The Travis Corner

[Wagner83]

[...]
Those Okinawans ate tubers . . . and they really do seem better than grains, rice, and corn.
[...]

This is what he had implied, but this idea is seemingly based off the theoretical mental activity of only one person. I suppose you could see it going both ways, but I think he had mainly included this line of thinking to bolster his argument. He was, after all, shamelessly pimping his brand of enzymes to the point of making emotional appeals in a patent application.
I saw them online and had thought I might experiment with them someday.

The three main objections to dairy are: (1) There can be immunogenic peptide fragments released; (2) There can be opiate peptides released, and; (3) There can be enough androgens to cause acne. Prolyl peptidase enzymes could be expected to overcome objections #1 and #2.

From your posts on corn and rice I did not think you valued them much less than potatoes, of course potatoes have more minerals, proteins, keto acids and vitamins but still, in terms of erring on the side of caution I did not think potatoes would be way ahead of white jasmine rice and nixtamalized (or not) corn.

Ok thanks.

About #3, if you are interested haidut's take on it was that it raises dhea in a lot of people, and that estrogenic metabolites of dhea resulted in acne as dht does not cause acne but may help cure it.

 

[BenPatrick]

I’ve been pondering any potential downsides of my rekindled romance with dates as of late, as I have a fear— fueled by claims made by former fruitarians that dates and citrus provided them with an unnerving number of dental carries— that I could be asking for trouble, dentally speaking.

Have you run into any issues regarding dates and dental health? I sure hope not, but I’m curious to look into it when I get home.

 

[Travis]

I’ve been pondering any potential downsides of my rekindled romance with dates as of late, as I have a fear— fueled by claims made by former fruitarians that dates and citrus provided them with an unnerving number of dental carries— that I could be asking for trouble, dentally speaking.

Have you run into any issues regarding dates and dental health? I sure hope not, but I’m curious to look into it when I get home.

I think you should be more worried about candy . . . or even rice. Dates have fiber, no starch, and don't readily stick to teeth.

 

[Fractality]

Pineapples from Thailand, and especially Bangkok, can spread herpes (kidding; Navy joke.)

But seriously, this stops with repeated pineapple‐eating. Perhaps it is bromelain breaking‐down the collagen of the skin?

Ketnawa, Sunantha. "Two phase partitioning and collagen hydrolysis of bromelain from pineapple peel Nang Lae cultivar." Biochemical Engineering Journal (2010)​

It appears that bromelain does have collagenase activity:

'The bromelain extract was applied to hydrolyze the skin collagen of beef and giant catfish (0–0.3 units). The β, α₁, and α₂ of giant catfish skin collagen extensively degraded into small peptides when treated with 0.02 units of the bromelain extract. Bovine collagen was hydrolyzed using higher bromelain up to 0.18 units.' ―Ketnawa​

It appears as if these properties of bromelain have not been entirely neglected by dermatologists:

'It has been known for clinical and therapeutic applications, particularly for modulation of tumor growth and third degree burns [3]. In cosmetic industries, bromelain is used as active ingredient to provide gentle peeling effect [10].' ―Ketnawa​

So one could read about Ketnawa's in vitro collagen experiments, or perhaps get some first‐hand accounts from dermatologists:

Maurer, H. R. "Bromelain: biochemistry, pharmacology and medical use." Cellular and Molecular Life Sciences (2001)​

...in an article such as this:

'This is also true for bromelain effects on the modulation of immune functions, its potential to eliminate burn debris and to accelerate wound healing.' ―Maurer

'They modulate the functions of adhesion molecules on blood and endothelial cells, and also regulate and activate various immune cells and their cytokine production.' ―Maurer​

Although having superimposable names, the bromelain of the stem is in fact a different protein than the bromelain of the pulp.

