The following presentation is only for quick reference. I would advise you to read the theoretical aspects of the respective topic and then use this presentation for your last minute revision. I hope it helps you..!!
Mayur D. Chauhan
Introduction :
Antibiotics are antimicrobial agents produced naturally by other microbes (usually fungi or bacteria)
The first antibiotic was discovered in 1896 by Ernest Duchesne and in 1928 "rediscovered" by Alexander Fleming from the filamentous fungus Penicilium notatum.
The antibiotic substance, named penicillin, was not purified until the 1940s (by Florey and Chain), just in time to be used at the end of the second world war.
Penicillin was the first important commercial product produced by an aerobic, submerged fermentation
The following presentation is only for quick reference. I would advise you to read the theoretical aspects of the respective topic and then use this presentation for your last minute revision. I hope it helps you..!!
Mayur D. Chauhan
Introduction :
Antibiotics are antimicrobial agents produced naturally by other microbes (usually fungi or bacteria)
The first antibiotic was discovered in 1896 by Ernest Duchesne and in 1928 "rediscovered" by Alexander Fleming from the filamentous fungus Penicilium notatum.
The antibiotic substance, named penicillin, was not purified until the 1940s (by Florey and Chain), just in time to be used at the end of the second world war.
Penicillin was the first important commercial product produced by an aerobic, submerged fermentation
AMYLASES AND PROTEASES ARE THE ENZYMES USED A LOT IN FOOD INDUSTRIES FOR THE PRODUCTION OF FOODS. THESE ARE SUPPOSED TO PRODUCE AT A LARGER QUANTITIES IN ORDER TO FULFILL THE DEMANDS FROM THESE INDUSTRIES, THE LARGE SCALE PRODUCTION OF THESE ENZYMES MUST BE CARRIED OUT. THIS METHOD OF LARGER PRODUCTION OF THESE ENZYMES ARE EXPLAINED IN THIS PRESENTATION.
UNIT-5 Protein Engineering: Brief introduction to protein engineering,Use of ...Shyam Bass
UNIT-5 6th Sem B.PHARMA PHARMACEUTICAL BIOTECHNOLOGY)
Protein Engineering: Brief introduction to protein engineering, Use of microbes in industry, Production of enzymes-general considerations, Amylase, Catalase, peroxidase, Lipase Basic principles of genetic engineering
BY- SHYAM BASS
VIRAL VACCINES
Since viruses are intracellular parasites they will grow only within other living cells.
Methods of viral vaccine production:
Cultivation of virus using free living animals
Fertile eggs
Tissue cultures
Objective:
To create a superior enzymes to catalyze the production of high value specific chemicals.
To produce enzyme in large quantities.
Eliminate the need for co factor in enzymatic reaction.
Change substrate binding sites to increase specificity.
Change the thermal tolerance and pH stability.
Increase protein resistance to proteases.
To produce biological compounds.
Investigate how desired mutations can be introduced into a cloned gene
Polymerase chain reaction (PCR)
Polymerase chain reaction (PCR) is a common laboratory technique used to make many copies (millions or billions) of a particular region of DNA.
Immunoglobulins:
The Antibodies or Immunoglobulins are globular proteins present in the serum and tissue fluids. They are produced by the plasma cells (B-cells) and are used in the immune system of the body to neutralize pathogenic microbes or other toxic foreign components.
immunostimulants
Immunomodulators are natural or synthetic materials that regulate the immune system and induce innate and adaptive defense mechanisms. These substances are classified into two types, immunostimulants and immunosuppressants.
Immunostimulants can enhance body's resistance against various infections through increasing the basal levels of immune response.
IMMUNITY:
INTRODUCTION:
Our immune system is essential for our survival.
Without an immune system, our bodies would be open to attack from bacteria, viruses, parasites, and more.
It is our immune system that keeps us healthy as we drift through a sea of pathogens.
1. Type I Hypersensitivity:
Type I hypersensitive reactions are the commonest type among all types which is mainly induced by certain type of antigens i.e. allergens. Actually anaphylaxis means “opposite of protection” and is mediated by IgE antibodies through interaction with an allergen
Hybridoma
Hybridomas are cells that have been engineered to produce a desired antibody in large amounts, to produce monoclonal antibodies.
Monoclonal antibodies can be produced in specialized cells through a technique now popularly known as hybridoma technology.
Hybridoma technology was discovered in 1975 by two scientists, G. Kohler and C. Milstein, were awarded Noble prize for physiology and medicine in 1984.
