Enzymes for Celiacs

[Guest guest]

I knew I had seen a few times that amylase helps people with celiac

disease with gluten but could never find anything substantial …until

now!!!

The following describes the situation with references. Apparently

the part of the gliadin in gluten that causes problems to a person

with celiac is not the protein, it is portions of carbohydrate.

Although the protein can antagonize the situation, the enzymes

needed are amylases and a some subgroups of amylases (other enzymes

that work on starch bonds). This correlates exactly to what we have

seen on the board. The proteases create more, smaller pieces but

would not necessarily break down the carbohydrate bonds (if at all),

thus making the situation for a celiac eating gluten with enzymes

worse than if they ate gluten without enzymes. It also follows that

some people with suspected celiac have done better with the the

amylase containing enzymes with gluten (like Zyme Prime – Dana? Is

this right). So a person with suspected celiac should be taking

enzymes for carbs with gluten contamination or infractions, not just

the proteases. If anyone with celiac happens to have the

<ahem> " opportunity " to try amylases with gluten, please post if

this helps. If this is true and holds up, the guidelines for a

person with celiac wanting to take enzymes for contamination should

be recommended the amylase/glucoamylase products.

I think this if very exciting and helpful! I checked several of the

references at Pubmed and the articles are listed there.

On pages 598-599 of the Pharmacology of Natural Medicines, there is

this information:

" It has been known since the 1950s that the gluten found in wheat,

rye and other grains is the cause of intestinal damage in celiac

disease, with the gliadin fraction of gluten being the source of its

toxicity. [references 1,2] By the 1970s, fractionation studies had

succeeded at identifying the components of gliadin involved in teh

toxic mechanism. The carbohydrate moiety, consisting mainly of

glucose, galactose, xylose and arabinose, is the source of gluten's

gastrointestinal toxicity in the celiac patient, rather than the

protein fraction as had been previously suspected. [3,4,5]

" Amylytic enzymes from Aspergillus species are effective in vitro in

the treatment of celiac disease, as they enzymatically cleave the

toxic carbohydrate portion of gliadin. Fungal carbohydrase

preparations render grains like wheat and rye virtually harmless to

individuals with gluten enterophathy.

A 1977 study attempting to identify the source of gliadin toxicity

used a preparation of amylytic enzymes from Aspergillus niger to

remove the carbohydrate portion of gliadin in vitro.

To be certain of the variables being tested, native gliadin was

chromatographed showing that carbohydrate was associated with four

main protein bands. When the carbohydrase-treated gliadin was

chromatographed, no alteration was detected in the protein pattern,

but carbohydrate was completely absent.

To further establish that the protein make-up remained unchanged as

compared with native gliadin, peptide mapping of the treated gliadin

was carried out using electrophoresis followed by chromatography.

Peptide maps showed no difference between the treated and untreated

gliadin, confirming that no alteration had occurred in the primary

structure of the protein.

Gliadin treated in this manner was baked into loaves of bread made

with gluten-free flour. The study compared the effect of bread with

treated versus untreated gliadin on four patients with previously

diagnosed celiac disease. All four patients had been on gluten-free

diets for at least 3 months prior to the study and were virtually

symptom-free. Previously, their clinical and physical signs and

symptoms had included the diarrhea, malabsorption, decreased body

weight and height, anemia, tetany, impaired D-xylose absorption,

decreased intestinal mucosal enzyme secretion flattened mucosal

brush-border and subepithelial tissue lymphocytosis typical of

celiac disease.

During the test period, patients 1,2, and 3 received a total of 50g

of treated gliadin baked into loaves of bread (10g gliadin/450 g

loaf). Xylose absorption tests and intestinal biopsies from jejunal

villi were performed before and after each test period.

The celiac patient receiving untreated gliadin (patient no 4)

experienced a return of signs and symptoms of celiac disease –

diarrhea, abdominal pain, low values on xylose absorption studies,

decreased mucosal enzyme secretion (alkaline phosphates, lactase,

surcease) and characteristic histological damage (mucosal

lumphocytosis and loss of enterocyte height). The patients who

received the treated glidin remained symptom-free during the test

period and showed no abnormalitites in histological parameters (i.e.

general morphology, epithelial cell height, tissue lymphocytes were

normal in these patients).

This study demonstrated that carbohydrate-digesting enzymes from

Aspergillus sp. can be used in vitro to remove the toxicity of

gluten to celiac patients and supports the hyypothsis that

carbohydrate components of gliadin are responsible for its toxicity,

rather than protein components as had been widely suspected. It

appears that no controlled studies have been done to evaluate the

effectiveness of amylytic fungal enzymes at reducing gluten toxicity

to celiac patients in vivo by administering these enzymes with

gluten containing foods at mealtime.

It should be noted that although celiac patients show intolerance to

the carbohydrate portion of gliadin, this is likely not he only

source of gluten-induced pathology. A number of studies suggest that

protein components of gluten produce systemic allergic

manifestations in some patients. It appears that both

gastrointestinal intolerance and immunological hypersensititity are

capable, either individually or in concert, of producing disease

symptoms in susceptible individuals. Future studies may also show

that both pathological mechanisms are amenable to treatment by

hydrolysis of the offending portions of gluten with the appropriate

orally administered fungal enzymes. This, however, remains to be

proven. "

1.Dicke WK. An investigation into the injurious constituents of

wheat in connection with their action on patients with Coeliac

disease. Acta Pediatr 1953; 42:223-231

2.Van De Kamer JH, Weijers HA, Coeliac disease: some experiments on

the cause of the harmful effect of the gliadin. Acta Pediatr 1955;

44: 465-469

3.Phelan JJ, s FM, McNicholl B et a. Coelic disease: the

abolition of gliadin toxicity by enzymes from Asergillus niger. Clin

Sci Molec Med 1977; 53: 35-43

4.McCarthy CF. Nutritional defects in patients with malabsorption.

Proc Nutr Soc 1976; 35:37-40

5.Phelan JJ. The nature of gliadin toxicity in celiac disease.

Biochem Soc Trans 1974; 2:1368-1370

6.Hekkens WTMJ et al. Antibodies to gliadin in serum of normals,

celiac patients and schizophrenics. Nature 1963; 199; 259-261