This document discusses proteases, which are enzymes that catalyze the breakdown of proteins. It describes the seven main classes of proteases based on their catalytic residue: serine, cysteine, threonine, aspartic, glutamic, metallo, and asparagine peptide lyases. Each class is explained along with examples. The document also covers protease structure, classification based on pH, mechanisms of action, and various industrial and medical uses of proteases.
Proteases: Introduction, activation, catalytic mechanism, different sources (Plants,animals and microbial), physiological functions,industrial applications and clinical applications. References
Institute of Industrial Biotechnology, Government College University, Lahore (Pakistan)
Proteases: Introduction, activation, catalytic mechanism, different sources (Plants,animals and microbial), physiological functions,industrial applications and clinical applications. References
Institute of Industrial Biotechnology, Government College University, Lahore (Pakistan)
Coenzyme - Introduction, Definition, Examples for coenzyme, reaction catalysed by coenzyme, Types of coenzymes - cosubstrate and prosthetic group coenzymes, second type of classification of coenzyme- hydrogen group transfer , other than hydrogen group transfer.
Enzymes principles and applications Likhith KLIKHITHK1
Enzymes are biological catalysts (also known as biocatalysts) that speed up biochemical reactions in living organisms. They can also be extracted from cells and then used to catalyse a wide range of commercially important processes. For example, they have important roles in the production of sweetening agents and the modification of antibiotics, they are used in washing powders and various cleaning products, and they play a key role in analytical devices and assays that have clinical, forensic and environmental applications. The word ‘enzyme’ was first used by the German physiologist Wilhelm Kühne in 1878, when he was describing the ability of yeast to produce alcohol from sugars, and it is derived from the Greek words en (meaning ‘within’) and zume (meaning ‘yeast’).In the late nineteenth century and early twentieth century, significant advances were made in the extraction, characterization and commercial exploitation of many enzymes, but it was not until the 1920s that enzymes were crystallized, revealing that catalytic activity is associated with protein molecules. For the next 60 years or so it was believed that all enzymes were proteins, but in the 1980s it was found that some ribonucleic acid (RNA) molecules are also able to exert catalytic effects.These RNAs, which are called ribozymes, play an important role in gene expression. In the same decade, biochemists also developed the technology to generate antibodies that possess catalytic properties. These so-called ‘abzymes’ have significant potential both as novel industrial catalysts and in therapeutics. Notwithstanding these notable exceptions, much of classical enzymology, and the remainder of this essay, is focused on the proteins that possess catalytic activity.As catalysts, enzymes are only required in very low concentrations, and they speed up reactions without themselves being consumed during the reaction.
In this ppt the viewer will able to know about PEPSIN Enzyme. It is the enzyme prepared from the mucous membrane of the stomach of various animals like pig, sheep, or calf. The commonly used species of pig is Sus scrofa Linn, belonging to family Suidae. The stomach consists of an outer muscular layer and an inner mucous layer. The inner surface is covered with a single layer of epithelial cells which also lines the piths present on them. The piths are about 0.2 mm in diameter, and each pith has two to three narrow tubular ducts opening at the base. The epithelial layer is made of either the parietal cell or the central cell. The central cells are mainly covered with almost cubical shape and secrete pepsinogen and rennin zymogen, whereas the parietal cells are round or oval shaped cells, and they secrete the hydrochloric acid to activate the zymogen to produce rennin and pepsin.
•
Portion explained:
Biological Source of Diastase Enzyme
Preparation of Diastase Enzyme
Description of Diastase Enzyme
Uses of Diastase Enzyme
An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process. The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes
IOSR Journal of Pharmacy and Biological Sciences(IOSR-JPBS) is an open access international journal that provides rapid publication (within a month) of articles in all areas of Pharmacy and Biological Science. The journal welcomes publications of high quality papers on theoretical developments and practical applications in Pharmacy and Biological Science. Original research papers, state-of-the-art reviews, and high quality technical notes are invited for publications.
Coenzyme - Introduction, Definition, Examples for coenzyme, reaction catalysed by coenzyme, Types of coenzymes - cosubstrate and prosthetic group coenzymes, second type of classification of coenzyme- hydrogen group transfer , other than hydrogen group transfer.