Genetic Organisation:
All cellular activities are encoded within a cell’s DNA.
The sequence of bases within a DNA molecule represents the genetic information of the cell.
Segments of DNA molecules are called genes, and individual genes contain the instructional code necessary for synthesizing various proteins, enzymes, or stable RNA molecules.
Introduction to Genetic engineering
Process:
Genetic engineering, also called genetic modification or genetic manipulation, is the direct manipulation of an organism's genes using biotechnology.
It is a set of technologies used to change the genetic makeup of cells, including the transfer of genes within and across species boundaries to produce improved or novel organisms.
New DNA is obtained by either isolating and copying the genetic material of interest using recombinant DNA methods or by artificially synthesising the DNA.
elisa
Applications
methods
types
The enzyme-linked immuno sorbent assay (ELISA) is an assay technique designed for detecting and quantifying peptides, proteins, antibodies and hormones.
The ELISA has been used as a diagnostic tool in medicine and plant pathology, as well as a quality-control check in various industries.
The process of the ELISA result in a colored end product which correlates to the amount of analyte present in the original sample.
PREPARATION OF BACTERIAL VACCINES:
Steps involved in killed bacterial vaccine preparation:
1. Selection of an antigen:
The exact strain or strains to be incorporated for preparation of bacterial vaccine.
Eg. Cholera vaccine: smooth strains of the two serological types Inaba and Ogawa
TABC vaccine: O and H antigens in S. typhi and S. paratyphi microorganisms and these organisms also contains Vi antigen.
Each strain is carefully checked for freedom from variation and absence of contaminating organisms.
Biotechnology with reference to pharmaceutical scienceAdarsh Patil
Introduction: Hisory
Biotechnology Biology + Technology
Defn:-
Any Technological application that uses biological system, living organisms, cells, tissues, explants or derivatives thereof, to make or modify products or process for specific uses.
Applications of rdna technology in medicinesAdarsh Patil
Applications of R-DNA Technology in medicines:
Introduction Steps involved in recombinant technology:
DNA fragments coding for proteins of interest are synthesized chemically or isolated from an organism.
These DNA fragments are inserted into an endonuclease cleavage site of the vector that does not inactivate any gene that is required for the vector’s maintenance and selective marker.
The recombinant DNA molecules are then introduced into a host to replicate using the replication origin of the vector.
Biosensers are the integrated receptor transducer device, which is capable of providing selective quantitative or semi-quantitative analytic information using a biological recognition element.
Analytical device.
Contains Biological or Biological derived recognition element to detect specific bio-analyte a transducer to convert a biological signal into an electrical signal.
Honest Reviews of Tim Han LMA Course Program.pptxtimhan337
Personal development courses are widely available today, with each one promising life-changing outcomes. Tim Han’s Life Mastery Achievers (LMA) Course has drawn a lot of interest. In addition to offering my frank assessment of Success Insider’s LMA Course, this piece examines the course’s effects via a variety of Tim Han LMA course reviews and Success Insider comments.
A Strategic Approach: GenAI in EducationPeter Windle
Artificial Intelligence (AI) technologies such as Generative AI, Image Generators and Large Language Models have had a dramatic impact on teaching, learning and assessment over the past 18 months. The most immediate threat AI posed was to Academic Integrity with Higher Education Institutes (HEIs) focusing their efforts on combating the use of GenAI in assessment. Guidelines were developed for staff and students, policies put in place too. Innovative educators have forged paths in the use of Generative AI for teaching, learning and assessments leading to pockets of transformation springing up across HEIs, often with little or no top-down guidance, support or direction.
This Gasta posits a strategic approach to integrating AI into HEIs to prepare staff, students and the curriculum for an evolving world and workplace. We will highlight the advantages of working with these technologies beyond the realm of teaching, learning and assessment by considering prompt engineering skills, industry impact, curriculum changes, and the need for staff upskilling. In contrast, not engaging strategically with Generative AI poses risks, including falling behind peers, missed opportunities and failing to ensure our graduates remain employable. The rapid evolution of AI technologies necessitates a proactive and strategic approach if we are to remain relevant.
The Roman Empire A Historical Colossus.pdfkaushalkr1407
The Roman Empire, a vast and enduring power, stands as one of history's most remarkable civilizations, leaving an indelible imprint on the world. It emerged from the Roman Republic, transitioning into an imperial powerhouse under the leadership of Augustus Caesar in 27 BCE. This transformation marked the beginning of an era defined by unprecedented territorial expansion, architectural marvels, and profound cultural influence.
