CHEMICAL AND
ENZYMATIC
MODIFICATION OF
   PROTEIN
INTRODUCTION
• Protiens are used abundantly in the food industries because of their
  nutritional value and techno funtional properties such as
  emulsification,foaming,gelation,hydration and textural properties.
• These funtional properties of proteins are related to their molecular
  structures.
• There have been number of ways to enhance functionalities of maney
  food proteins including physical chemicals and enzymatic methods.
• Modifications of functionality of food proteins increases their
  applications as food ingredient.
• Chemical modifications describes the modification addition or removal
  through chemical reaction of any of variety of macro molecules including
  proteins and nucleic acids.
• The various funtional groups of proteins including
  amino,carboxyl,disulfide,imitate,phenolic,sulahydrle,thioether and
  guanidine.
• Consequently, reaction such as
  actuation,phosphorylation,estarification,glycation.
Chemical modifications of food protien
1.Acylation of food protien
protien s-acylation is the reversible addition of fatty acids to the cysteine
residues of target protien
2. Glycosylation of food protien
• Glycosylation is an interesting tool for improving food protien
  functionality .
• Prevents the progression of mailard reaction ,resulting in a glycosylatio
  the end product.
Enzymatic modification of food protein
• Protease and transglutaminase are the most frequently used enzymes for
  modifying the polypeptide back bone of food protien.
• Functional properties of proteins like solubility,gelation, emusification
  and foaming.
1.Solubility
• Prototypical modification has special important for the
  improvement of solubility of protein.
• Zeina, the maize protein that is highly insoluble at ph 2-
  5,exhibited good solubility (30%-50%).
• At this ph range when only 1.9%of the peptide bond were split
  by treatment with trypsin.
2.Gelation
• Hydrolysis was presumed to be detrimental to the gelling properties
  of protein because of the reduced hydrophobicity of hydrolysis.
• The increased net changes on the protien result in increased charge
  repulsion between peptide, decreasing their gelling ability .
3. Emulsification
• Emulsifying properties of protein are sensitive to proteolytic
  modification.
• Limited hydrolysis of casein decreased the Emulsifying activity at all
  ph.
4. Foaming
• The excellent foaming properties of soybean protien from mucor miehel.
• Due to narrow molecules weight distribution of peptide produced by this
  enzymes.
Applications
• a) Cereal products:
• Cross linking of cereal proteins has major potential in modification of technological and sensory
  properties of cereal products. TG mediated protein crosslink results in alluring of rheological
  properties of gluten by decreasing dough extensibility, increased water absorption and hinder the
  growth of air bubbles in the dough, thereby decreasing volume of bread. In the preparation of
  pasta and noodles, cross linking of gluten causes an increase in resistance for thermal processing.
• b) Milk products:
• Creation of inter-/ or intra molecular covalent bonds by TG cross-linking of milk proteins results
  in modification of textural and water binding properties of milk products especially, in low fat or
  protein products with acceptable texture.. In the production of fermented milk product such as
  yogurt, the introduction of covalent bond by enzymatic cross linking into gel network results in
  increase in gel firmness and sensory properties.
• c) Meat products:
• Enzymatic cross linking of the myofibrillar protein myosin
  improves the texture and water holding properties of meat or fish
  products and add value to meat and fish of poorer quality. In
  addition to restructuring, TG is successfully exploited in
  improving textural properties of heated meat products such as
  hams and sausages and enhancing surimi (fish paste) gelation and
  textural properties.
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