Isomaltase Deficiency & Solution
The human digestive tract contains seven enzymes which split dietary disaccharides into free monosaccharides: trehalase [EC 188.8.131.52] which acts on the sugar trehalose that comes from fungi and yeast; lactase [EC 184.108.40.206] which acts on lactose (milk sugar); and phlorizin hydrolase [EC 220.127.116.11], which are all contained with the beta-glucosidase complex; glycoamylase complex [EC 18.104.22.168]; also known as glycoamylase 1 plus glycoamylase 2, or heat-stable maltase 1 plus heat-stable maltase 2; and sucrose [EC 22.214.171.124; also called heat labile maltase and isomaltase [EC 126.96.36.199]; which are both contained with the sucrose-isomaltase complex.
Prior to the late 1990’s, it was believed that some sensitive individuals suffered from health problems from incomplete digestion of protein, not carbohydrates.
Analysis of the urine of autistic children showed increased levels of peptides, in particular the exorphins casomorphin and gluteomorphin, compared to normal individuals (Reichlet et al. J. Applied Nutr., 42:1-11 (1990). Casomorphins are released during the digestion of A1 casein by pepsin & elastase, while gluteomorphins are released during the digestion of gluten, a primary protein of wheat products.
These exorphins have been shown to have opiate-type effects on the body and have been implicated in a variety of human diseases including schizophrenia and attention deficit disorders. Opioids peptides can stimulate T cells, and induce peptide T cell responses and abnormal levels of cytokine production, which in turn can lead to inflammation, autoimmune reactions and disruption of neuroimmune communications.
It has been shown that eliminating gluten & A1 casein from the diet & supplementing with broad-spectrum proteolytic enzymes including PEP and DPPIV type protease and live kefir grains probiotic yoghurt with the ability to crowd out pathogenic bacteria & repopulate digestive enzymes greatly improves the digestion of proteins.
In 1999, Horvath et al. published findings of carbohydrate maldigestion in autistics (J. Pediatrics, 135:559-563, 1999). In a clinical study of 36 autistic children, 58% were found to have subnormal carbohydrate digestive enzyme activity. Horvath et al. determined that disaccharidase and/or glucoamylase were at fault.
In a subsequent study on 112 autistic patients, Horvath and Perman found that over half of the patients had symptoms consistent with maldigestion and again provided evidence of carbohydrate maldigestion (Horvath and Perman Curr Opin. In Pediatrics 14:583-587 (2002).
In particular, they identified deficiencies in lactase, maltase, sucrase, isomaltase (palatinase) and glucoamylase in 58% of the patients. Palatinase (also known as isomaltase) is of particular interest as it is expressed in the same crypts in the intestinal mucosa as dipeptidyl peptidase IV (DPPIV) [EC 188.8.131.52], which is responsible for digesting many exorphin peptides (Gorvel et al., Gastroenterology 101:618-625 (1991); Misumi and Ikahara, in Handbook of Proteolytic Enzymes, ed. Barrett, Rawlings and Woessner, Academic Press, p. 387-382 (1998)).
More recently, Kushak and Buie of Massachusetts, General Children’s Hospital reported on intestinal biopsy of over 100 autistic individuals, in which they found that 60-65% of the individuals, had weak lactase activity and 25% had weak isomaltase/palatinase activity, indicating that many autistic individuals are deficient in these enzymes.
Food grade isomaltase is not commercially available in large quantities and not readily available as a digestive aid. Transglucosidase can be used to compensate for a deficiency in the enzyme isomaltase and therefore used to treat disaccharidase deficiencies.
Transglucosidase [EC 184.108.40.206] is a food grade alpha-glucosidase that is used in in grain processing and brewing, and is known to have some isomaltase activity (McCleary et al. Carbohydrate Research 185:147-162 (1989). Transglucosidase is included in Zygest, the new 13 Food Enzyme System Formulation, including a Protease with DPPIV activity, 10 Carbohydrase, Phytase and Lipase.
Philippe Thebault ND. Fellow ANTA
‘ 0425 225 671