'Stem-bromelain (EC. 3.4.22.32) is distinguished from fruit-bromelain (EC. 3.4.22.33), previously called bromelin [2].' ―Maurer

'The substrate spectrum is similarly broad, extending from synthetic low molecular mass amides and dipeptides up to high molecular substrates such as fibrin, albumin, casein, angiotensin II, bradykinin. Bromelain preferentially cleaves glycyl, alanyl and leucyl bonds.' ―Maurer​

So we are not limited to collagen. Bromelain appears capable of cleaving peptide bonds at short‐chain nonpolar amino acids. No mention is made of proline, and due to the unusual nature of the prolyl peptide bond the omission of such could perhaps be taken as synonymous with 'it don't.'

Maurer then provides a litany expounding the wonderful benefits of bromelain.

'From a variety of in vitro and animal experiments, mainly with rodents, as well as from clinical observations, based on uncontrolled and controlled studies, the general properties of bromelain may be summarized as follows: Bromelain:

– prevents edema formation and reduces existing edemas
– reduces the blood level of fibrinogen
– supports fibrinolysis
– activates plasmin
– prolongs the prothrombin and partial thromboplastin time (after relatively high doses)
– prevents aggregation of blood platelets
– prevents adhesion of platelets to endothelial cells of blood vessels
– reduces the blood level of plasmakinins
– reduces the level of prostaglandine E₂ and of thromboxane A₂ in exsudates during acute inflammation
– acts as an antiinflammatory agent
– induces the secretion of interleukin Il-1, Il-6, Il-8 and tumor necrosis factor alpha (TNFα) from blood monocytes and granulocytes
– supports the oxidative burst and the cytotoxicity of granulocytes against tumor cells
– increases the tissue permeability of antibiotic drugs
– prevents metastases in a mouse model
– supports skin debridement of burns

Some effects of bromelain may result from its capacity to alter and modulate distinct cell surface structures by cleaving off peptides [15]. Thus, the bromelain-mediated modification of adhesion molecules on platelets and on other normal and malignant tumor cells may inhibit their aggregation. The dissolution of cell membrane constituents and the effects on components of hemostatic processes may explain antiedemateous and fibrinolytic phenomena.' ―Maurer​

'Bromelain was more effective than chymotrypsin, papain and trypsin.' ―Maurer​

'Topical bromelain (35% in a lipid base) has achieved complete debridement on experimental burns in rats in about 2 days, as compared with collagenase, which required about 10 days, with no side effects or damage to adjacent burned tissue [67].' ―Maurer

'Is bromelain absorbed following oral application? This frequently asked question can now be answered in the affirmative. In 1992, Smyth et al. [20] showed that bromelain given orally to rabbits increases the plasmin serum level and prolongs the prothrombin and antithrombin times. Seifert et al. [70] found that up to 40% of ¹²⁵I-labelled bromelain is absorbed from the intestine in high molecular form. Later, by means of different methods, a large body of direct and indirect evidence supported the conclusion that bromelain is absorbed from the intestine.' ―Maurer​

Bromelain is absorbed in high molecular form. In the blood, it is capable of reducing fibrin adhesion. Pauling and Rath readers out there will tell you that fibrin is more‐or‐less synonymous with its molecular cousin lipoprotein(a), similar in that they both have the lysine kringle binding domain conferring to them artery‐binding propensities. Pauling mechanics indicate that this adhesion to frayed collagen of the arterial wall is to prevent blood loss in the case of scurvy, an idea justified by the fact that lipoprotein(a) is upregulated in the event of ascorbate deficiency.

This proteolytic pineapple effect coupled with its high‐vitamin C content is probably sufficient to propel the pineapple to the #1 spot—or to the apex of the cartoon fruit cheerleader pyramid (bananas occupying the base)—in the prevention of cardiovascular disease . . . and perhaps even, if I dare say, its reversal.*

Now for the paragraph we have all been waiting our entire lives for:

'Finally: Why do pineapple plants produce and need bromelain? The significance of bromelain proteinases for pineapples has been a mystery for a long time. The most compelling hypothesis is based on the well-known fact that carnivorous plants derive their supply of nitrogen and phosphorus from degradation of organic material (foliage, insects, microbes) by means of highly active proteinases and other digesting enzymes. In the tropical jungle, the pineapple plant is an epiphytic bromeliad, growing on other plants which offer hardly any nutrients. The rosettelike arrangement of the pineapple plant’s leaves forms funnel-type rainwater reservoirs, so-called phytotelmata, that are always filled with water, as well as with nitrogen and phosphorus suppliers. This hypothesis is supported by recent findings that leaves react to mechanical stimuli of only 2 s by producing proteinkinases [86]. Moreover, the carnivorous pitcher plant Sarracenia purpurea was shown to respond to various chemical signals (nucleic acids, proteins, ammonia) by secreting hydrolytic enzymes [87]. In order to digest as many proteins from insects and microorganisms as possible, enzyme ‘families’ with a broad spectrum of pH optima, such as the ‘papain superfamily’, have evolved.' ―Maurer​

Insects abound in the tropical jungle, and the pineapple bromeliad does want their amino acids. Perhaps its not too hard to imagine that some amino acids of bromelain itself had previously constituted an insect—digested beforehand by yet another, independent bromelain predecessor.

[*] This statement has not been evaluated by the FDA. ​

Interesting and detailed reply! I wonder why the corners of the mouth are affected but not the rest of the mouth/lips? Is it from topical exposure? I do eat slices of pineapple and invariably the corners of my mouth touch the pineapple and its juice.

 

[Travis]

Interesting and detailed reply! I wonder why the corners of the mouth are affected but not the rest of the mouth/lips? Is it from topical exposure? I do eat slices of pineapple and invariably the corners of my mouth touch the pineapple and its juice.

I don't know, but it has to be the bromelain enzyme. I really don't think there is any other molecule characteristic to pineapples that could potentially do this, and it's used in dermatology specifically to cleave peptide bonds of the skin.

But the papaya appears to be even better. It has a more moderate pH, more vitamin C, some carotenes, and even a proteolytic enzyme of its own: papain, which isn't correlated with mouth sores (for whatever reason; enzymes do have idiosyncrasies, and preferentially cleave peptides at certain amino acids.) I used to buy more papaya than pineapple when I lived next to that Asian store, but where I shop now the pineapples are about ¹⁄₂ the price per calorie.

Perhaps it has something to do with mouth fluid dynamics? with bromelain in the mouth being diluted except for at the corners, where bromelain is allowed to act for hours . . . mindlessly cleaving collagen with no remorse.

 

[Fractality]

I don't know, but it has to be the bromelain enzyme. I really don't think there is any other molecule characteristic to pineapples that could potentially do this, and it's used in dermatology specifically to cleave peptide bonds of the skin.

But the papaya appears to be even better. It has a more moderate pH, more vitamin C, some carotenes, and even a proteolytic enzyme of its own: papain, which isn't correlated with mouth sores (for whatever reason; enzymes do have idiosyncrasies, and preferentially cleave peptides at certain amino acids.) I used to buy more papaya than pineapple when I lived next to that Asian store, but where I shop now the pineapples are about ¹⁄₂ the price per calorie.

Perhaps it has something to do with mouth fluid dynamics? with bromelain in the mouth being diluted except for at the corners, where bromelain is allowed to act for hours . . . mindlessly cleaving collagen with no remorse.

I'll have to experiment and see if eating bite size chunks of pineapple still produce the mouth sores. Why would I even have peptides I just ate my half pineapple in the form of circular slices for the day and the corners of my mouth are stinging. I'm going to check for papaya next time I go to the local Asian grocer. The mangoes are too hit and miss at this time. Perhaps the papayas are more cost effective than the pineapples...I've been paying $2.99 per pineapple.

 

[Wagner83]

Perhaps it has something to do with mouth fluid dynamics? with bromelain in the mouth being diluted except for at the corners, where bromelain is allowed to act for hours . . . mindlessly cleaving collagen with no remorse.