Enzymes principles and applications Likhith KLIKHITHK1
Enzymes are biological catalysts (also known as biocatalysts) that speed up biochemical reactions in living organisms. They can also be extracted from cells and then used to catalyse a wide range of commercially important processes. For example, they have important roles in the production of sweetening agents and the modification of antibiotics, they are used in washing powders and various cleaning products, and they play a key role in analytical devices and assays that have clinical, forensic and environmental applications. The word ‘enzyme’ was first used by the German physiologist Wilhelm Kühne in 1878, when he was describing the ability of yeast to produce alcohol from sugars, and it is derived from the Greek words en (meaning ‘within’) and zume (meaning ‘yeast’).In the late nineteenth century and early twentieth century, significant advances were made in the extraction, characterization and commercial exploitation of many enzymes, but it was not until the 1920s that enzymes were crystallized, revealing that catalytic activity is associated with protein molecules. For the next 60 years or so it was believed that all enzymes were proteins, but in the 1980s it was found that some ribonucleic acid (RNA) molecules are also able to exert catalytic effects.These RNAs, which are called ribozymes, play an important role in gene expression. In the same decade, biochemists also developed the technology to generate antibodies that possess catalytic properties. These so-called ‘abzymes’ have significant potential both as novel industrial catalysts and in therapeutics. Notwithstanding these notable exceptions, much of classical enzymology, and the remainder of this essay, is focused on the proteins that possess catalytic activity.As catalysts, enzymes are only required in very low concentrations, and they speed up reactions without themselves being consumed during the reaction.
In this ppt the viewer will able to know about PEPSIN Enzyme. It is the enzyme prepared from the mucous membrane of the stomach of various animals like pig, sheep, or calf. The commonly used species of pig is Sus scrofa Linn, belonging to family Suidae. The stomach consists of an outer muscular layer and an inner mucous layer. The inner surface is covered with a single layer of epithelial cells which also lines the piths present on them. The piths are about 0.2 mm in diameter, and each pith has two to three narrow tubular ducts opening at the base. The epithelial layer is made of either the parietal cell or the central cell. The central cells are mainly covered with almost cubical shape and secrete pepsinogen and rennin zymogen, whereas the parietal cells are round or oval shaped cells, and they secrete the hydrochloric acid to activate the zymogen to produce rennin and pepsin.
•
Portion explained:
Biological Source of Diastase Enzyme
Preparation of Diastase Enzyme
Description of Diastase Enzyme
Uses of Diastase Enzyme
An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process. The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes
IOSR Journal of Pharmacy and Biological Sciences(IOSR-JPBS) is an open access international journal that provides rapid publication (within a month) of articles in all areas of Pharmacy and Biological Science. The journal welcomes publications of high quality papers on theoretical developments and practical applications in Pharmacy and Biological Science. Original research papers, state-of-the-art reviews, and high quality technical notes are invited for publications.
Protein Structure, Post Translational Modifications and Protein FoldingSuresh Antre
Post-translational modifications (PTMs) are covalent processing events that change the properties of a protein by proteolytic cleavage or by addition of a modifying group to one or more amino acids.
Protein post-translational modification (PTM) plays an essential role in various cellular processes that modulates the physical and chemical properties, folding, conformation, stability and activity of proteins, thereby modifying the functions of proteins
This file is all about protein, its composition, functions, metabolism, importance in body, degradation and ways involved, as well as secretion with post transitional changes
structure of proteins
definition of Digestion
sources of Proteins --> EXOGENEOUS SOURCES 50-100g/day and ENDOGENEOUS SOURCES 30-100g/day
Proteins DEGRADED BY --> HYDROLASES specifically PEPTIDASES(ENDOPEPTIDASES & EXOPEPTIDASES)
1. Gastric Digestion of Proteins
2. Pancreatic Digestion of Proteins
3. Digestion of Proteins by Small Intestine Enzymes
Absorption of Amino ACids by Na+Dependent, Na+ Independent, Meister Cycle or gama-glutamyl cycle
THE IMPORTANCE OF MARTIAN ATMOSPHERE SAMPLE RETURN.Sérgio Sacani
The return of a sample of near-surface atmosphere from Mars would facilitate answers to several first-order science questions surrounding the formation and evolution of the planet. One of the important aspects of terrestrial planet formation in general is the role that primary atmospheres played in influencing the chemistry and structure of the planets and their antecedents. Studies of the martian atmosphere can be used to investigate the role of a primary atmosphere in its history. Atmosphere samples would also inform our understanding of the near-surface chemistry of the planet, and ultimately the prospects for life. High-precision isotopic analyses of constituent gases are needed to address these questions, requiring that the analyses are made on returned samples rather than in situ.
