Molecular gastronomy

Introduction

Some interesting experiments about molecular gastronomy.

Molekyyligastronomia. Gastronomia.

Theory

Egg

Koageloituminen; valkuainen ja keltuainen.

Butter

Voin kirkastaminen.

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.

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.

https://www.sciencedirect.com/science/article/pii/S0733521022000753

• The glutenin fraction represents about half of the total gluten proteins and consists of polymers stabilised by inter-chain disulphide bonds.
• HMW subunits are coded by six genes in wheat: Glu-1 loci, chromosomes 1A (Glu-A1), 1B (Glu-B1) and 1D (Glu-D1)
• Glu-1: x type (masses 80,000-100,000) and y-type (masses 60,000-80,000)
• LMW-GS's are about 65-70% of the total glutenin fraction. They are more diverse than HMWs.
• Glutenin polymers:
  • not soluble in the aqueous media
  • interact strongly with other glutenin polymers and gliadins by non-covalent forces, notably hydrogen bonds
  • Masses from(?) 2x10⁶ up to 10⁸
  • Large gluten polymers may also be sheared by vigorous stirring (should be avoided).
• Stabilization of glutenin polymers
  • Glutenin polymers are stabilised by interchain disulphide bonds
  • HMW-GS:HMW-GS, LMW-GS:LMW-GS, HMW-GS:LMW-GS bonds
  • Glutenin polymers associate with each other and with gliadins by non-covalent forces, in addition.
  • The behaviour of dough and gluten on heating: will “melt” hydrogen bonds but strengthen hydrophobic interactions.
• Models of glutenin structure
  • The ratio of HMW:LMW subunits in total glutenin is about 1:4
  • Linear Glutenin Hypothesis” of Ewart, 1977: glutenin consists of linear chains (concatenations) of glutenin molecules joined by disulphide bonds.
  • Bietz and Wall, 1980: the HMW subunits forms linear chains, but the LMW subunits forms oligomers of mass 100,000 to 150,000. The oligomers and individual LMW subunits could be linked to the HMW subunit concatenates by disulphide bonds.
  • Graveland et al., 1985
  • HMW subunits form the backbone of glutenin with LMW subunits forming side branches.
  • The HMW subunit polymers also form disulphide bonds with LMW subunits while gliadins interact by non-covalent forces.
  • We know much less about the organisation of LMW subunits in glutenin polymers.
  • LMW subunits (B, C and D-type)
  • Our current knowledge can therefore be summarised as follows:
    1. HMW subunits may form head-to-tail concatenates which form the backbone of large glutenin polymers.
    2. Individual LMW subunits and/or LMW subunit oligomers and polymers may be attached to this backbone by interchain disulphide bonds
    3. Soluble polymers are enriched in chain-terminating C-type and D-type LMW subunits.
    4. Smaller polymers and oligomers comprising only LMW subunits also occur.

P.R. Shewry, S.M. Gilbert, A.W.J. Savage, A.S. Tatham, Y.-F. Wan, P.S. Belton, N. Wellner, R. D'Ovidio, F. Bekes, N.G. Halford Sequence and properties of HMW subunit 1Bx20 from pasta wheat (Triticum aestivum) which is associated with poor end use properties

CW Wrigley, Nature, 1996: Giant proteins with flour power

.R. Shewry, N.G. Halford, A.S. Tatham, Y. Popineau, D. Lafiandra, P.S. Belton, The high molecular weight subunits of wheat glutenin and their role in determining wheat processing properties, Adv. Food Nutr. Res., 45 (2003), pp. 221-302,

H. Wieser, Chemistry of gluten proteins, Food Microbiol., 24 (2007), pp. 114-119, 10.1016/j.fm.2006.07.004

https://www.sciencedirect.com/science/article/pii/S0733521022000753#bib73

https://www.sciencedirect.com/science/article/pii/S0733521022000753#bib51

https://www.sciencedirect.com/science/article/pii/S0733521022000753#bib72

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