FACULTY OF HEALTH SCIENCES

PROFESSIONAL SCHOOL OF OBSTETRICS

BIOCHEMISTRY

Lactase Enzyme

Teacher:

Q. F. Roger Esquivel Reyna

Alumna:

Majuan Alberca María Elizabeth

Cycle:

II cycle - Section A

Piura–2017
 Index

Resumen

Introduction

I. Methodological Framework
[Link]
[Link]
[Link]
II. Theoretical Framework
[Link]: Mechanism of action.
[Link] importance of enzymes.
[Link] enzyme: composition.
2.3.1. Producción de lactasa en el organismo.
2.3.2. Why is the enzyme lactase important?
[Link] intolerance: Symptoms and causes.
2.4.1. Types of Intolerance

Attachments

Bibliographic References
 Summary

Like many other disciplines, biochemistry is a science of the chemical basis of life.
In this way, it is also feasible to describe biochemistry as the science of the constituents.
chemicals of living cells, and of the reactions and processes they undergo. A close
The relationship between biochemistry and medicine has stimulated mutual advances. The present
monograph, therefore complete as a research paper in the field of health: The enzyme
lactase. Enzymes are biological polymers that catalyze the chemical reactions that they conduct.
possible life as we know it. The commonly used names for almost all the
enzymes describe the type of catalyzed reaction, followed by the suffix -ase. Thus, for example,
las deshidrogenasas eliminan átomos de hidrogeno, las proteasas hidrolizan proteínas. Los
modifiers can precede or follow the name to indicate the substrate, the source of the
enzyme or a characteristic of the mechanism of action. The presence and maintenance of a
A complete and balanced set of enzymes is essential for the breakdown of nutrients.
in order to provide energy. The metabolism of a process with high requirements for the
life makes use of enzymes. Similarly, nutrition, digestion, and absorption of nutrients is done
requerimiento de varios grupos de enzimas que catalizan estos procesos. A cierto nivel, enzimas
located at the brush border of the intestinal mucosal cells absorb the
monosaccharides resulting from enzyme catalysis. Thus, for example, lactase is an enzyme.
produced in the small intestine, which plays a vital role in the breakdown of lactose into
its two basic components: glucose and galactose. The ability to evaluate the activity of
enzymes in the blood help in the diagnosis and prognosis of diseases. Deficiencies of
The amount or the catalytic activity of key enzymes can arise due to genetic defects.
nutritional deficit or toxins. Rarely, congenital lactase deficiency occurs in infants, which
what leads to lactose intolerance and lack of growth and development when they are fed
with breast milk or formula for normal infants.
 Introduction

Lactose is a disaccharide composed of glucose and galactose, linked by a beta-1,4 bond. It is the
the principal sugar in the milk of mammals and the only free carbohydrate in it in quantity
considerable. For its absorption, it must be hydrolyzed in the small intestine by the enzyme
lactase, located in the brush border cell. However, some people develop a
intolerance based on metabolic disorders that prevent its digestion. It rarely occurs
congenital lactase deficiency in infants, leading to lactose intolerance and lack of
growth and development when fed with breast milk. Lactose intolerance
it causes diarrhea and intestinal discomfort when lactose is consumed. It can also be
secondary to mucosal intestinal damage.
 I. Methodological Framework
1.1 Objetivos
Briefly summarize the importance of enzymes in human health.
Indicate the composition, mechanisms of action, uses, and application of enzymes.
Explain the composition of the enzyme lactase and its location in the body.
Describe the digestion and absorption of lactose in the body.
Describe the symptoms of lactose intolerance.
1.2 Background

Since the time of Galen, over 2000 years ago, it is known that milk can induce
diarrhea and other gastrointestinal symptoms in certain people. The first
Observations that lactose caused diarrhea in dogs date back to 1860, and it was in 1958 when
Durand described that lactose intolerance was associated with chronic diarrhea in the infant.
Subsequent studies confirmed that this malabsorption was due to a 'deficiency of the
enzymes that break down sugars" and in 1963 the first observations were published about
lactose malabsorption in adults. Currently, it is estimated that two-thirds of
the global population exhibits lactose intolerance, with a very variable distribution among
the different races and geographical areas, and even among subpopulations and tribes.

Children suspected of lactose intolerance can be clinically evaluated through

the elimination of lactose in the diet or the conduct of non-invasive tests such as the one of
expired hydrogen or invasive methods such as the determination of lactase concentration (and others
disaccharides) in the intestinal biopsy.

1.3 Definiciones
Enzymes are protein catalysts that increase the speed of a reaction.
chemistry and that are not consumed during the reaction they catalyze.
Enzymes are the most efficient catalysts known: Most of the
Reactions that are catalyzed by enzymes proceed at a speed of 10.3a 108times
greater than the uncatalyzed reactions,
The enzymes that catalyze the conversion of one or more compounds (substrates) into one
or more different compounds (products). That is to say, they are effective and very catalysts.
specific.
II. Theoretical Framework

2.1 Enzymes: Mechanism of Action.

Enzymes are highly specific, even to the extent of being able to distinguish between
stereoisomers of a given compound. Some enzymes act only with the part
protein. Others, however, require the presence of others to function properly.
non-protein molecules called cofactors. In this latter case, the enzymes are called
holoenzymes and the protein part apoenzyme.
Enzymatic molecules contain a special pocket or groove called the active site. The site
fixed to the substrate, and forms the enzyme-substrate complex. This complex turns into a
enzyme and product complex, which then dissociates from these two components. (Annex 01)

The active site is not a passive receptacle for substrate binding but rather a device.
complete molecular that occurs to a diversity of chemical mechanisms to facilitate the conversion
from substrate to product. The enzymatic action mechanism can be considered from two
different perspectives. The first is related to catalysis, necessarily a reaction pathway.
energetically favorable different from the uncatalyzed reaction. The second perspective describes
the way in the active site facilitates chemical catalysis.