A flesh-eating fruit, I knew the fruitarian diet was not safe.
This reminds me of this abstract:
[Does garlic protect against vampires? An experimental study]. - PubMed - NCBI

Spoiler: Abstract

Abstract
Vampires are feared everywhere, but the Balkan region has been especially haunted. Garlic has been regarded as an effective prophylactic against vampires. We wanted to explore this alleged effect experimentally. Owing to the lack of vampires, we used leeches instead. In strictly standardized research surroundings, the leeches were to attach themselves to either a hand smeared with garlic or to a clean hand. The garlic-smeared hand was preferred in two out of three cases (95% confidence interval 50.4% to 80.4%). When they preferred the garlic the leeches used only 14.9 seconds to attach themselves, compared with 44.9 seconds when going to the non-garlic hand (p < 0.05). The traditional belief that garlic has prophylactic properties is probably wrong. The reverse may in fact be true. This study indicates that garlic possibly attracts vampires. Therefore to avoid a Balkan-like development in Norway, restrictions on the use of garlic should be considered.

 

[Amazoniac]

Casein Allergy
Food-derived opioid peptides inhibit cysteine uptake with redox and epigenetic consequences

 

[Travis]

Casein Allergy
Food-derived opioid peptides inhibit cysteine uptake with redox and epigenetic consequences

Do you know if an immunogenic peptide can release cytokines, or mast cells, and yet not form antibodies against said peptide?

 

[EIRE24]

Travis, any new findings on acne or do you still think dairy and androgens are the main culprits?

 

[Travis]

Travis, any new findings on acne or do you still think dairy and androgens are the main culprits?

Well, @Koveras has informed me of the undeniable role of IGF‐1. After a few exchanges it had been determined that they both induce acne in the exact same way, and that is activate the transcription factor SREBP. Both androgens and IGF‐1 increase squalene synthesis through the same transcription factor, and also upregulate the enzyme wax ester synthase. If you look at the hard chemical data, it's plain that the sebum from people with acne is characterized by increased wax esters and often triglycerides with a corresponding reduction in free fatty acids; in short, larger lipids are produced which raise the viscosity of the sebum—leading to a clog. I find all experimental evidence superimposable over this mechanism without contradiction; this seems to be a quite logical physical‐chemical explanation, linking the biological to the physical. With lowered viscosity and melting point, you have the propensity for pore clogging at lower temperature.

It should be no surprise that two things which activate SREBP are most correlated with acne. The role of androgens is undeniable, as is the role of IFG‐1. This would make the 'acne diet' high in dairy and sugar/starch, perhaps milk chocolate would be the most reliable way to induce acne as it has both.. .

Eliminating acne is then simple: Reduce insulin spikes and reduce androgen consumption . . . or try reducing one or the other.

 

[Travis]

The answer is yes: there are both IgE and non‐IgE immune reactions, as can read about here:

Sabra, Aderbal. "IgE and non-IgE food allergy." Annals of Allergy, Asthma & Immunology (2003)​

We only have a finite amount of nascent T‐helper cells (Th₀), produced in the thymus and circulated throughout the body. These cells will differentiate further to either Th₁ cells or Th₂ cells: two species producing different products. The Th₁ cells produce interferon-γ and interleukin-1, among others, and the Th₂ cells are what produce interleukin-4 and the IgE antibodies (among others.) Many people respond to food peptides, but the Th₁/Th₂ ratio largely determines what cytokines and antibodies are produced—and hence both the response and clinical blood profile. Although IgE levels alone are generally considered diagnostic of 'food allergy,' this definition commonly fails. Perhaps the most outrageous immune response—celiac disease—is characterized by INF-γ with often moderate or even subnormal IgE concentrations. Thus: charts and tables of allergic prevalence based on circulating IgE levels alone, as most are, are an underestimate of the true prevalence of food-initiated immunological reactions.

'At present, non–IgE mediated gastrointestinal reactions to food proteins are less well studied than other food allergies.' ―Nowak-Węgrzyn​

Perhaps even more troublesome is that most writers on food allergy use an en dash (–) when they should use a hyphen (‐). And it gets worse: Not to be outdone by most immunologists, Aderbal Sabra uses the longer em dash—perhaps as Freudian compensation for being female:

'Recent studies from our group have suggested a link between attention-deficit-hyperactive disorder, ileal-lymphoid-nodular hyperplasia, and
non—IgE-mediated FA.' ―Sabra​