Slide 1: Title Slide
Extrachromosomal Inheritance
Slide 2: Introduction to Extrachromosomal Inheritance
Definition: Extrachromosomal inheritance refers to the transmission of genetic material that is not found within the nucleus.
Key Components: Involves genes located in mitochondria, chloroplasts, and plasmids.
Slide 3: Mitochondrial Inheritance
Mitochondria: Organelles responsible for energy production.
Mitochondrial DNA (mtDNA): Circular DNA molecule found in mitochondria.
Inheritance Pattern: Maternally inherited, meaning it is passed from mothers to all their offspring.
Diseases: Examples include Leber’s hereditary optic neuropathy (LHON) and mitochondrial myopathy.
Slide 4: Chloroplast Inheritance
Chloroplasts: Organelles responsible for photosynthesis in plants.
Chloroplast DNA (cpDNA): Circular DNA molecule found in chloroplasts.
Inheritance Pattern: Often maternally inherited in most plants, but can vary in some species.
Examples: Variegation in plants, where leaf color patterns are determined by chloroplast DNA.
Slide 5: Plasmid Inheritance
Plasmids: Small, circular DNA molecules found in bacteria and some eukaryotes.
Features: Can carry antibiotic resistance genes and can be transferred between cells through processes like conjugation.
Significance: Important in biotechnology for gene cloning and genetic engineering.
Slide 6: Mechanisms of Extrachromosomal Inheritance
Non-Mendelian Patterns: Do not follow Mendel’s laws of inheritance.
Cytoplasmic Segregation: During cell division, organelles like mitochondria and chloroplasts are randomly distributed to daughter cells.
Heteroplasmy: Presence of more than one type of organellar genome within a cell, leading to variation in expression.
Slide 7: Examples of Extrachromosomal Inheritance
Four O’clock Plant (Mirabilis jalapa): Shows variegated leaves due to different cpDNA in leaf cells.
Petite Mutants in Yeast: Result from mutations in mitochondrial DNA affecting respiration.
Slide 8: Importance of Extrachromosomal Inheritance
Evolution: Provides insight into the evolution of eukaryotic cells.
Medicine: Understanding mitochondrial inheritance helps in diagnosing and treating mitochondrial diseases.
Agriculture: Chloroplast inheritance can be used in plant breeding and genetic modification.
Slide 9: Recent Research and Advances
Gene Editing: Techniques like CRISPR-Cas9 are being used to edit mitochondrial and chloroplast DNA.
Therapies: Development of mitochondrial replacement therapy (MRT) for preventing mitochondrial diseases.
Slide 10: Conclusion
Summary: Extrachromosomal inheritance involves the transmission of genetic material outside the nucleus and plays a crucial role in genetics, medicine, and biotechnology.
Future Directions: Continued research and technological advancements hold promise for new treatments and applications.
Slide 11: Questions and Discussion
Invite Audience: Open the floor for any questions or further discussion on the topic.
Nutraceutical market, scope and growth: Herbal drug technologyLokesh Patil
As consumer awareness of health and wellness rises, the nutraceutical market—which includes goods like functional meals, drinks, and dietary supplements that provide health advantages beyond basic nutrition—is growing significantly. As healthcare expenses rise, the population ages, and people want natural and preventative health solutions more and more, this industry is increasing quickly. Further driving market expansion are product formulation innovations and the use of cutting-edge technology for customized nutrition. With its worldwide reach, the nutraceutical industry is expected to keep growing and provide significant chances for research and investment in a number of categories, including vitamins, minerals, probiotics, and herbal supplements.
Richard's aventures in two entangled wonderlandsRichard Gill
Since the loophole-free Bell experiments of 2020 and the Nobel prizes in physics of 2022, critics of Bell's work have retreated to the fortress of super-determinism. Now, super-determinism is a derogatory word - it just means "determinism". Palmer, Hance and Hossenfelder argue that quantum mechanics and determinism are not incompatible, using a sophisticated mathematical construction based on a subtle thinning of allowed states and measurements in quantum mechanics, such that what is left appears to make Bell's argument fail, without altering the empirical predictions of quantum mechanics. I think however that it is a smoke screen, and the slogan "lost in math" comes to my mind. I will discuss some other recent disproofs of Bell's theorem using the language of causality based on causal graphs. Causal thinking is also central to law and justice. I will mention surprising connections to my work on serial killer nurse cases, in particular the Dutch case of Lucia de Berk and the current UK case of Lucy Letby.
