Chiba process with Mascarpone - Casein print

Walking with this idea in my head for a few days. In the fridge some expired Mascarpone.. Thinking just adding some FAC (25gr - 100ml) and some black acryllic paint.
Mixed it for some minutes and painted it on 200gr paper, dried with hair-dryer.
Some quick test with dried leaves in 30 minute UV exposure

Development with water and some Oxi-Action (this contains some H2O2) after some 10 minutes indeed the result I expected.
The Mascarpone hardened with the UV and FAC and the unexposed parts let go of the dye.

Perhaps some alternative for multi color prints?
I guess a variation on the Chiba process.
Next to try some 10% Yogurt

We will call it mascarponetype....

Isn't this stuff mostly fat - I guess there is enough of milk solids in there to make the image. It looks better than anything I I made with fish glue.

:Niranjan.

nmp said:

We will call it mascarponetype....

Isn't this stuff mostly fat - I guess there is enough of milk solids in there to make the image. It looks better than anything I I made with fish glue.

:Niranjan.

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I asked Bard:


The chemical composition of mascarpone cheese varies depending on the manufacturer, but it typically contains the following:

• Moisture: 44-50%
• Fat: 45-55%
• Protein: 7-8%
• Ash: 0.5-0.7%

Other components of mascarpone cheese include lactose, minerals, and lactic acid. The fat in mascarpone cheese is mostly saturated fat, followed by monounsaturated fat and polyunsaturated fat. The protein in mascarpone cheese is mostly casein.

: I have considered it is the acrylic paint polimerizing, but that does not wash off as well, still some effect but not as much.
I am surprised about the Ash as part of the ingredients though.

I will try some more papers I have coated yesterday let see what it brings.
Not sure if it will start to smell bad after some time also.

While I don't condone the misuse of cheese, no matter how expired, I applaud your experimenting!
Happy continued exploration!

nmp said:

We will call it mascarponetype....

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How about Tiramissutype?

MattKing said:

How about Tiramissutype?

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Now I am hungry....

Jan de Jong said:

I am surprised about the Ash as part of the ingredients though.

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Perhaps ash is a thickening agent - like activated ash or something. Or may be that's just the residue that stays during analysis that they lump as ash.

:Niranjan.

Interesting! I expect that yogurt will also work as would cottage cheese (aka pot cheese, alias curds & whey, etc). Casein, the major protein component of milk, is present in all cheese.

These softer cheeses will be easier to homogenize and therefore result in a more uniform coating on paper than would, say parmesan or gruyere for instance!

As for the use of "ash" in cheese making... wood ash is a traditional source of alkali used in many processes, soapmaking is the one that pops to mind immediately.

Dry ash say from the fireplace consists mainly of the oxides of the metals present in wood. Sodium, potassium, calcium and magnesium are most common metallic elements in living systems and thus wood ash would contain all of them. When these oxides encounter water they become hydroxides, which are "alkalis".

Not knowing much about cheese making specifically, but knowing much about proteins in general, I suspect that adding ash to the process aids in the formation of the curds. I could go on and bore you with more details about this aspect of biochemistry, but I'll stop there!

fgorga said:

I could go on and bore you with more details about this aspect of biochemistry, but I'll stop there!

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No, please, feel free to elaborate! This piques my interest.

Parmasan actually seems to have the highest casein content, but you would need to grind it very fine I guess to get an emulsion.

Some other things I have found:
- the acrylic paint has some polymerization properties also but less as in combination with the mascarpone.
- brush needs extra care for cleaning as it becomes greasy.
- print on coated paper should be done as soon as it has dried else it will polymerize as to be expected I guess, like casein paint.
- I will have to use a flatter paper to have better wash off of the unexposed emulsion.

Not sure if I will revisit it soon again although I still have a lot of the cheese left as it will only take a quarter spoon for 5 sheets or so.

Concerning use of cheese in prints in my view it is quite sustainable as it will create a long-term carbon capture as opposed to eating and digesting it.
On the point of wasting food however I agree, that is a no-go.

cheers
Jan.

"Ash" in food contents means "stuff that remains if the matter in question is burned". I.e. mineral content.

koraks said:

No, please, feel free to elaborate! This piques my interest.

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OK!

Native proteins have a specific conformation (shape) that is critical for its function. Different proteins have different shapes and therefore different functions.

There are a number of chemical "forces" that stabilize these native conformations.

The major one is the "hydrophobic effect". This is basically the idea that water and oil don't mix. Proteins fold up into their native shapes in order to minimize the exposure of the hydrophobic parts (i.e. the "oily bits") to the aqueous environment (i.e. the water).

Secondarily, native conformations are stabilized by hydrogen-bonding and ionic iterations within a protein molecule.

The folding of proteins into their native structures is much, much more complex (entire semester-long graduate-level biochemistry course complex!) than stated above, but for this discussion the above is all that is necessary.