So non‐IgE immunological reactions do occur. Since the lack of IgE antibodies means lack of Th₂ cells, and thus more Th₁ cells, you'd expect this to be characterized by INFγ—exactly as seen. Gamma interferon is part of the 'cell‐mediated immunity,' a particle which transfers to cells and upregulates the enzyme phospholipase A₂. This enzyme has one function only, and that is to release the lipid occupying the sn‐2 position of membrane phopholipids. Arachidonic acid is generally found in this postition, but hopefully our cells have a bit more eicosapentaneoic acid and Mead acid; these two lipids form safer eicosanoids upon release. Arachidonic acid forms the most problematic eicosanoid subclassification: the prostaglandins, which can be seen as oxygenated lipids purposefully‐created to destroy pathogens. Plants make similar peroxygenated lipids upon attack, called lipoxins; so cytokines can be seen to forming the link between circulating T‐cell immunity and the periphery by collectively upregulating a suite defensive enzymes: cyclooxygenase‐2, inducible nitric oxide synthase, and tryptophan dioxygenase are a few other cytokine‐induced enzymes transcribed for defense. A powerful induction of COX‐2 and PLA₂ can cause hair loss and cancer (prostaglandins), vascular disease in the case of iNOS (nitric oxide), and muscle wasting and depression in the case of TDO (very low tryptophan). All of this can happen without clinical IgE‐mediated food allergy, or 'allergy' as commonly defined. For these reasons, I believe the distinction between 'immunogenicity' and 'allergy' should be made; perhaps these should be mentally separated, with INFγ kept in the cell‐mediated paradigm and IgE in the humoral. This is how most immunologists appear to see things, despite their imprudent use of dashes.

Nowak-Węgrzyn, Anna. "Non–IgE-mediated gastrointestinal food allergy." Journal of Allergy and Clinical Immunology (2015)
Rowley, Arthur Frederick. "Eicosanoids and related compounds in plants and animals." Princeton University Press (2015)

Typographic horizontal lines—and their names!

The horizontal bar: ―
The em dash: —
The en dash: –
The figure dash: ‒
They hyphen: ‐
The non‐breaking hyphen: ‑
The minus sign: −
The wave dash: 〜​

 

[Blossom]

Pineapples from Thailand, and especially Bangkok, can spread herpes (kidding; Navy joke.)

But seriously, this stops with repeated pineapple‐eating. Perhaps it is bromelain breaking‐down the collagen of the skin?

Ketnawa, Sunantha. "Two phase partitioning and collagen hydrolysis of bromelain from pineapple peel Nang Lae cultivar." Biochemical Engineering Journal (2010)​

It appears that bromelain does have collagenase activity:

'The bromelain extract was applied to hydrolyze the skin collagen of beef and giant catfish (0–0.3 units). The β, α₁, and α₂ of giant catfish skin collagen extensively degraded into small peptides when treated with 0.02 units of the bromelain extract. Bovine collagen was hydrolyzed using higher bromelain up to 0.18 units.' ―Ketnawa​

It appears as if these properties of bromelain have not been entirely neglected by dermatologists:

'It has been known for clinical and therapeutic applications, particularly for modulation of tumor growth and third degree burns [3]. In cosmetic industries, bromelain is used as active ingredient to provide gentle peeling effect [10].' ―Ketnawa​

So one could read about Ketnawa's in vitro collagen experiments, or perhaps get some first‐hand accounts from dermatologists:

Maurer, H. R. "Bromelain: biochemistry, pharmacology and medical use." Cellular and Molecular Life Sciences (2001)​

...in an article such as this:

'This is also true for bromelain effects on the modulation of immune functions, its potential to eliminate burn debris and to accelerate wound healing.' ―Maurer

'They modulate the functions of adhesion molecules on blood and endothelial cells, and also regulate and activate various immune cells and their cytokine production.' ―Maurer​

Although having superimposable names, the bromelain of the stem is in fact a different protein than the bromelain of the pulp.