The empire's roots lie in the city of Rome, founded, according to legend, by Romulus in 753 BCE. Over centuries, Rome evolved from a small settlement to a formidable republic, characterized by a complex political system with elected officials and checks on power. However, internal strife, class conflicts, and military ambitions paved the way for the end of the Republic. Julius Caesar’s dictatorship and subsequent assassination in 44 BCE created a power vacuum, leading to a civil war. Octavian, later Augustus, emerged victorious, heralding the Roman Empire’s birth.
Under Augustus, the empire experienced the Pax Romana, a 200-year period of relative peace and stability. Augustus reformed the military, established efficient administrative systems, and initiated grand construction projects. The empire's borders expanded, encompassing territories from Britain to Egypt and from Spain to the Euphrates. Roman legions, renowned for their discipline and engineering prowess, secured and maintained these vast territories, building roads, fortifications, and cities that facilitated control and integration.
The Roman Empire’s society was hierarchical, with a rigid class system. At the top were the patricians, wealthy elites who held significant political power. Below them were the plebeians, free citizens with limited political influence, and the vast numbers of slaves who formed the backbone of the economy. The family unit was central, governed by the paterfamilias, the male head who held absolute authority.
Culturally, the Romans were eclectic, absorbing and adapting elements from the civilizations they encountered, particularly the Greeks. Roman art, literature, and philosophy reflected this synthesis, creating a rich cultural tapestry. Latin, the Roman language, became the lingua franca of the Western world, influencing numerous modern languages.
Roman architecture and engineering achievements were monumental. They perfected the arch, vault, and dome, constructing enduring structures like the Colosseum, Pantheon, and aqueducts. These engineering marvels not only showcased Roman ingenuity but also served practical purposes, from public entertainment to water supply.
Model Attribute Check Company Auto PropertyCeline George
In Odoo, the multi-company feature allows you to manage multiple companies within a single Odoo database instance. Each company can have its own configurations while still sharing common resources such as products, customers, and suppliers.
Read| The latest issue of The Challenger is here! We are thrilled to announce that our school paper has qualified for the NATIONAL SCHOOLS PRESS CONFERENCE (NSPC) 2024. Thank you for your unwavering support and trust. Dive into the stories that made us stand out!
Welcome to TechSoup New Member Orientation and Q&A (May 2024).pdfTechSoup
In this webinar you will learn how your organization can access TechSoup's wide variety of product discount and donation programs. From hardware to software, we'll give you a tour of the tools available to help your nonprofit with productivity, collaboration, financial management, donor tracking, security, and more.
Palestine last event orientationfvgnh .pptxRaedMohamed3
An EFL lesson about the current events in Palestine. It is intended to be for intermediate students who wish to increase their listening skills through a short lesson in power point.
1. SJM College of Pharmacy,
Chitradurga
Prepare By,
Adarsh Patil
Ass Professor(Pharmacognosy)
SJM College of Pharmacy
1
PHARMACEUTICAL
BIOTECHNOLOGY
2. Production of Enzymes:
Steps Involved:
1. Selection of organisms
2. Formulation of medium
3. Production process
4. Recovery & Purification of enzymes
3.
4. 1. Selection of organism:
• The most important criteria for selecting the microorganism
are that the organism should produce the maximum
quantities of desired enzyme in a short time while the
amounts of other metabolite produced are minimal.
• Once the organism is selected, strain improvement for
optimising the enzyme production can be done by appropriate
methods (mutagens, UV rays). From the organism chosen,
inoculum can be prepared in a liquid medium.
5. 2. Formulation of medium:
• The culture medium chosen should contain all the nutrients to support adequate
growth of microorganisms that will ultimately result in good quantities of
enzyme production.
• The ingredients of the medium should be readily available at low cost and are
nutritionally safe. Some of the commonly used substrates for the medium are
starch hydrolysate, molasses, corn steep liquor, yeast extract, whey, and soy
bean meal. Some cereals (wheat) and pulses (peanut) have also been used.
• The pH of the medium should be kept optimal for good microbial growth and
enzyme production.
6. 3. Production process:
• Industrial production of enzymes is mostly carried out by submerged
liquid conditions and to a lesser extent by solid-substrate fermentation.
• In submerged culture technique, the yields are more and the chances of
infection are less. Hence, this is a preferred method.
• However, solid substrate fermentation is historically important and still
in use for the production of fungal enzymes e.g. amylases, cellulases,
proteases and pectinases.