Multi-source connectivity as the driver of solar wind variability in the heli...Sérgio Sacani
The ambient solar wind that flls the heliosphere originates from multiple
sources in the solar corona and is highly structured. It is often described
as high-speed, relatively homogeneous, plasma streams from coronal
holes and slow-speed, highly variable, streams whose source regions are
under debate. A key goal of ESA/NASA’s Solar Orbiter mission is to identify
solar wind sources and understand what drives the complexity seen in the
heliosphere. By combining magnetic feld modelling and spectroscopic
techniques with high-resolution observations and measurements, we show
that the solar wind variability detected in situ by Solar Orbiter in March
2022 is driven by spatio-temporal changes in the magnetic connectivity to
multiple sources in the solar atmosphere. The magnetic feld footpoints
connected to the spacecraft moved from the boundaries of a coronal hole
to one active region (12961) and then across to another region (12957). This
is refected in the in situ measurements, which show the transition from fast
to highly Alfvénic then to slow solar wind that is disrupted by the arrival of
a coronal mass ejection. Our results describe solar wind variability at 0.5 au
but are applicable to near-Earth observatories.
2. •A protease (also called a peptidase or proteinase) is
an enzyme that catalyzes (increases the rate of) proteolysis,
the breakdown of proteins into smaller polypeptides or
single amino acids. They do this by cleaving the peptide
bonds within proteins by hydrolysis, a reaction where water
breaks bonds.
•Proteases are involved in many biological functions,
including digestion of ingested proteins, protein
catabolism (breakdown of old proteins), and cell signaling.
•Proteases can be found in all forms of life and viruses.
•Without additional helping mechanisms, proteolysis would be
very slow, taking hundreds of years.
4. Classification-
1.Serine proteases - (using a serine alcohol)- Serine proteases (or serine
endopeptidases) are enzymes that cleave peptide bonds in proteins, in
which serine serves as the nucleophilic amino acid at the (enzyme's) active site. They
are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into
two broad categories based on their structure: chymotrypsin-like (trypsin-like)
or subtilisin-like.
Uses-1.Coagulation factor levels may be required in the diagnosis of hemorrhagic or
thrombotic conditions.2.Fecal elastase is employed to determine the exocrine activity of
the pancreas, e.g., in cystic fibrosis or chronic pancreatitis.3.Serum prostate-specific
antigen is used in prostate cancer screening, risk stratification, and post-treatment
monitoring.4.Serine protease, as released by mast cells, is an important diagnostic
marker for type 1 hypersensitivity reactions (e.g. anaphylaxis). More useful than
e.g. histamine due to the longer half-life, meaning it remains in the system for a
clinically useful length of time.
5. 2.Cysteine proteases - (using a cysteine thiol) It is also known as thiol
proteases. They are enzymes that degrade proteins.
These proteases share a common catalytic mechanism that involves
a nucleophilic cysteine thiol in a catalytic triad or dyad. They are found
in fruits including the papaya, pineapple, fig and kiwifruit. The
proportion of protease tends to be higher when the fruit is unripe.
Cysteine proteases are used as an ingredient in meat tenderizers.
This protease classification system counts 14 superfamilies.
Uses- 1.In plants they are important in growth and development and in
accumulation and mobilization of storage proteins such as in seeds.
2. they are involved in signalling pathways and in the response
to biotic and abiotic stresses.
3. They are responsible for senescence and apoptosis (programmed cell
death), MHC class II immune responses, prohormone processing,
and extracellular matrix remodeling important to bone development.
4. They may also lead to accelerated collagen and elast in degradation at
sites of inflammation in diseases such as atherosclerosis and emphysema.
6. 5. They are resistance to acid digestion, allowing possible oral
administration.
6. They are used as a feed additives for livestock to improve the
digestibility of proteins and nucleic acids.