'Stem-bromelain (EC. 3.4.22.32) is distinguished from fruit-bromelain (EC. 3.4.22.33), previously called bromelin [2].' ―Maurer

'The substrate spectrum is similarly broad, extending from synthetic low molecular mass amides and dipeptides up to high molecular substrates such as fibrin, albumin, casein, angiotensin II, bradykinin. Bromelain preferentially cleaves glycyl, alanyl and leucyl bonds.' ―Maurer​

So we are not limited to collagen. Bromelain appears capable of cleaving peptide bonds at short‐chain nonpolar amino acids. No mention is made of proline, and due to the unusual nature of the prolyl peptide bond the omission of such could perhaps be taken as synonymous with 'it don't.'

Maurer then provides a litany expounding the wonderful benefits of bromelain.

'From a variety of in vitro and animal experiments, mainly with rodents, as well as from clinical observations, based on uncontrolled and controlled studies, the general properties of bromelain may be summarized as follows: Bromelain:

– prevents edema formation and reduces existing edemas
– reduces the blood level of fibrinogen
– supports fibrinolysis
– activates plasmin
– prolongs the prothrombin and partial thromboplastin time (after relatively high doses)
– prevents aggregation of blood platelets
– prevents adhesion of platelets to endothelial cells of blood vessels
– reduces the blood level of plasmakinins
– reduces the level of prostaglandine E₂ and of thromboxane A₂ in exsudates during acute inflammation
– acts as an antiinflammatory agent
– induces the secretion of interleukin Il-1, Il-6, Il-8 and tumor necrosis factor alpha (TNFα) from blood monocytes and granulocytes
– supports the oxidative burst and the cytotoxicity of granulocytes against tumor cells
– increases the tissue permeability of antibiotic drugs
– prevents metastases in a mouse model
– supports skin debridement of burns

Some effects of bromelain may result from its capacity to alter and modulate distinct cell surface structures by cleaving off peptides [15]. Thus, the bromelain-mediated modification of adhesion molecules on platelets and on other normal and malignant tumor cells may inhibit their aggregation. The dissolution of cell membrane constituents and the effects on components of hemostatic processes may explain antiedemateous and fibrinolytic phenomena.' ―Maurer​

'Bromelain was more effective than chymotrypsin, papain and trypsin.' ―Maurer​

'Topical bromelain (35% in a lipid base) has achieved complete debridement on experimental burns in rats in about 2 days, as compared with collagenase, which required about 10 days, with no side effects or damage to adjacent burned tissue [67].' ―Maurer

'Is bromelain absorbed following oral application? This frequently asked question can now be answered in the affirmative. In 1992, Smyth et al. [20] showed that bromelain given orally to rabbits increases the plasmin serum level and prolongs the prothrombin and antithrombin times. Seifert et al. [70] found that up to 40% of ¹²⁵I-labelled bromelain is absorbed from the intestine in high molecular form. Later, by means of different methods, a large body of direct and indirect evidence supported the conclusion that bromelain is absorbed from the intestine.' ―Maurer​

Bromelain is absorbed in high molecular form. In the blood, it is capable of reducing fibrin adhesion. Pauling and Rath readers out there will tell you that fibrin is more‐or‐less synonymous with its molecular cousin lipoprotein(a), similar in that they both have the lysine kringle binding domain conferring to them artery‐binding propensities. Pauling mechanics indicate that this adhesion to frayed collagen of the arterial wall is to prevent blood loss in the case of scurvy, an idea justified by the fact that lipoprotein(a) is upregulated in the event of ascorbate deficiency.

This proteolytic pineapple effect coupled with its high‐vitamin C content is probably sufficient to propel the pineapple to the #1 spot—or to the apex of the cartoon fruit cheerleader pyramid (bananas occupying the base)—in the prevention of cardiovascular disease . . . and perhaps even, if I dare say, its reversal.*

Now for the paragraph we have all been waiting our entire lives for:

