Definition of Digestion

1. Digestion

breaking down the food by

mechanical and chemical means
2. Absorption
taking up the soluble digestion
products into the body's cells
3. Assimilation
using the absorbed materials
taking large pieces of food into the body
4. Ingestion
5. Egestion
elimination of material from the
body cavity
[the removal of
undigested semi-solid(feaces)from
your anus]
6. Excretion
elimination of substances from
within body cells
7. Mucous membrane
Moist tissue that lines certain parts
Mucosa(sing)/Mucosa of the inside of your body. It is in
e(plu)
your nose, mouth, lungs, and the
urinary and digestive tracts
.Glands in this tissue release a
thick fluid called mucus.
A layer of loose connective tissue
8. Submucosa
beneath a mucous membrane.
Smooth membrane consisting of
9. Serosa
two layers of epithelial cells (two
membranes of epithelial cells)
which secrete serous fluid.
10.
A large group of enzymes that
catalyze the hydrolysis of peptide
Endopeptidase
bonds in the interior of a

polypeptide chain or protein

molecule. For example: pepsin,
trypsin
11.
Exopeptidases A group of enzymes that catalyze
the hydrolysis of single amino

acids from the end of a polypeptide

chain.
Remove amino acids one by one
from the ends of peptide chains.
12.

Gastric pits

Indentations in the stomach

which denote entrances to the
tubular shaped gastric glands.
13. Gastric juice
Gastric juice is secreted from
gastric glands, which are located in
narrow tube like structures called
gastric pits. Gastric juice contains
hydrochloric acid, pepsinogen and
mucus in a healthy adult.
Hydrochloric acid is secreted by
parietal cells, pepsinogen is
secreted by gastric chief cells and
mucus is secreted by mucus neck
cells.
14.
A protease enzyme that hydrolyzes
Carboxypeptidases (cleaves) a peptide bond at the
carboxy-terminal (C-terminal) end
of a protein or peptide. Most of the
known carboxypeptidases are not
involved in catabolism; they help
to mature proteins (e.g., Post-

15.
Aminopeptidase

16. Zymogens
(proenzyme)

translational modification) or
regulate biological processes. For
example, the biosynthesis of
neuroendocrine peptides such as
insulin requires a
carboxypeptidase.
Carboxypeptidases also function in
blood clotting, growth factor
production, wound healing,
reproduction, and many other
processes.
Catalyze the cleavage of amino
acids from the amino terminus of
protein (N-terminus) or peptide
substrates.
An inactive enzyme precursor.
A zymogen requires a
biochemical change (such as a
hydrolysis reaction revealing
the active site, or changing the
configuration to reveal the
active site) for it to become an
active enzyme. The biochemical
change usually occurs in a
lysosome where a specific part of
the precursor enzyme is cleaved in
order to activate it. The
inactivating piece which is cleaved
off can be a peptide unit, or can be
independently folding domains
comprising more than 100
residues. Although they limit the
enzyme's ability, these n-terminal
extensions of the enzyme or a
prosegment often aid in the

stabilizing and folding of the

enzyme they inhibit. The
pancreas secretes zymogens
partly to prevent the enzymes
from digesting proteins in the
cells in which they are
synthesised. Enzymes like
pepsin are created in the form
of pepsinogen, an inactive
zymogen. Pepsinogen is
activated when chief cells
release it into HCl which
partially activates it. Another
partially activated pepsinogen
completes the activation by
removing the peptide turning
the pepsinogen into pepsin.
Accidental activation of zymogens
can happen when the secretion
duct in the pancreas is blocked by
a gallstone resulting in acute
pancreatitis . Fungi also
secrete digestive enzymes into the
environment as zymogens. The
external environment has a
different pH than inside the fungal
cell and this changes the
zymogen's structure into an active
enzyme.

17.
Hypha
Hyphae(plu)

18.

Rhizoid