7. • The medium can be sterilized by employing batch or continuous sterilization techniques.
The fermentation is started by inoculating the medium. The growth conditions (pH,
temperature, O2 supply, nutrient addition) are maintained at optimal levels. The froth
formation can be minimised by adding antifoam agents.
• The production of enzymes is mostly carried out by batch fermentation and to a lesser
extent by continuous process.
• The bioreactor system must be maintained sterile throughout the fermentation process.
The duration of fermentation is variable around 2-7 days, in most production processes.
Besides the desired enzyme(s), several other metabolites are also produced. The enzyme(s)
have to be recovered and purified.
8. 4. Recovery and purification of enzymes:
• The desired enzyme produced may be excreted into the culture
medium (extracellular enzymes) or may be present within the cells
(intracellular enzymes). Depending on the requirement, the
commercial enzyme may be crude or highly purified.
• Further, it may be in the solid or liquid form. The steps involved in
downstream processing i.e. recovery and purification steps
employed will depend on the nature of the enzyme and the degree of
purity desired.
9. • In general, recovery of an extracellular enzyme which is present in the broth is relatively simpler
compared to an intracellular enzyme. For the release of intracellular enzymes, special techniques
are needed for cell disruption.
• Microbial cells can be broken down by physical means (sonication, high pressure, glass beads).
The cell walls of bacteria can be lysed by the enzyme lysozyme. For yeasts, the enzyme β-
glucanase is used. However, enzymatic methods are expensive.
• The recovery and purification (briefly described below) steps will be the same for both
intracellular and extracellular enzymes, once the cells are disrupted and intracellular enzymes
are released. The most important consideration is to minimise the loss of desired enzyme
activity.
10. 5. Removal of cell debris:
Filtration or centrifugation can be used to remove cell debris.
6. Removal of nucleic acids:
Nucleic acids interfere with the recovery and purification of enzymes. They can be precipitated and removed
by adding poly-cations such as polyamines, streptomycin and polyethyleneimine.
7. Enzyme precipitation:
Enzymes can be precipitated by using salts (ammonium sulfate) organic solvents (isopropanol, ethanol, and
acetone). Precipitation is advantageous since the precipitated enzyme can be dissolved in a minimal
volume to concentrate the enzyme.
8. Liquid-liquid partition:
Further concentration of desired enzymes can be achieved by liquid-liquid extraction using polyethylene
glycol or polyamines.
11. 9. Separation by chromatography:
There are several chromatographic techniques for separation and purification of enzymes. These
include ion-exchange, size exclusion, affinity, hydrophobic interaction and dye ligand
chromatography .Among these, ion- exchange chromatography is the most commonly used for
enzyme purification.
10. Drying and packing:
• The concentrated form of the enzyme can be obtained by drying. This can be done by film
evaporators or freeze dryers (lyophilizers). The dried enzyme can be packed and marketed. For
certain enzymes, stability can be achieved by keeping them in ammonium sulfate suspensions.
• All the enzymes used in foods or medical treatments must be of high grade purity, and must meet
the required specifications by the regulatory bodies. These enzymes should be totally free from
toxic materials, harmful microorganisms and should not cause allergic reactions.
12. 1. Amylase:
• Amylases are important hydrolase enzymes which
have been widely used since many decades.
• These enzymes randomly cleave internal
glycosidic linkages in starch molecules.
• To hydrolyze them and yield: (dextrins )
(oligosaccharides)
13. TYPES:
1. α-Amylase:
•α-Amylase is a hydrolase enzyme that catalyses the
hydrolysis of internal α-1, 4- glycosidic linkages in starch to
yield products like glucose and maltose.
• It is a calcium metalloenzyme i.e. it depends on the
presence of a metal co factor for its activity.
•The optimum pH for activity is found to be 7.0
•he substrate that α-amylase acts upon is starch.
• Starch: is a polysaccharide composed of two types of
polymers – amylose and amylopectin.
14. • Amylose constitutes 20-25% of the starch molecule.
• It is a linear chain consisting of repetitive glucose units linked
by α-1,4-glycosidic linkage.
• Amylopectin constitutes 75-80% of starch and is
characterized by branched chains of glucose units.
• The linear successive glucose units are linked by α-1, 4-
glycosidic linkage.
• while branching occurs every 15-45 glucose units where α-1, 6
glycosidic bonds are present.
15. 2. β-Amylase:
• an exo-hydrolase enzyme that acts from the nonreducing end of a polysaccharide chain by
hydrolysis of α-1, 4-glucan linkages to yield successive maltose units.