'Finally: Why do pineapple plants produce and need bromelain? The significance of bromelain proteinases for pineapples has been a mystery for a long time. The most compelling hypothesis is based on the well-known fact that carnivorous plants derive their supply of nitrogen and phosphorus from degradation of organic material (foliage, insects, microbes) by means of highly active proteinases and other digesting enzymes. In the tropical jungle, the pineapple plant is an epiphytic bromeliad, growing on other plants which offer hardly any nutrients. The rosettelike arrangement of the pineapple plant’s leaves forms funnel-type rainwater reservoirs, so-called phytotelmata, that are always filled with water, as well as with nitrogen and phosphorus suppliers. This hypothesis is supported by recent findings that leaves react to mechanical stimuli of only 2 s by producing proteinkinases [86]. Moreover, the carnivorous pitcher plant Sarracenia purpurea was shown to respond to various chemical signals (nucleic acids, proteins, ammonia) by secreting hydrolytic enzymes [87]. In order to digest as many proteins from insects and microorganisms as possible, enzyme ‘families’ with a broad spectrum of pH optima, such as the ‘papain superfamily’, have evolved.' ―Maurer​

Insects abound in the tropical jungle, and the pineapple bromeliad does want their amino acids. Perhaps its not too hard to imagine that some amino acids of bromelain itself had previously constituted an insect—digested beforehand by yet another, independent bromelain predecessor.

[*] This statement has not been evaluated by the FDA. ​

Pre-Peat in 2006 I had pelvic surgery. I was taking bromelain post-op because I had gotten the idea somewhere that taking the enzyme would help my recovery. When I went for my follow up visit my recovery was apparently going so much better than most of this physician's patients that he commented on it. I obviously wasn't in excellent health at the time so maybe the bromelain really did help. You're explanation does lead me to believe bromelain had a positive impact.

 

[Amazoniac]

perhaps as Freudian compensation for being female

Travis, I didn't have anything to add: I had no idea.

I forgot to include this:
Formation and Degradation of Beta-casomorphins in Dairy Processing

And later came across these:
Systematic Review of the Gastrointestinal Effects of A1 Compared with A2 β-Casein | Advances in Nutrition | Oxford Academic (updated review involving Keith Woodford)

Impact of milk-derived b-casomorphins on physiological functions and trends in research: A review
If BCM-7 has similar effects on a Holstein calf, then those are justified: it must have a good purpose indeed, but nothing can be said about its usefulness when you steal the milk, curdle, discart the liquid, add salt, accidentally drop it on the floor, recover (5 sec rule), let it age and then grate on top of pasta with meat and tomato sauce.

 

[Travis]

Pre-Peat in 2006 I had pelvic surgery. I was taking bromelain post-op because I had gotten the idea somewhere that taking the enzyme would help my recovery. When I went for my follow up visit my recovery was apparently going so much better than most of this physician's patients that he commented on it. I obviously wasn't in excellent health at the time so maybe the bromelain really did help. You're explanation does lead me to believe bromelain had a positive impact.

You know, I was quite surprised that it was absorbed 'in high molecular form.' There seems to be a prevailing myth that proteins are broken down into amino acids in the body, but this cannot be true in all cases. It is very easy to find evidence of 7‐amino acid peptide chains in the blood, and the notorious 33‐mer is the most antigenic gluten peptide. And just a few minutes ago, I saw an article that go me thinking about IFG‐1. Milk contains this growth factor, which is increased by rBGH, and milk also raises IFG‐1 in humans. Since bovine and human IFG‐1 are identical, there is actually some dispute as to whether this protein is absorbed whole.

And I do remember reading something along these lines a few years ago, in a Ray Peat article:

'The absorption of immunologically intact proteins and other particles has been demonstrated many times, but myth is more important than fact; all of my biology professors, for example, denied that proteins could be absorbed by any part of the digestive system.' ―Ray Peat​

I have seen experimental evidence of β-casomorphin-11 in the brain, proving that a peptide this long can be absorbed, but have yet to see much experimental data for whole proteins over 200 amino acids like IFG‐1 and bromelain. Perhaps I should make myself 100% convinced of this by crawling through to footnotes of these articles and reading the experiments themselves.

I can see a protelytic enzyme increasing tissue remodeling. It could break down damaged proteins while providing the amino acids for new ones. These must be constantly replaced, as random chemical adducts in the body age proteins; many collagen crosslinks known for the strength they contribute come only later after methylglyoxal addition. Papayas and pineapples provide both proteolytic enzymes and vitamin C, a vitamin shown to increase the rate of collagen synthesis over fourfold in some experiments.

