

? Optimum pH for pepsin is 1.6 to 2.5 and pepsin gets denatured

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if the pH is greater than 5.

Cont--

? Pepsinogen is hydrolysed

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in stomach with help of

HCl or pepsin itself

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(autocatalytically) to form

the "active" pepsin

? In process of activation (i)

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An inactive peptide called

as "pepsin inhibitor and (ii)

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5 smaller peptides are

liberated.
Cont--

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? Pepsin is a proteinase, a non-specific endopeptidase, and it

hydrolyses peptide bonds inside protein molecule and produces

proteoses and peptones

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? It is particularly active on a peptide bond, which connects the ?

COOH group of an aromatic aa like Phe, Tyr, and Tryp with

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amino group of either a dicarboxylic acid or an aromatic a.a

Cont--

Pepsin also hydrolyse the peptide bonds of:

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COOH group of methionine and leucine
Leucine and glutamic acid
Glutamic acid and asparagine
Leucine-valine
Valine and cysteine

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? Pepsin cannot act on proteins like keratins, Silkfibroins,

mucoproteins, mucoids and protamines
Digestion by pancreatic secretion

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? Optimum pH for activity of pancreatic enzymes (pH 8) provided

by alkaline bile and pancreatic juice.

? Secretion of pancreatic juice is stimulated by peptide hormones,

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Cholecystokinin

Cont--

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? On entering the small intestine, large polypeptides produced in

stomach by action of pepsin are cleaved to oligopeptides and

amino acids

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? Catalyzed by a group of pancreatic proteases that include both

endopeptidases (Trypsin, Chymotrypsin, Elastase) and

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exopeptidases (metalloenzyme, contains zinc).
Digestion by proteolytic enzymes in intestinal juice
Amino-peptidases: Luminal surface of intestinal epithelial cells

contains aminopeptidase, an exopeptidase repeatedly cleaves N-

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terminal residue from oligopeptides to produce smaller peptides

and free aa.

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? Requires Zn++, Mn++ and Mg++ as a cofactor which help in

formation of a metal-enz-substrate coordination complex for

catalysis

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Cont--

? Can hydrolyse a terminal peptide bond connected to an end a.a

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bearing a free- NH2 group and splits off the end a.a. from N-

terminal end of a peptide, changing latter to a "tripeptide"

Tri and Di-peptidases: hydrolyse the peptides at either of two

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places
? In microvil us membrane of intestinal epithelial cells, or inside

epithelial cells after peptides absorbed inside cell

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Cont--

? Tri-peptidase acts on a tri-peptide and produces a di-peptide

and free a.a

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? Di-peptidase hydrolyses a di-peptide to produce two molecules

of aa

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? They require Mn++, Co++ or Zn++ as cofactors for their activity.

Cleavage of dietary protein in small intestine by pancreatic proteases

? Peptide bonds susceptible

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to hydrolysis for each of

the five major pancreatic

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proteases

? First three are serine

endopeptidases, whereas

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last two are exopeptidases

Fig 19.5. Lippincott's Illustrated Reviews, Biochemistry, 6th Ed

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? Each is produced from an

inactive zymogen
Absorption of Amino Acids

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? Free aa are taken into enterocytes by a sodium-linked

secondary transport system of apical membrane.

? Di- and tripeptides, are taken up by a proton-linked transport

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system.

? Peptides are hydrolyzed in cytosol to aa that are released into

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portal system by facilitated diffusion.

Cont--

? Therefore, only free aa are found in portal vein after a meal

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containing protein

? These aa are either metabolized by liver or released into

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general circulation
Absorption of products of protein digestion by carrier protein

transport system

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? AA are absorbed into epithelial cells by

Na+-linked secondary transport via

symporter

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? Various aa are transported by carriers

specific for them

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? AA exit cell at basal membrane via

various passive carriers by facilitated

transporter

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? AA enter the blood by simple diffusion

Marks, Marks and Smith, Medical Biochemistry

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Interaction with students

? Distributed subtopics of class to students for participate in group

discussion in next class.

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Reference Books

1) Text Book of Medical Biochemistry by Chatterjee & Rana

Shinde, 8th Ed

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2) Biochemistry, Lippincott's Il ustrated Reviews, 6th Ed
3) Harper's Il ustrated Biochemistry-30th edition
4) Lehninger Principles of Biochemistry
5) Marks, Marks and Smith, Medical Biochemistry

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27

Thank you

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