View source for Molecular gastronomy

== 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 ===
# Munanvalkuaisen / sokerin suhde
# Vatkauksen määrä
# Uunituksen määrä

Mikroskooppi.

=== Puuron pentagoni ===


=== Tuulihatut ===

*100 g voita
*3 dl vettä
*2 dl vehnäjauhoja 
*3 munaa
*1/2 tl leivinjauhetta

# Sidokset 
# Uunittamisen fysiikkaa
# Kananmunan merkitys

=== Sitko eli gluteeni ===

Some questions to be answered
# How does it look in wheat
# How it creates longer polys with water
# How does it look after formed as a giant molecule

Size of molecule
* gliadin: monomeric proteins with molecular weights (MWs) around 28,000-55,000
* glutenin: LMW; MW=32,000-35,000 and HMW; MW=67,000-88,000
Shape of the molecule
* gliadin:
* glutenin:

Proteins consists of aminoacids ()



Prolamins are called in:
* wheat gliadins
* rye secalins
* barley hordeins
* oat avenins
Prolamins are polymorphic (many variations and genotypes of the same protein).




Vehnässä on proteiinia n 13% [Wikipedia] (josta 47% gluteniinia). 
Wheat (Triticum aestivum L. 2n = 6 × = 42) flour is composed of starch (~70–75%: main component), proteins (~10–15%), lipids (~2%), minerals (~2%)
* As gliadins influence the extensibility and viscous nature and glutenins are responsible for the elasticity and strength of dough, gluten is known as the main factor in determining the quality of the baked products and processed foods' texture and flavor

Hydrophobic collapes, beta helix (beta sheet structure).

Molecules:
* Gliadin: 
** 1S9V Crystal structure of HLA-DQ2 complexed with deamidated gliadin peptide
** 5IG7 anti-gliadin
** 4OZH T-cell receptor recognition of HLA-DQ2-gliadin complexes associated with celiac disease.
** 4GG6 Biased T cell receptor usage directed against human leukocyte antigen DQ8-restricted gliadin peptides is associated with celiac disease.
** Not data, but images: https://ar.inspiredpencil.com/pictures-2023/gliadin-molecule
** https://www.dreamstime.com/stock-illustration-gliadin-molecule-component-gluten-d-illustration-protein-present-wheat-other-cereals-toxic-image94296314    C<sub>29</sub>H<sub>41</sub>N<sub>7</sub>O<sub>9</sub>
** Gliadin peptide
* Glutenin
** AF_AFP08488F1
** 6PX6 HLA-TCR complex
** 6PX6 HLA-TCR complex

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, [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. Gliadins contain four subfamilies, α/β-, γ-, δ- and ω-gliadins. Gli-A1, -B1, -D1, Gli-A2, -B2, -D2. Gliadins may act as plasticizer to modify the extensibility of gluten and dough.

* 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; MW=32,000-35,000; Glu-A3, Glu-B3 and Glu-D3) 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. The glutenins can be further divided into two subfamilies: HMW and LMW. 


Scientific Reports volume 7, Article number: 44609 (2017) , Da-Wei Wang, Da Li, Junjun Wang, Yue Zhao, Zhaojun Wang, Guidong Yue, Xin Liu, Huanju Qin, Kunpu Zhang, Lingli Dong & Daowen Wang: Genome-wide analysis of complex wheat gliadins, the dominant carriers of celiac disease epitopes. https://www.nature.com/articles/srep44609







P.R. Shewry, D. Lafiandra, vol 106, 2022, 103486, Wheat glutenin polymers 1. structure, assembly and properties 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(?) 2x10<sup>6</sup> up to  10<sup>8</sup>
** 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:
**# HMW subunits may form head-to-tail concatenates which form the backbone of large glutenin polymers.
**# Individual LMW subunits and/or LMW subunit oligomers and polymers may be attached to this backbone by interchain disulphide bonds
**# Soluble polymers are enriched in chain-terminating C-type and D-type LMW subunits.
**# Smaller polymers and oligomers comprising only LMW subunits also occur.
* Glutenin structure and gluten elasticity
** HMW subunits forms a loose β-spiral structure https://en.wikipedia.org/wiki/Beta_helix
** Glutamine zips contributes to gluten elascticity
** Hydrogen bond on hydration by orientation of the β-turns  vs dry gluten
** Further hydration results in the replacement of some of the interchain hydrogen bonds with hydrogen bonds with water, resulting in an equilibrium between aligned regions (trains) and loop regions. This is suggested to contribute to elasticity as mechanical deformation will lead to disruption
* Glutenin macropolymer GMP
** The gluten network in dough is not a continuous covalently linked polymer but consists of many polymers and monomers interacting by non-covalent forces.
** depolymerisation and repolymerisation.