Peat, Ray. "Food-junk and some mystery ailments: Fatigue, Alzheimer's, Colitis, Immunodeficiency." raypeat.com (c. 2006)
Spanheimer, R. G. "A specific decrease in collagen synthesis in acutely fasted, vitamin C-supplemented, guinea pigs." Journal of Biological Chemistry (1985)​

 

[Travis]

Travis, I didn't have anything to add: I had no idea.

I forgot to include this:
Formation and Degradation of Beta-casomorphins in Dairy Processing

And later came across these:
Systematic Review of the Gastrointestinal Effects of A1 Compared with A2 β-Casein | Advances in Nutrition | Oxford Academic (updated review involving Keith Woodford)

Impact of milk-derived b-casomorphins on physiological functions and trends in research: A review
If BCM-7 has similar effects on a Holstein calf, then those are justified: it must have a good purpose indeed, but nothing can be said about its usefulness when you steal the milk, curdle, discart the liquid, add salt, accidentally drop it on the floor, recover (5 sec rule), let it age and then grate on top of pasta with meat and tomato sauce.

Did you know that some strains of Lactobacilli commonly used in sourdough fermentation can destroy the immunogenicity of gluten, and perhaps even its exorphin properties? Although the exorphin peptides are smaller than the antigens, I think perhaps you could see some reductions (one particular strain of L. Casei completely degraded gliadin into individual amino acids within 12 hours.)

 

[Amazoniac]

Did you know that some strains of Lactobacilli commonly used in sourdough fermentation can destroy the immunogenicity of gluten, and perhaps even its exorphin properties? Although the exorphin peptides are smaller than the antigens, I think perhaps you could see some reductions (one particular strain of L. Casei completely degraded gliadin into individual amino acids within 12 hours.)

Did you know that Élie Metchnikoff was giving people lactic acid bacteria, while Koch mentioned that those in fact create a favorable environment for biogenic amine generation? One that selects bacteria that can thrive on sulfur compounds for example, dispensing even the need for iron if I remember correctly.
Endotoxin And Fat Consumption
Meats for sale appear to only start being a source of biogenic amines once the glycogen is decomposed.

 

[Travis]

Did you know that Élie Metchnikoff was giving people lactic acid bacteria, while Koch mentioned that those in fact create a favorable environment for biogenic amine generation? One that selects bacteria that can thrive on sulfur compounds for example, dispensing even the need for iron if I remember correctly.
Endotoxin And Fat Consumption
Meats for sale appear to only start being a source of biogenic amines once the glycogen is decomposed.

Do you remember the data on bacteria and polyamine production? Only some strains of bacteria can produce polyamines, and only a few select others are capable of cleaving proline peptide bonds. You'd think the intestinal biome would matter a great deal, but even more in those consuming a high protein diet.

There's an interesting study out there showing boiled meat to be a greater risk factor for colon cancer than grilled. This apparently places Koch's diamines higher than 'polycyclic aromatic hydrocarbons' as a cause, what are commonly thought to be the greatest risk factor. Obviously, boiled meat has no PAHs but would likely have more linoleic acid and different diamine kinetics. Ray Peat had mentioned that linoleic acid becomes conjugated linoleic acid upon grilling, or course destroying its prostaglandin potential in the process.

Meat more‐or‐less gets a free ride on this forum, but it is associated with colon cancer. Selenomethionine can displace methionine, eliminating polyamine production in a totally safe manner. Many of the protein amino acids in our body are in fact selenomethionine, a fact commonly forgotten since protein sequences only list sulfur‐methionine where it could rightly be either. There seems to be no limit to how many methionines can be replaced by selenomethionine, and Asians are found to have about 7× the amount in structural proteins. The associations between cancer and selenomethionine are quite good, really.

de Verdier, Maria Gerhardsson. "Meat, cooking methods and colorectal cancer: a case‐referent study in Stockholm." International Journal of Cancer (1991)​

 

[danishispsychic]

" Shotguns, alligators, and blowtorches can cure cancer if used properly."- best sentence EVER right there.

 

[Wagner83]

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