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Experiential Learing
RV College of
Engineering
Go, change the
world
SEM IV
BRANCH BIOTECHNOLOGY
RV College of
Engineering Go, Change the World
TEAM INTRODUCTION
PHOTO
MEMBER-1
PHOTO
MEMBER-2
PHOTO
MEMBER-3
Roll No. Admission No. Name Email Id
RV College of
Engineering Go, Change the World
Presentation Outline
• Introduction
• Structure and properties of Casein
• Properties of various Casein proteins
• Casein gene translation in bovine mammary gland
• Extraction of casein and confirmatory test
• Various uses of casein
• Use of casein as a Bioplastic
• Results and Discussion
• References
RV College of
Engineering Go, Change the World
INTRODUCTION
•What is casein?
Casein is a family of related phosphoprotein that is commonly found in milk
comprising of 80% of protein in cow and buffalo to 20-60 % in human milk.
It is of four types (alphaS1,alphaS2,beta,kappa).In fresh milk it is present as a
colloidal form casein micelles.
In this project we are analyzing properties and structure of the casein protein.
Its genetic translational properties. Extraction of casein from cow milk. Its
various uses. Casein protein as an alternative for plastic.
RV College of
Engineering Go, Change the World
Structure & Properties of Casein
• It is a type of phosphoprotein which is present commonly in milk.
• It is composed of (as1, as2, beta, kappa) in the ratio of (4:1:4:1).
• These proteins are translated by their respective genes present in mammary
gland(csn1s1, csn1s2, csn2, csn3).
• Its most common form is sodium caseinate.
• In fresh milk it is present as a colloidal form due to phase separation known as casein
micelles.
• Casein micelles is composed of several similar proteins, forming a multi- ‐ molecular
granular structure. The casein micelle contains water plus salts (mainly from Calcium
and Phosphorus).
• Average diameter of the micelle is about 120 to 180 nm.
• Salts present in the micelles are nano clusters of calcium and phosphorous.
RV College of
Engineering Go, Change the World
Structure & Properties of Casein
• It is believed that Ca and P are connectors of the protein since the removal of them
leads to dissociation of micelles into sub micelles.
• Micelles are formed by proteins and the colloidal calcium phosphates.
• CCP acts like cement as it connect the sub micelles.
• Under Electron microscope it is seen that there are no sub micelles but a protein
matrix and channels inside of the micelle.
• But recently using high resolution microscope and carefully made samples show that
the sub micelle model may exist.
• According to horne model whole micelle consist of small sub micelles connected with
CCP.
RV College of
Engineering Go, Change the World
Structure & Properties of Casein
• Outer surface of the micelle is kappa-rich having protruding hairs of –ve charges
which induces a steric repulsion between micelles preventing them to coagulate and
hence stabilizes the micelle.
• Holt model explains how the nano-clusters of the CCP acts like cement and connect
the protein to form big micelle. Both alpha and beta are attached to the cluster. The
difference between the proteins enables them to make a bridge with the cluster.
RV College of
Engineering Go, Change the World
Structure & Properties of Casein
• It is generally flexible and heat stable.
• It is water insoluble, dilute alkali soluble.
• Casein micelles contain calcium, phosphate, citrate ions.
• It also contains lipase and plasmid enzymes which help to digest it.
• It precipitates at the ph. 4.6 by addition of dilute acid, salt and rennet
• It is a lyophilic compound.
• It is isoelectric at ph 4.6 amphoteric below 4.6 and forms soluble salt above 4.6 it
makes salt with bases at ph above 4.6.
• Alkali salts of casein like sodium caseinate are soluble without limit whereas the
alkaline earth metal salts like calcium caseinate are nearly insoluble.
• Casein forms gel when slowly coagulated from concentrated solutions.
• Formaldehyde forms insoluble compound with casein.
RV College of
Engineering Go, Change the World
Properties of various Casein Proteins
1. alpha s1 casein
• It consists of 199 amino acid chain.
• (1-44), (90-199) region of the chain is non-polar hydrophobic.
• (45-89) region is hydrophilic and polar nature.
• It is a chain of loose flexible polypeptides.
• It aggregates and precipitates at the low concentration of calcium.
2. alpha s2 casein
• It is a dipolar structure.
• Its n terminal is –vely charged and c terminal is +vely charged.
• In case of precipitation it is more sensitive than alpha s1 casein.
3. beta casein
• It consists of 209 amino acid chain.
• N terminal is –vely charged.
• A1 and A2 are 2 genetic variants. Histidine and proline are present at the 67th
position respectively.
• Gamma casein is a part of beta casein.
RV College of
Engineering Go, Change the World
Properties of various Casein Protein
• It is formed by cleavage of beta casein at the positions (28-29), (105-106), (107-
108) by plasma enzymes.
• The cleaved part consist of gamma casein(29-209), (106-209), (108-209) and whey
components.
4. Kappa casein
• It consists of 169 amino acid chain.
• It is a glycoprotein.
• It is present on the surface of the casein micelles.
• It prevent precipitation and provide stability to the micelle.
• When ingested it is broken into insoluble pera kappa-casein and soluble
glycopeptide.