If one disrupts the native structure of (i.e. denatures) proteins in solution, the hydrophobic parts are exposed to the water which is not 'good' energetically. This causes proteins to proteins in more-or-less random conformations to clump together in order to again minimize their exposure to water. Again... oil and water don't mix.

Bringing this back to cheese. If you gather enough clumps of denatured milk protein (mainly casein) together you get curds!

In cheese making (again I am no expert), proteins (mainly casein) can be denatured in a number of ways. Acids, bases and high salt concentrations will all denature proteins. Another way to denature proteins is partial digestion with enzymes (via the action of bacteria or using rennet). Heat will also denature proteins.

Different cheeses are made using different combinations these methods which affects the exact nature of the curds including their size, their firmness and especially the amount of fat entrapped in the curds. Those curds are, of course, further processed to get the wonderful variety of cheeses we have.

I hope that this explanation is what you were looking for.

@fgorga - great, many thanks! This is really interesting. The reason why I'm asking is because I do a lot of carbon transfer printing, where the processes you mention seem to play a vital role as well. Sometimes I hit upon things I can't really explain very well for a lack of theoretical awareness of the processes involved. Carbon transfer, as you probably know, revolves around selectively hardening gelatin. While this is not longer protein, I understand that the mechanisms involved still overlap significantly with the theory of protein folding given that the gelatin still consists of peptide chains, which are subject to the same effects that also play a role in protein folding.

For instance, in carbon transfer, two often-used hardening agents are dichromate and diazostilbene (DAS). One thing that I ran into (and I surely wasn't the first to notice) is that layers of protein of the same thickness hardened with dichromate vs DAS behave quite differently, with the DAS-hardened layers being far more fragile and likely to wash away during hot water development. I always assumed that a certain degree of hardening would be more or less the same regardless of how the hardening occurred (through which agent or process), but there appear to be distinct qualitative differences in hardening even for the same quantitative degree (if that makes sense).

In order to understand such effects (I mentioned just one), knowledge of protein behavior and the mechanisms involved in folding seems vital. Hence my interest - although sadly, I'm still far from knowledgeable enough even to start asking relevant questions.

Btw, if it's bothersome to anyone that this goes beyond the original topic of using cheese curds to make prints, don't hesitate to hit 'report' to indicate so, and I'll split off the digression into a new thread.

@koraks

As you might know the major component of gelatin is partly hydrolyzed collagen.

Collagen is an unusual protein. First, it is a fibrous protein. Most proteins have a globular structure. However, the native structure of collagen is long and narrow, sort of like a sphagetti. Second, collagen has a very stable structure. It is difficult to denature.

The partial hydrolysis which converts collagen into gelatin results in shortening the fibers but leaving its structure more-or-less intact. This results in a molecule that is water soluble at higher temperatures but turns into a gel at cooler temperatures, as I am sure you are well aware!

The formation of the gel occurs because the fragments of collagen stick to one another. These interactions are relatively weak (and thus reversible). In chemical terms these interactions are non-covalent.

The hardening of gelatin involves stabilizing the gel by introducing stronger (covalent) bonds between the collagen fragments... i.e. cross-linking them together.

There are many ways to harden gelatin. The gelatin in traditional silver-gelatin emulsions is hardened using formaldehyde or glutaraldehyde. This reaction is not dependent on light.

Dichromate is the traditional way to harden gelatin in a light dependent reaction.
DAS will also introduce cross-links between collagen fragments in a light dependent manner.

However, the nature of the cross-links made by the two compounds are very different (both in their chemical details and in their frequency). Thus the behavior of hardened layers made by different methods are likely to be similar (especially in terms of trapping pigment) but not exactly the same.

Lastly, it might be worth noting that the chemistry of gum printing is, at one level, similar to that described above even though gum is a carbohydrate polymer and not a protein (an amino acid polymer). In other words gum arabic is a long thin molecule that is cross-linked to make it insoluble while trapping pigment particles to form an image.

@fgorga and @koraks

Thank you for more detail on this, I have read it with interest. Of course I more or less approached it from a fun point to see if it would give some results. My interest however is if it would have been possible in an ancient past before the current photographic processes, that there would have been already a means to produce images or photogramms. I think there must have been occasions where for example the Romans, Greek or Chinese would have noticed paint bleaching in sunlight and not in the shaded parts. Similar a process based on milk or cheese could have been found.
Not sure if there is any evidence that it has been found, but I think the possible access to this and hopefully also the wish to make a photo or shadow print in the ancient times looks possible.
anyway just a thought ;-)

Jan de Jong said:

I think there must have been occasions where for example the Romans, Greek or Chinese would have noticed paint bleaching in sunlight and not in the shaded parts

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Like anthotypes. Yes, I imagine this must have occurred to people across history from time to time. I never looked into historical records, and there's still a difference between a contact print of an object (think of the 19th century cyanotype leaf studies that were at the cradle of modern photography) vs a photograph representing a scene. Concerning the latter, there are rather persistent allegations that many of the 17th masters (e.g. Vermeer) used optical devices such as the camera obscura to set up their compositions.