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Continuation to Biochemical composition….

Dr. Tanya L. Swer
11/8/2020, 18/9/2020, 25/8/2020
 Lipids are the generic names assigned to a group of compounds that are
 Hydrophobic, non-polar and mostly made up of hydrocarbon chains.

 Marine lipids are composed of

 Triacylglycerols, phospholipids, sterols, wax, and
 Some unusual lipids, such as glyceryl esters, glycolipids, sulfolipids, and
hydrocarbons.

 Role: Store energy, provide insulation, make up cell membrane, building blocks for
hormones.

 The amounts of lipids in fish may vary from 0.2% to 23.7%,

 Depending upon species, anatomical position, organs, sex, season, and diet.

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 Lean fish store lipids only to a limited extent in the liver,
 Fatty fish store lipids in fat cells distributed in other body tissues
located in the subcutaneous tissue, in the belly flap muscle, and
in the muscles moving the fins and tail.

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 Lipids are composed of fatty acids.
R–COOH where R is a hydrocarbon chain

 The hydrocabon chain length of fatty acids in fishes generally range from C14 to C24
although C12 and C26 are also found.
 monounsaturated (15-40%), saturated (20-35%), and polyunsaturated (38-51%) acids

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 SFA: No double bonds

 Palmitic acid (C16:0) and stearic (C18:0) most important

 Some odd number SFA pentadecanoic acid (C15:0) and margaric acid (C17:0) may be

present in small amount in some species.

 Recommended value of PUFA/ SFA is 0.45 for a balance diet.

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 MUFA:
 Crustacean: Palmitoleic (C16:1n-7) and oleic acids (C18:1n-9)
 Fresh water fishes: oleic acids (C18:1n-9)

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 Polyunsaturation: -3 or -6

 Marine oils are particularly rich in the two nutritionally important -3 PUFAs, namely, C20:5n-
3 (eicosapentaenoic acid—EPA) and C22:6n-3 (docosahexaenoic acid—DHA)

 Freshwater fish contain less -3 and more -6 PUFAs

 In marine fish: the ratio of polyenoic to saturated acids being 3:1 (highly unsaturated)
 In freshwater fish, the ratio is 1:1.

 -3 PUFAs are less sensitive to oxidation by lipoxygenases than -6

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 Pelagic fish are better sources of EPA and DHA than ground fish.
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 Red muscles > 2-5 times more lipid than white muscles.
 (as well as more B‐vitamins, glycogen and nucleic acids)

 In many species fat content increases during the feeding season and its
proportion decreases substantially after spawning.

 The lipid content is affected by external factors such as seasonal fluctuations

in the environmental conditions and availability of phytoplankton.

 In many pelagic fish, lipid contents ranging from 12 to 20% are found during
winter compared with 3–5% during summer.

 It is accepted that there is an inverse relationship between unsaturated fatty

acid content and environmental temperature for many marine fish 10
 Fish has less cholesterol than animal meat.

 Cholesterol is the main sterol in marine fish like haddock, pollock, salmon,
and crustaceans like shrimp and lobster.

 Fish muscle : ↓ cholesterol,

 Shrimps, prawns; squid and octopus: ↑ cholesterol.

 Freshwater fish muscle > marine fish muscles.

 There were no significant correlations of cholesterol content of fish between

the catching season and the catching ground
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 Fish is a very poor source of carbohydrates.
 Fish store carbohydrate as glycogen in a level varying from 0.1 to 1%.
 * Oyster= 6.45 %, Spiny Lobster= 10.2% Blue crab= 12.5 % (glucose, galactose and
mannose).
 Glycogen:
 pH value
 Texture
 WHC
 Bacterial growth
 Colour
 Some CHO Also occur as part of the chemical constituents of nucleotides in fish muscle.

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 Fat-soluble vitamins (vitamin A, D, and E)
 Dependent on the species

 Lean fish: 25-50 IU of vitamin A

 Fatty Fish: Mackerel=100 IU; and Herring=1500 IU

 Warm water pelagic fish species such as tuna have a vitamin A content as high
as 10,000-250,000 IU/g of their liver oils.

 Vitamin E: 0.2 to 270 mg/100 g wet weight.

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 Water-soluble vitamins (B-complex and C)
 Less dependent on the species

 Vitamin B1, B2, B3, B12 = Large amount.

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 Fishes > animal.

 Mineral content: 0.6-1.5 % (marine fish and invertebrate)

 Shell fish> fin fish (almost twice)

 Macro-elements : sodium, potassium, magnesium, calcium, iron, phosphorus

 Microelements :iodine, fluorine, selenium, manganese, cobalt

 Toxic metals: Mercury=1-2 ppm

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Role of proteins
1. Nutrition
 Energy and essential amino acids

2. Structure
 Provide structure in fish and fish products

3. Catalysts
 Enzymes (which are proteins) catalyze chemical
reactions in living tissue and foods

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 Role of proteins
4. Functional properties
 Solubility
 Gelation (Texture)
 Emulsification
 Foaming
 Water holding capacity, etc.

5. Browning
 Have amino acids that can react with reducing sugars
 Some enzymes can also cause browning
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 Solubility  protein extractability  Recovery of protein.

 Sarcoplasmic protein and myofibrillar protein

 Salt concentration and pH

 It is the % of total protein that enters the solution but does not sediment due to
centrifugation.

 Important in the manufacture of muscle food products, Hydrolysates:

1. Comminuting of fish muscles mixed solution with pH or ionic strength

2. protein cleaved to peptides which are highly soluble due to
 Reduction in molecular weight
 Increased number of polar groups.
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 Solution
 Transformation of protein from sol state
(viscous state) to gel like state (elastic
material).