7. In several traditional medicines, the fruits or latex of the papaya,
pineapple and fig are widely used for treatment of intestinal
worm infections both in humans and livestock.
7. 3.Threonine proteases - (using a threonine secondary alcohol)-
Threonine proteases are a family of proteolytic enzymes harbouring
a threonine (Thr) residue within the active site. The prototype members
of this class of enzymes are the catalytic subunits of the proteasome,
however the acyltransferases convergently evolved the same active
site geometry and mechanism.
Five families belonging to two separate superfamilies are currently
recognised.
8. 4.Aspartic proteases - (using an aspartate carboxylic acid)
Aspartic proteases are a catalytic type
of protease enzymes that use an activated water molecule
bound to one or more aspartate residues for catalysis of their
peptide substrates. Eukaryotic aspartic proteases
include pepsins, cathepsins, and renins.
Five superfamilies (clans) of aspartic proteases are known,
each representing an independent evolution of the same active
site and mechanisms.
9. 5.Glutamic proteases - (using a glutamate carboxylic acid)
Glutamic proteases are a group
of proteolytic enzymes containing a glutamic acid residue
within the active site. This group of proteases are found
primarily in pathogenic fungi affecting plant and human.
Structure contain the active site of a catalytic dyad, glutamic
acid (E) and glutamine (Q), which give rise to the
name eqolisin. There are two independent families of glutamic
proteases (G1 and G2).
10. 6.Metalloproteases - (using a metal, usually zinc)
A metalloproteinase, or metalloprotease, is
any protease enzyme whose catalytic mechanism involves
a metal. It plays a significant role in the fusion of muscle cells
during embryo development, in a process known
as myogenesis.
Their are two types
1.Exopeptidases, metalloexopeptidases.
2. Endopeptidases, metalloendopeptidases
11. 7.Asparagine peptide lyases - using an asparagine to perform
an elimination reaction (not requiring water)
Asparagine peptide lyase are one of the seven groups in
which proteases, also termed proteolytic enzymes, peptidases,
or proteinases, are classified according to their catalytic
residue.
Types- Viral coat proteins
Autotransporter proteins
Intein-containing proteins
12. Classification based on optimal pH.
Alternatively, proteases may be classified by the optimal pH in
which they are active:
1.Acid proteases
2.Neutral proteases involved in type 1 hypersensitivity. Here,
it is released by mast cells and causes activation.
of complement and kinins. This group includes the calpains.
3.Basic proteases (or alkaline proteases)
13. Mechanisms:
1.Aspartic, glutamic and metallo- proteases activate a water
molecule which performs a nucleophilic attack on the peptide
bond to hydrolyse it.
2.Serine, threonine and cysteine proteases use a nucleophilic
residue (usually in a catalytic triad). That residue performs a
nucleophilic attack to covalently link the protease to the
substrate protein, releasing the first half of the product. This
covalent acyl-enzyme intermediate is then hydrolysed by
activated water to complete catalysis by releasing the second
half of the product and regenerating the free enzyme.
14.
15. Uses
1.Proteases are involved in digesting long protein chains into shorter
fragments by splitting the peptide bonds that link amino acid residues.
Some detach the terminal amino acids from the protein chain
(exopeptidases, such as aminopeptidases, carboxypeptidase A); others
attack internal peptide bonds of a protein (endopeptidases, such
as trypsin, chymotrypsin, pepsin, papain, elastase).
2. laundry detergents.
3. in the bread industry in bread improver. for quicker preparation of
dough, its gluten is partially hydrolyzed by a heat-labile fungal protease
because of its early inactivation in subsequent baking.
4. A variety of proteases are used medically both for their native
function (e.g. controlling blood clotting) or for completely artificial
functions (e.g. for the targeted degradation of pathogenic proteins).
5. Highly specific proteases such as TEV protease and thrombin are
commonly used to cleave fusion proteins and affinity tags in a controlled
fashion.
ation
16. 6. In the food industry, proteases are utilized for modification,
palatability, and storage life of all available sources of proteins.
7. In meat tenderiz
8.Food and Feed Industry-During cheese production from
milk, proteases are added to hydrolyze kappa casein to prevent
coagulation by stabilizing micelle formation.
9. pharmaceutical drug formations.
10. fortification of soft drinks and juices
11. Waste Management
12. Leather Industry-in the soaking, bating, and dehairing phase of
preparing skin and hides.