100% tevredenheidsgarantie Direct beschikbaar na betaling Zowel online als in PDF Je zit nergens aan vast
logo-home
Eerder door jou gezocht
Eerder door jou gezocht
logo
Summary Food Ingredient Functionality - Protein part €3,49   In winkelwagen
Snel navigeren naar
Voorbeeld
  2.  
  3. Wageningen University (WUR)
  4.  
  5. Food Ingredient Functionality (FCH30306)

Samenvatting

Summary Food Ingredient Functionality - Protein part

3 beoordelingen
 196 keer bekeken  3 keer verkocht

Don't feel like reading all 58 pages of the reader Food Ingredient Functionality? This summary describes all theory of the Protein part (reader, knowledgde clips, lectures) in just 6 pages! The content of the summary is: - Functionality - Variation in protein ingredients - Milk proteins - Protein...

[Meer zien]

Voorbeeld 2 van de 6  pagina's

Document informatie

  • 15 oktober 2020
  • 6
  • 2020/2021
  • Samenvatting

Onderwerpen

Geschreven voor

Alle documenten voor dit vak (7)

3  beoordelingen

review-writer-avatar

Door: foodtechaspirant • 2 jaar geleden

review-writer-avatar

Door: laurensnikolopoulos33 • 2 jaar geleden

review-writer-avatar

Door: mettehamers • 3 jaar geleden

Verkoper

avatar-seller
bsc_msc_food_technology

Ontvangen beoordelingen

Beschikbare oefenvragen

Questions to practice exam Food Ingredient Functionality (Proteins)

Oefenvragen 83 Oefenvragen
Gratis 12 verkocht
Oefenvragen 83 Oefenvragen
Gratis 12 verkocht

Enkele voorbeelden uit deze set oefenvragen

1.

Name five sources of variation in protein ingredients

Antwoord: The source, the isolation method, the modification (Mailard, hydrolysis, enzymatic browning), the processing and the powder properties

2.

What is protein content?

Antwoord: grams of protein in 100 grams of dry matter

3.

What is protein composition?

Antwoord: gram of specific protein in 100 gram of proteins

4.

If you filtrate milk, which component is the easiest to filter out?

Antwoord: Casein proteins because they are much larger than whey and lactose

5.

Can casein interact with calcium?

Antwoord: Yes, because casein molecules are phosphorylated. These phosphate groups can have a strong interaction with divalent ions as calcium.

6.

True or false? Caseins are random coil proteins

Antwoord: True

7.

True or false? Casein molecules have a secondary and tertiary structure

Antwoord: False, casein molecules do not have a secondary or tertiary structure

8.

What is the reason that casein molecules cluster together into micelles?

Antwoord: Because of their unequal distribution of the hydrophobicity and charge.

9.

How do the micelles cluster together into macro-micelles?

Antwoord: Because of bridges between calcium and phosphate.

10.

What is on the outside of the macro-micelles?

Antwoord: The kappa-casein. They contain a larger carbohydrate group that provides steric repulsion between different macro-micelles.

Voorbeeld van de inhoud

Summary Food Ingredient Functionality – FCH30306 WUR
Proteins
Functionality
Types of functionality
• Nutritional → (essential) amino acids in primary structure of proteins
• Physiological → polypeptides that trigger allergic reactions or reduce blood pressure
• Physical/technological → primary and tertiary structure of proteins makes it possible to form
and stabilise structures as foams, emulsions and gels.

What you want to know about a protein sample:
• Techno-functionality: which droplet size will it give, what kind of rheology does it give?
• Influence of system conditions: how does pH, ionic strength and temperature influence the
functionality of this protein?
• Influence of processing: what kind of processing is applied to make the isolate and what is the
effect of it on the protein?
• Interactions with non-protein compounds: will the proteins interact with other compounds?

Functionality Mechanism for functionality What can you measure?
Solubility Interaction with water / with other proteins Hydrophobicity, charge
Emulsification Adsorption kinetics, stabilisation of the Hydrophobicity, charge
interface
Gelation Unfolding, aggregation Hydrophobicity, charge, size,
structure, disulfide bridges
Viscosity Volume fraction of particles, interaction Size (protein aggregates),
between particles charge
Water binding H-bonding with amino acid side chains, gel Charge, polarity
properties
Fat and flavour Interaction with hydrophobic groups Hydrophobicity
binding


Variation in protein ingredients
Sources of variation in protein ingredients
• Source → a different source gives different proteins
• Isolation → different conditions will give different protein content* or composition**
• Modification → can change state of protein (Mailard, hydrolysis, enzymatic browning)
• Processing (heating) → proteins may aggregate or Mailard reaction.
• Powder properties → some powders will dissolve completely, other form lumps