• Since it is unable to cleave branched linkages in branched polysaccharides such as
glycogen or amylopectin.
• the hydrolysis is incomplete and dextrin units remain.
• Primary sources of β-Amylase are the seeds of higher plants and sweet potatoes.
• The optimal pH of the enzyme ranges from 4.0 to 5.5.
• β-Amylase can be used for different applications on the research as well as industrial front.
• It can be used for structural studies of starch and glycogen molecules produced by various
methods.
16. 3. γ-Amylase:
• γ-Amylase cleaves α(1-6)glycosidic linkages, in
addition to cleaving the last α(1- 4)glycosidic
linkages at the nonreducing end of amylose and
amylopectin, unlike the other forms of amylase,
yielding glucose.
• γ- amylase is most efficient in acidic environments
and has an optimum pH of 3.
17. Sources:
• α-Amylase can be isolated from plants, animals or
microorganisms.
• The enzyme has been isolated from barley and rice plants.
• It has been found that cassava mash waste water is a source of
α-Amylase.
• In the recent past, there has been extensive research on
microbial production of α- Amylase.
18. There are 2 major reasons for the increasing interest in microbial sources:
1) The growth of microorganisms is rapid and this will in turn speed up the
production of enzyme.
• Microorganisms are easy to handle when compared to animals and plants.
• They require lesser space and serve as more cost effective sources.
2) Microorganisms can be easily manipulated using genetic engineering or other means.
• They can be subjected to strain improvement, mutations and other such changes
by which the production of α-Amylase can be optimized.
• α-Amylase is produced by several bacteria, fungi and genetically modified species
of microbes.
21. Production:
There are mainly two methods which are used for production of α-Amylase on a commercial scale.
These are:
1) Submerged fermentation (SMF)
2) Solid State fermentation (SSF)
1) Submerged fermentation (SMF):
Submerged fermentation (SmF) employs free flowing liquid substrates, such as molasses and broths.
The products yielded in fermentation are secreted into the fermentation broth.
This fermentation technique is suitable for microorganisms such as bacteriathat require high
moisture content for theirgrowth.
SmF is primarily used for the extraction of secondary metabolites that need to be used in liquid form .
22. This method has several advantages.SmF allows
the utilizationof genetically modified organisms
to a greater extent than SSF.
The sterilization of the medium and purification
process of the end products can be done easily.
Also the controlof process parameters like
temperature, pH, aeration, oxygen transfer and
moisture can be done conveniently.
23. 2. Solid State Fermentation:
Solid state fermentation is a method used for microbes which require less moisture
contentfor their growth.
The solid substrates commonly used in this method are bran, bagasse, and paper
pulp.
The main advantage is that nutrient-rich waste materials can be easily recycled
and used as substrates in this method
Other advantages that SSF offers over SmF are
simpler equipments, higher concentration of products and lesser effluent generation.
For several such reasons SSF is considered as a
promising method for commercial production of enzymes.
24. 3 methods
4.1. Dinitrosalicylic Acid Method (DNS):
In the dinitrosalicylic acid method, aliquots of the substrate stock
solution are mixed with the enzyme solution.
Followed by 10 min of incubation at 50°C,
DNS reagent is added to the test tube and the
mixture is incubated in a boiling water bath for 5 min.
After cooling to room temperature, the absorbance of the supernatant at 540 nm is measured.
25. In the NS method, an aliquot of stock solution
of substrate is heated at 50°C for 5min.
Preheated (50°C for 5 min) enzyme solution is added to the substrate.
This reaction mixture is incubated at 50°C and the reaction is carried out for 10min.
After incubation Somogyi copper reagent is addedto
terminate the reaction.
This is then incubated in boiling water bath for 40 min & cooled to room temperature.
Finally water is added and the mixtureis centrifuged at 13,000 rpm for 1 min and absorbance
of supernatant is read at 610 nm .
26. The hydrolytic activity of α-Amylase can be determined based on the principle
that starch and iodine react to form a blue colored
complex.
On hydrolysis of starch this complex changes to a reddish
brown colored one.
The absorbance can be read after the enzyme substrate reaction has been
terminated.
This gives a measure of the extent of hydrolysis of starch by α-Amylase.
27. This can be followed by any of the chromatographic
techniques like ion exchange,
Gel filtration and affinity chromatography for
further separation and purification of the enzyme.
the enzyme was precipitated was followed by
dialysis and then column chromatography