Wheat gluten proteins
* Monomeric gliadins
** alpha-gliadins
** gamma-gliadins
** omega-gliadins
* Polymeric glutenins
** LMW subunits
** HMW subunits

Reiko Urade, Nobuhiro Sato, and Masaaki Sugiyama, Biophys rev 2018, 10(2), 435-443,  Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates
* Storage proteins in wheat are collectively referred to as gluten, but gluten is actually an aggregate formed from two major types of protein: gliadin and glutenin.
* The gluten in dough is created from these proteins by mixing wheat grain flour and water.
* Gliadins and glutenins make up approximately 30% and 50%, respectively, of the total protein in wheat grain
* gliadin contributes to the flow properties, while glutenin contributes to its elasticity and strength.
* Glutenin is composed of macropolymers. These macropolymers intermingle randomly with individual particles of gliadins to form the aggregate, which is held together with non-covalent interactions. 
* Gluten proteins show extensive polymorphism.
* Gliadins
** large families of proteins with similar amino acid sequences: α-, β-, γ-, and ω based on their electrophoretic mobility in two-dimensional electrophoresis .
** Cells of bread wheat are hexaploid and composed of genomes A, B, and D.
** proteins that are soluble in aqueous alcohols, but insoluble in water or neutral salt solutions.  Some researchers have reported that a considerable amount of gluten protein could be extracted with water from gluten to which NaCl had been added. For example, when gluten was homogenized in 1 M NaCl and repeatedly washed with pure water, both gliadin and glutenin could be extracted with distilled water. Why can gliadins only be extracted from salt-treated dough? It may be that interactions between ions, proteins and water are relevant to this question. Intramolecular disulfide bonds are essential for the solubility of gliadin in pure water.
** The circular dichroism. α-helix
** Calculating the molecular dimensions (d) and semi-major axes (a) of the gliadins in 70% ethanol, assuming both a rod model and a prolate ellipsoid model: The prolate ellipsoid is a more appropriate model than a rod.


Gluten: A balance of gliadin and glutenin https://www.researchgate.net/profile/Frank-Bekes-2/publication/285263416_Chapter_1_Gluten_A_Balance_of_Gliadin_and_Glutenin/links/5e83c7354585150839b2be30/Chapter-1-Gluten-A-Balance-of-Gliadin-and-Glutenin.pdf
* Einhof (1805): gluten could be separated into two fractions, based on the extractability of gliadin in (70%) aqueous ethanol.
* a critical balance between the complementary roles of the gliadin and glutenin components 
* the gluten-forming proteins of the grain appear to serve no other role than to provide a reserve of amino acids for the developing seedling when germination occurs (storage proteins, providing a source of amino acids for the germinating grain.)
* Protein synthesis occurs on the ribosomes (attached to the endoplasmic reticulum) by the translation of the RNA nucleotide sequence, which in turn has been derived (transcribed) from the DNA sequence of the relevant genes on the chromosomes. 
* Peptide bonds are formed between appropriate amino acid
* The process of disulfide-bond formation (degree of polymerization) continues in the storage proteins during the ripening (desiccation) of the grain
* Disulfide-bond formation again accelerates during the heat treatment of processing e.g., baking or extrusion (a process by which a set of ingredients are forced through an opening in a plate, and is then cut by blades.); see Fig 2. 
* DOUGH FORMATION AND DEVELOPMENT
** Three components of dough: flour [flour is starch, protein and water], water and mixing. Other (yeast, salt, sugar, fat, etc) is not considered.
** Examination of flour under a microscope reveals that it varies widely in particle shape and size.
** Dough formation begins when water comes into contact with flour.
** Flour particle interact (stick together) to form a cohesive dough.
**# Dough mixing blends the ingredients into a homogeneous mass (at the super-molecular
level of structure)
**# Flour particles absorb water at a rate and amount depending on their water-binding capacity and the amount of water added
**# Mixing aids hydration by exposing new dry surfaces on flour particles for interaction with water.
**# Changes occur at the molecular level including interaction of gliadin and
glutenin and re-orientation of glutenin via S-S interchange
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Paywall: CW Wrigley, Nature 381, pages 738–739 (1996), 1996:  Giant proteins with flour power


Paywall: 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


Paywall: P.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




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




<youtube>SKtXURKDJjI</youtube>

=== 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 (C<sub>24</sub>H<sub>36</sub>O<sub>18</sub>), 
* caramelens (C<sub>36</sub>H<sub>50</sub>O<sub>25</sub>), and 
* caramelins (C<sub>125</sub>H<sub>188</sub>O<sub>80</sub>). 

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


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== Compounds ==

* glykoalkaloidi (Solaniini, Kakoniini)
* Kalsiumpropionaatti

== References ==

[https://en.wikipedia.org/wiki/List_of_cooking_techniques List_of_cooking_techniques]