Molecular gastronomy: Difference between revisions

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Gluten usually refers to a combination of prolamin and glutelin proteins; in wheat it consists of gliadin and glutenin.
Gluten usually refers to a combination of prolamin and glutelin proteins; in wheat it consists of gliadin and glutenin.
* Prolamins are a group of plant storage proteins (a high proline amino acid content). High glutamine and proline content, poor solubility in water.  
* Prolamins are a group of plant storage proteins (a high proline amino acid content). High glutamine and proline content, poor solubility in water.  
** Gliadin (a type of prolamin) is a class of proteins present in wheat etc.  Gliadins are essential for giving bread the ability to rise. Are soluble in 70% ethanol. There are 3 main types of gliadin. Gliadins are intrinsically disordered proteins (continously altering shapes), but the average shape is an ellipse with an tadpole like structure with hydrophobic core and disordered tail. Gliadins are monomeric molecules in the cell: the gliadins are unable to form polymers because its cysteines form intra-chain disulphide bonds are synthesis due to hydrophobic interactions. However, gliadins are capable to aggregate into larger oligomers and interact with other other gluten proteins (due to large hydrophobic sections, [https://en.wikipedia.org/wiki/Polyglutamine_tract poly-Q] and [https://en.wikipedia.org/wiki/Protein_tandem_repeats repetative sequencies]). Gliadins contribute to the extensibility.
** Gliadin (a type of prolamin) is a class of proteins present in wheat etc.  Gliadins are essential for giving bread the ability to rise. Are soluble in 70% ethanol. There are 3 main types of gliadin. Gliadins are intrinsically disordered proteins (continously altering shapes), but the average shape is an ellipse with an tadpole like structure with hydrophobic core and disordered tail. Gliadins are monomeric molecules in the cell: the gliadins are unable to form polymers because its cysteines form intra-chain disulphide bonds are synthesis due to hydrophobic interactions. However, gliadins are capable to aggregate into larger oligomers and interact with other other gluten proteins (due to large hydrophobic sections, [https://en.wikipedia.org/wiki/Polyglutamine_tract poly-Q] and [https://en.wikipedia.org/wiki/Protein_tandem_repeats repetative sequencies]). Gliadins contribute to the extensibility. Gliadins are mainly monomeric proteins with molecular weights (MWs) around 28,000-55,000


* glutelin is a class of prolamin proteins. Glutelins are rich in hydrophobic amino acids ([https://en.wikipedia.org/wiki/Phenylalanine phenylalanine], [https://en.wikipedia.org/wiki/Valine valine], [https://en.wikipedia.org/wiki/Tyrosine tyrosine], [https://en.wikipedia.org/wiki/Proline proline] and [https://en.wikipedia.org/wiki/Leucine leucine]) [wikipedia].  
* glutelin is a class of prolamin proteins. Glutelins are rich in hydrophobic amino acids ([https://en.wikipedia.org/wiki/Phenylalanine phenylalanine], [https://en.wikipedia.org/wiki/Valine valine], [https://en.wikipedia.org/wiki/Tyrosine tyrosine], [https://en.wikipedia.org/wiki/Proline proline] and [https://en.wikipedia.org/wiki/Leucine leucine]) [wikipedia].  
** [https://en.wikipedia.org/wiki/Glutenin Glutenin] is major protein within wheat flour (47% of total proteins). Thus, it is the most common glutelin, barley and rye has different glutelin proteins. The glutenins are protein aggregates. Glutenin forms extended polymer networks due to disulphide bonds. Is thought to be largely responsible for the elastic properties of gluten, and hence, doughs (elastomeric proteins: the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed). There are of two different types of glutenins, named low (LMW) and high molecular weight (HMW) subunits.
** [https://en.wikipedia.org/wiki/Glutenin Glutenin] is major protein within wheat flour (47% of total proteins). Thus, it is the most common glutelin, barley and rye has different glutelin proteins. The glutenins are protein aggregates. Glutenin forms extended polymer networks due to disulphide bonds. Is thought to be largely responsible for the elastic properties of gluten, and hence, doughs (elastomeric proteins: the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed). There are of two different types of glutenins, named low (LMW; MW=32,000-35,000) and high molecular weight (HMW; MW=67,000-88,000) subunits. Each gluten protein type consists or two or three different structural domains; one of them contains unique repetitive sequences rich in glutamine and proline. Native glutenins are composed of a backbone formed by HMW subunit polymers and of LMW subunit polymers branched off from HMW subunits.  





Revision as of 17:33, 26 January 2024

Introduction

Some interesting experiments about molecular gastronomy.

Molekyyligastronomia. Gastronomia.

Theory

Egg

Koageloituminen; valkuainen ja keltuainen.

Butter

Voin kirkastaminen.

Sorbetti

Gelato

Kerma (6-9%), sokeri ja ilma (65%). Jäätelössä on enemmän ilmaa kuin gelatossa. Lisäksi jäätelössä on usein munanvalkuaista. Gelatossa on yleensä enemmän maitoa.