 Gelation of proteins is one of the principal

means to :
 give desirable texture to food products.
 Organoleptic properties
 Binding : retention and fat binding,
 Enhances stabilization of emulsions and foams,
 Retention of significant amount of sugars, flavor
and other food ingredients in a three dimensional
matrix is widely utilized in food processing and
Gel
 in the development of new food products.
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 The gelling capacity of fish proteins in comminuted fish products is one of their
most important functional properties.
utilized commercially in the production of
Surumi
Imitation shellfish meats, such as crab meat, scallops and shrimp.
Other Minced meat product

 Gelling properties dependent on the myofibrillar proteins (myosin).

 Myosin: water retention capacity, gel hardness, cohesiveness and elasticity.
 Molecular size decreases gelling ability.
 Other myofibrillar protein: affect viscoelastic properties of myosin gel.

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 This gelling capacity depends on:
1. Seafood species (hydrophobic groups, etc.)
2. Freshness.
3. Inherent protein characteristics (amount of sulfhydryl groups, amino acid types,
hydrophobicity, charge, and others),
4. External factors (gelling temperature, protein concentration, ionic strength, pH,
and others)

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 Solution
 A gel can form when proteins are denatured by
 Chemical: salt, pH; Physical: Heat, Pressure,
Shearing

 When seafood muscle tissue is comminuted in the

presence of NaCl, initially a viscous sol is formed,
which after heating turns into a viscoelastic gel.

 Intermolecular interactions (protein-protein)

 resulting in the three- dimensional network
of protein fibers which develop high structural rigidity. Gel

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 Thermally induced gels
(the most common)
 Involves unfolding of the protein structure by heat which exposes its
hydrophobic regions which leads to protein aggregation to form a
continuous 3D network
 This aggregation can be irreversible (myosin) or reversible (collagen/
gelatin)
 High ionic strength (i.e., added NaCl) favors myosin depolymerization resulting in
increased surface hydrophobicity, even at temperatures below 30°C.

 The weak hydrophobic interactions between myosin molecules initiate formation of a

gel structure.

 Myosin and actin are critical for thermal gelation of fish proteins.

 Myosin and actin undergo thermal denaturation at different temperatures, leading to

the development of a typical gel texture.

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 During thermal gelation of fish actomyosin complex, the viscosity increases between
30–41°C and 51–80°C.

 Muscle proteins isolated from cold-temperature fish such as Alaska pollack and hoki
are known to gel at slightly above 0°C in a few hours due to endogenous enzyme in
fish muscle, transglutaminase (Torley et al., 1991).

 Gelation at low temperature due to transglutaminase is unique for seafood proteins

and is often referred to as “suwari”.

 The gel-forming ability of dark fish muscle is lower than the white muscle due to the
difference in unfolding ability of myosin rods.

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 Fish muscle tissue consists of approximately 70–80% water.

 The ability of fish muscle proteins to hold water molecules during cooking and
comminution is called water-holding capacity (WHC).

 Paramount importance to the food industry:

 More H2O = Higher product yield = Higher financial benefit.
 Product quality may also be better tenderness, juiciness or succulence.

 Decrease in WHC= Poor protein quality= >> moisture loss= less yield.

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 Functional properties: Emulsification
Emulsion: A suspension of small globules of one liquid in a
second liquid with which the first will not mix.
 Fish Proteins can be excellent
emulsifiers
 They contain both hydrophobic
and hydrophilic groups.
 To form a good emulsion the protein has
to be able to:

 Rapidly adsorb to the oil-water interface

 Rapidly and readily open up and orient its

hydrophobic groups towards the oil phase
and its hydrophilic groups to the water
phase

 Form a stable film around the oil droplet

 Fish muscle proteins stabilize emulsions and are therefore good emulsifiers
in food products.

 Fish myosin and actin are the best emulsifiers.

 Emulsification of oil is possible because fish muscle proteins contain

hydrophobic amino acids.

 The emulsification of oil with fish muscle proteins involves two steps:
comminuting of fish muscle and heating.

 Protein hydrophobicity and length of protein chain influence this

functionality.
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Fish muscle proteins have various emulsifying
capacities and stabilize emulsions to different
degrees.

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Foams are very similar to emulsion where air is the
hydrophobic phase instead of oil

Principle of foam formation is similar to that of

emulsion formation (most of the same factors are
important)

Foams are typically formed by:

 Injecting gas/air through orifice
 Mechanically agitate a protein solution
(whipping/ bubbling or shaking)
 Gas release in food, e.g. leavened breads (a
special case)
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 Several studies have shown that protein-stabilized foams are most stable at
the isoelectric point (pI) of protein, provided protein solubility is not
affected.

 The pI of fish muscle proteins is at pH 5.5. NaCl at 0.5M enhances foaming

of fish protein concentrate (FPC).

 The FPC with amphiphilic characteristics, that is with both hydrophobic and
hydrophilic properties, has the best foaming properties.

 Foaming capacity of the FPC is provided by the soluble proteins

(hydrophilic proteins), while the remaining denatured proteins
(hydrophobic proteins) act as foam stabilizers
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 Proteins affect the sensory properties of food, i.e.,
 appearance;
 texture (sols, gels, foams, emulsions, extruded pieces);
 color (via browning reactions); and
 flavor (via browning reactions and sulfide elimination reactions, via proteolysis, and by
entrapment and binding of both desirable and undesirable flavors).

 The sensory properties of food products results from interactions between several
functional ingredients and proteins are one of the most important ingredients in food
products.

 The physical and chemical properties that determine protein functionality include
 the size and the shape of the proteins,
 the charge and the distribution of charge and
 the flexibility as well as the ratio between the hydrophobicity and hydrophilicity
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