*Protein content = gram protein / 100 gram dry matter
**Protein composition = gram of specific protein / 100 gram total protein in sample


Milk proteins: isolation and properties
Milk proteins are for 80% casein and 20% whey. Besides that, milk contains fat, carbohydrates
(lactose) and ash (calcium, sodium, phosphor)

, Casein
• Caseins are much larger than whey and lactose! Easy to use filtration for milk.
• Caseins are precipitated by adding rennet or acid so they aggregate.
• Casein protein molecules are phosphorylated because acidic phosphate groups are added. This
results in a decrease of the IEP. Besides that, the phosphate groups can have a strong
interaction with divalent ions such as calcium.
• Caseins are random coil proteins! Do not have a secondary or tertiary structure!
• Because of unequal distribution of the hydrophobicity and charge, caseins associate in micelles.
These micelles cluster together in macro-micelles because of calcium-phosphate bridges.
Phosphate from the serine amino acids.
• On the outside of the macro micelles are kappa-caseins, which contain a larger carbohydrate
group.
• At the pH of milk (6.7), casein micelles are considered to be soluble. However, when
carbohydrate groups on kappa-casein are removed by rennet, or when the pH is lowered, the
micelles will aggregate.
o Rennet casein: precipitation by rennet (removal of kappa casein, aggregation)
o Acid casein: pH lowered to 4.6 (aggregation because less charge)
o Na/K-caseinate: acid casein of which the pH is re-adjusted.
o Micellar casein: milk is filtrated.
• Casein proteins are very hard to dissolve.

Whey
• Obtained after separation of lipids and caseins from milk. Sometimes lactose is also removed.
• By chromatography you can yield whey proteins enriched in a-lactalbumin or B-lactoglobulin.
• WPC 35 contains 65% other components. For instance lactose. This can give a lot of Mailard
reaction.
• It is always important to know what the other components are!

Protein concentrate = 35-80% protein
Isolate = > 90% protein


Other food proteins
Gelatin
• Formed from collagen after extraction from animal skin or bone tissue by boiling.
• Mainly consists of tropocollagen → triple helix (so made of three polypeptide chains)
• Consist mainly of three amino acids: glycine-x-x. One of the other two is mostly
(hydroxy)proline.
• Proline contains an angle that prevents the formation of normal alpha helices or B-sheet.

Alpha helix Triple helix Beta-sheet




• High temperatures induce loss of native triple helical structure. After cooling the rearrange →
reversible gel structure

Storage proteins from leguminosa and oil seeds
• Soy, pea and rapeseed protein
• Globular proteins (so more similar to whey than casein)
• Important: different non-protein compounds can come along during extraction and thereby
influence the composition and final properties of the isolate


Protein modifications
Heating
• Structure of proteins can be disrupted by heating. How, depends on the structure.

Voordelen van het kopen van samenvattingen bij Stuvia op een rij:

Verzekerd van kwaliteit door reviews

Verzekerd van kwaliteit door reviews

Stuvia-klanten hebben meer dan 700.000 samenvattingen beoordeeld. Zo weet je zeker dat je de beste documenten koopt!

Snel en makkelijk kopen

Snel en makkelijk kopen

Je betaalt supersnel en eenmalig met iDeal, creditcard of Stuvia-tegoed voor de samenvatting. Zonder lidmaatschap.

Focus op de essentie

Focus op de essentie

Samenvattingen worden geschreven voor en door anderen. Daarom zijn de samenvattingen altijd betrouwbaar en actueel. Zo kom je snel tot de kern!

Veelgestelde vragen

Wat krijg ik als ik dit document koop?

Je krijgt een PDF, die direct beschikbaar is na je aankoop. Het gekochte document is altijd, overal en oneindig toegankelijk via je profiel.

Tevredenheidsgarantie: hoe werkt dat?

Onze tevredenheidsgarantie zorgt ervoor dat je altijd een studiedocument vindt dat goed bij je past. Je vult een formulier in en onze klantenservice regelt de rest.

Van wie koop ik deze samenvatting?

Stuvia is een marktplaats, je koop dit document dus niet van ons, maar van verkoper bsc_msc_food_technology. Stuvia faciliteert de betaling aan de verkoper.

Zit ik meteen vast aan een abonnement?

Nee, je koopt alleen deze samenvatting voor €3,49. Je zit daarna nergens aan vast.

Is Stuvia te vertrouwen?

4,6 sterren op Google & Trustpilot (+1000 reviews)

Afgelopen 30 dagen zijn er 73918 samenvattingen verkocht

Opgericht in 2010, al 14 jaar dé plek om samenvattingen te kopen

Start met verkopen
€3,49  3x  verkocht
  • (3)
  Kopen