Munanvalkuainen lisää rasvaa ja stabiloi. Kaupallisessa jäätelössä on myös muita stabiloijia, kuten guargumia. Stabilointi estää isompien jääkiteiden synnyn.


Marenki

  1. Munanvalkuaisen / sokerin suhde
  2. Vatkauksen määrä
  3. Uunituksen määrä

Mikroskooppi.

Puuron pentagoni

Tuulihatut

  • 100 g voita
  • 3 dl vettä
  • 2 dl vehnäjauhoja
  • 3 munaa
  • 1/2 tl leivinjauhetta
  1. Sidokset
  2. Uunittamisen fysiikkaa
  3. Kananmunan merkitys

Sitko eli gluteeni

Vehnässä on proteiinia n 13% [Wikipedia] (josta 47% gluteniinia).

In the wheat seed, the two main components of gluten are gliadins and glutenins. Both are not water-soluble.

Gluten usually refers to a combination of prolamin and glutelin proteins; in wheat it consists of gliadin and glutenin.

  • Prolamins are a group of plant storage proteins (a high proline amino acid content). High glutamine and proline content, poor solubility in water.
    • Gliadin (a type of prolamin) is a class of proteins present in wheat etc. Gliadins are essential for giving bread the ability to rise. Are soluble in 70% ethanol. There are 3 main types of gliadin. Gliadins are intrinsically disordered proteins (continously altering shapes), but the average shape is an ellipse with an tadpole like structure with hydrophobic core and disordered tail. Gliadins are monomeric molecules in the cell: the gliadins are unable to form polymers because its cysteines form intra-chain disulphide bonds are synthesis due to hydrophobic interactions. However, gliadins are capable to aggregate into larger oligomers and interact with other other gluten proteins (due to large hydrophobic sections, poly-Q and repetative sequencies). Gliadins contribute to the extensibility. Gliadins are mainly monomeric proteins with molecular weights (MWs) around 28,000-55,000
  • glutelin is a class of prolamin proteins. Glutelins are rich in hydrophobic amino acids (phenylalanine, valine, tyrosine, proline and leucine) [wikipedia].
    • Glutenin is major protein within wheat flour (47% of total proteins). Thus, it is the most common glutelin, barley and rye has different glutelin proteins. The glutenins are protein aggregates. Glutenin forms extended polymer networks due to disulphide bonds. Is thought to be largely responsible for the elastic properties of gluten, and hence, doughs (elastomeric proteins: the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed). There are of two different types of glutenins, named low (LMW; MW=32,000-35,000) and high molecular weight (HMW; MW=67,000-88,000) subunits. Each gluten protein type consists or two or three different structural domains; one of them contains unique repetitive sequences rich in glutamine and proline. Native glutenins are composed of a backbone formed by HMW subunit polymers and of LMW subunit polymers branched off from HMW subunits.



Gluteiini on vehnän eräs proteiini, joka syntyy jyvän proteiineista taikinan vesiliuoksessa. Jauho-vesi-taikinaa vaivattaessa gliadiini ja gluteniini järjestyvät gluteeniksi.

https://en.wikipedia.org/wiki/Gluten

https://www.uniprot.org/uniprotkb/P04706/entry

Suola ja sitko

Suola on säilöntäaine: tappaa mikrobit (ja hiivan). Suolaa tarvitaan sitkoon eli gluteeiniin (tiivis, venyvä ja joustava verkosto, joka antaa taikinalle sen sitkon).

Gluteiini on vehnän eräs proteiini, joka syntyy jyvän proteiineista taikinan vesiliuoksessa. Jauho-vesi-taikinaa vaivattaessa gliadiini ja gluteniini järjestyvät gluteeniksi.

https://en.wikipedia.org/wiki/Gluten

Lihan pinta

Maillard reaction: amino acids and reducing sugars to create melanoidins (the compounds that give browned food its distinctive flavour) [Wikipedia]. Reaction proceeds rapidly between 140 and 165 °C.

Karamellisaatio

https://en.wikipedia.org/wiki/Caramelization

  • caramelans (C24H36O18),
  • caramelens (C36H50O25), and
  • caramelins (C125H188O80).

As the process occurs, volatile chemicals such as diacetyl are released, producing the characteristic caramel flavor. [wikipedia].

Suklaan määrän vaikutus masaliisan ominaisuuksiin

Masaliisa

  • 3 munaa
  • 4 dl sokeria
  • 5 dl jauhoja
  • 2 tl vaniljasokeria
  • 4 tl leivinjauhetta
  • 2 rkl kaakaota

Lisää vielä

  • 200 g voita

Varioi kaakaon määrää

  • 0,5 rkl
  • 1 rkl
  • 2 rkl
  • 3 rkl
  • 4 rkl


Compounds

  • glykoalkaloidi (Solaniini, Kakoniini)
  • Kalsiumpropionaatti

References

List_of_cooking_techniques