2.2 Medical importance of enzymes.

The ability to assess the activity of specific enzymes in the blood and other fluids.
Histological or cell extracts help in the diagnosis and prognosis of disease.
deficiencies in the amount or catalytic activity of key enzymes may occur due to
genetic defects, nutritional deficiency, or toxins. Medical scientists address imbalances
from the activity of enzymes when using drugs to inhibit specific enzymes and are
investigating gene therapy as a means to correct enzyme concentration deficiency
or the function of them. Enzymes are one of the classes of biomolecules directed
for the creation of drugs and other therapeutic agents, for example, many antibiotics
they inhibit enzymes that are unique to pathogenic microbes. Similarly, the analysis of
enzymes in blood plasma have played a fundamental role in diagnosis of
various morbid processes. Many enzymes are functional constituents of the blood, among
some examples of lipase protein, some groups of enzymes serve as markers for the
diagnosis of diseases. (Annex 02)

2.3 Lactase enzyme: composition.

It belongs to the family of disaccharidases, which are the enzymes responsible for breaking down the
disaccharides into the monosaccharides that make them up. Lactase is a type of β-galactosidase,
also called beta-gal and b-gal, is an enzyme that catalyzes the hydrolysis of glycosides to
monosaccharides. A galactoside is composed of a glycoside that contains galactose. It is
to say, the hydrogen from the hydroxyl group of carbon 1 of galactose is replaced by a residue
organic. Depending on the glycosidic bond between galactose and the organic rest, the
Galactosides are classified as α-galactosides or β-galactosides. The most common β-galactoside is the
lactose, a disaccharide between galactose and glucose (β 1,4 Galactose-Glucose). (Annex 03)

It is a protein enzyme that acts as an enzyme, produced in the small intestine, that plays a
vital role in the unfolding of lactose (a process necessary for its absorption by our
organism) in its two basic components: glucose and galactose. If the levels of lactase are
Low or this does not perform its job well, difficulties in digesting lactose appear.

2.3.1 Lactase production in the body.

Lactase is a digestive enzyme and is produced in the brush border of the cells that
they cover the intestinal villi (enterocytes), with maximum activity in the jejunum and ileum
proximal. The gene responsible for directing the production of lactase is called the LCT gene and is
located at position 21 of the long arm of chromosome 2.
 2.3.2 Why is the enzyme lactase important?

When the lactase in the intestinal mucosa is deficient, digestion cannot take place.
normal lactose, which accumulates in excessive amounts in the intestinal lumen, although
a small proportion, possibly less than 10%, is absorbed intact by passive diffusion
and finally excreted in the urine, most of the lactose passes into the colon where
again a minimal part is hydrolyzed to monosaccharides by bacterial lactase, but the
remaining amount undergoes fermentation with the production of low molecular weight organic acids
molecular and gas formation. The osmotic effect of these metabolic products is the cause of
an increase in intraluminal flow and consequently an acidic watery diarrhea, whose
intensity will depend on the load of lactose and the degree of lactase deficiency, considered
quantitatively.

2.4 Lactose intolerance: Symptoms and causes.

The clinical manifestations are directly related to the presence of sugars not
digested in the intestinal lumen, as well as with the time that has elapsed since ingestion of
lactose. Therefore, the first clinical manifestations occur around
the first 2 hours after the intake of milk or products containing lactose, since it is the
calculated time it takes for sugars to reach the colon.

In the infant, there is malabsorption of fats and proteins while the condition is present.
and therefore puts their nutritional status at risk. Babies' bodies produce this
enzyme, in such a way that they can digest milk, including breast milk. Babies
premature infants sometimes have lactose intolerance. Term-born children
They generally do not show signs of this intolerance until they are at least 3 years old.
Lactose intolerance can begin at various times in life.

Dehydration is, however, one of the risks of this ailment that can greatly affect
Infants and young children due to diarrhea can lead to significant impairment.
from the pondoestatural curve.

2.4.1 Types of Intolerance

Secondary intolerance (majority): The decrease in lactose production
it is secondary, since it is caused by a temporary intestinal damage (generally
caused by a viral gastroenteritis). This type of intolerance is very common in the
childhood after an episode of acute gastroenteritis.
Primary or genetic intolerance (minority): It results in a progressive loss of
the production of lactase, and therefore a gradual loss of the ability to digest the
milk. It usually occurs throughout life in certain ethnic groups and has a cause.
genetics. People with this intolerance notice how the intake of milk affects them.
causes more and more symptoms.

The absence of congenital lactase (at birth) is extremely rare, as up until now
little was incompatible with life. Generally, in the first year of life, we possess the greatest
ability to digest lactose.
Annexes

Annex 01

Annex 02

Annex 03

Bibliographic References

Munrray, R. Bioquímica de Harper. 14ª Ed. Editorial El Manual Moderno. 1997.