RV College of
Engineering Go, Change the World
Translational Properties of Casein gene
RV College of
Engineering Go, Change the World
Translational Properties of Casein gene
RV College of
Engineering Go, Change the World
Extraction of Casein from milk
RV College of
Engineering Go, Change the World
Extraction of Casein from milk
RV College of
Engineering Go, Change the World
Uses of Casein
RV College of
Engineering Go, Change the World
Use of Casein as a Bioplastic
RV College of
Engineering Go, Change the World
RV College of
Engineering Go, Change the World
Results & Discussion
RV College of
Engineering Go, Change the World
References

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Experiential learning molecular bio ppt.pptx

  • 1. Experiential Learing RV College of Engineering Go, change the world SEM IV BRANCH BIOTECHNOLOGY
  • 2. RV College of Engineering Go, Change the World TEAM INTRODUCTION PHOTO MEMBER-1 PHOTO MEMBER-2 PHOTO MEMBER-3 Roll No. Admission No. Name Email Id
  • 3. RV College of Engineering Go, Change the World Presentation Outline • Introduction • Structure and properties of Casein • Properties of various Casein proteins • Casein gene translation in bovine mammary gland • Extraction of casein and confirmatory test • Various uses of casein • Use of casein as a Bioplastic • Results and Discussion • References
  • 4. RV College of Engineering Go, Change the World INTRODUCTION •What is casein? Casein is a family of related phosphoprotein that is commonly found in milk comprising of 80% of protein in cow and buffalo to 20-60 % in human milk. It is of four types (alphaS1,alphaS2,beta,kappa).In fresh milk it is present as a colloidal form casein micelles. In this project we are analyzing properties and structure of the casein protein. Its genetic translational properties. Extraction of casein from cow milk. Its various uses. Casein protein as an alternative for plastic.
  • 5. RV College of Engineering Go, Change the World Structure & Properties of Casein • It is a type of phosphoprotein which is present commonly in milk. • It is composed of (as1, as2, beta, kappa) in the ratio of (4:1:4:1). • These proteins are translated by their respective genes present in mammary gland(csn1s1, csn1s2, csn2, csn3). • Its most common form is sodium caseinate. • In fresh milk it is present as a colloidal form due to phase separation known as casein micelles. • Casein micelles is composed of several similar proteins, forming a multi- ‐ molecular granular structure. The casein micelle contains water plus salts (mainly from Calcium and Phosphorus). • Average diameter of the micelle is about 120 to 180 nm. • Salts present in the micelles are nano clusters of calcium and phosphorous.
  • 6. RV College of Engineering Go, Change the World Structure & Properties of Casein • It is believed that Ca and P are connectors of the protein since the removal of them leads to dissociation of micelles into sub micelles. • Micelles are formed by proteins and the colloidal calcium phosphates. • CCP acts like cement as it connect the sub micelles. • Under Electron microscope it is seen that there are no sub micelles but a protein matrix and channels inside of the micelle. • But recently using high resolution microscope and carefully made samples show that the sub micelle model may exist. • According to horne model whole micelle consist of small sub micelles connected with CCP.
  • 7. RV College of Engineering Go, Change the World Structure & Properties of Casein • Outer surface of the micelle is kappa-rich having protruding hairs of –ve charges which induces a steric repulsion between micelles preventing them to coagulate and hence stabilizes the micelle. • Holt model explains how the nano-clusters of the CCP acts like cement and connect the protein to form big micelle. Both alpha and beta are attached to the cluster. The difference between the proteins enables them to make a bridge with the cluster.
  • 8. RV College of Engineering Go, Change the World Structure & Properties of Casein • It is generally flexible and heat stable. • It is water insoluble, dilute alkali soluble. • Casein micelles contain calcium, phosphate, citrate ions. • It also contains lipase and plasmid enzymes which help to digest it. • It precipitates at the ph. 4.6 by addition of dilute acid, salt and rennet • It is a lyophilic compound. • It is isoelectric at ph 4.6 amphoteric below 4.6 and forms soluble salt above 4.6 it makes salt with bases at ph above 4.6. • Alkali salts of casein like sodium caseinate are soluble without limit whereas the alkaline earth metal salts like calcium caseinate are nearly insoluble. • Casein forms gel when slowly coagulated from concentrated solutions. • Formaldehyde forms insoluble compound with casein.
  • 9. RV College of Engineering Go, Change the World Properties of various Casein Proteins 1. alpha s1 casein • It consists of 199 amino acid chain. • (1-44), (90-199) region of the chain is non-polar hydrophobic. • (45-89) region is hydrophilic and polar nature. • It is a chain of loose flexible polypeptides. • It aggregates and precipitates at the low concentration of calcium. 2. alpha s2 casein • It is a dipolar structure. • Its n terminal is –vely charged and c terminal is +vely charged. • In case of precipitation it is more sensitive than alpha s1 casein. 3. beta casein • It consists of 209 amino acid chain. • N terminal is –vely charged. • A1 and A2 are 2 genetic variants. Histidine and proline are present at the 67th position respectively. • Gamma casein is a part of beta casein.
  • 10. RV College of Engineering Go, Change the World Properties of various Casein Protein • It is formed by cleavage of beta casein at the positions (28-29), (105-106), (107- 108) by plasma enzymes. • The cleaved part consist of gamma casein(29-209), (106-209), (108-209) and whey components. 4. Kappa casein • It consists of 169 amino acid chain. • It is a glycoprotein. • It is present on the surface of the casein micelles. • It prevent precipitation and provide stability to the micelle. • When ingested it is broken into insoluble pera kappa-casein and soluble glycopeptide.
  • 11. RV College of Engineering Go, Change the World Translational Properties of Casein gene
  • 12. RV College of Engineering Go, Change the World Translational Properties of Casein gene
  • 13. RV College of Engineering Go, Change the World Extraction of Casein from milk
  • 14. RV College of Engineering Go, Change the World Extraction of Casein from milk
  • 15. RV College of Engineering Go, Change the World Uses of Casein
  • 16. RV College of Engineering Go, Change the World Use of Casein as a Bioplastic
  • 17. RV College of Engineering Go, Change the World
  • 18. RV College of Engineering Go, Change the World Results & Discussion
  • 19. RV College of Engineering Go, Change the World References