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Intestinal trehalase activity in a UK population: establishing a normal range and the effect of disease

Published online by Cambridge University Press:  09 March 2007

Iain A. Murray ,
Kathryn Coupland ,
Julie A. Smith ,
I. David Ansell  and
Richard G. Long
Iain A. Murray*
Affiliation:
Departments of Gastroenterology
Kathryn Coupland
Affiliation:
Departments of Gastroenterology
Julie A. Smith
Affiliation:
Departments of Gastroenterology
I. David Ansell
Affiliation:
Histopathology City Hospital, Nottingham NG5 1PB, UK
Richard G. Long
Affiliation:
Departments of Gastroenterology
*
*Corresponding author: Dr Iain A. Murray, fax +44 (0) 114 271 5531, email iainmurray10@hotmail.com
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Abstract

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Trehalose is a disaccharide, the main dietary source being mushrooms. It has been approved as an additive in the preparation of dried food. Isolated intestinal trehalase deficiency is found in 8 % of Greenlanders, but is rare elsewhere. The normal range of trehalase activity and the incidence of isolated trehalase deficiency in the UK have not been reported. Patients (n 400) were investigated for suspected malabsorption. Endoscopic distal duodenal biopsies were taken for histological assessment and maltase, sucrase, lactase and trehalase estimation. Disaccharidase activities were determined by Dahlqvist's technique (). Most patients (n 369) had normal duodenal histology. In these, square root transformation of trehalase activity produced a normal distribution. The normal range (mean ± 2 SD) was 4·79–37·12 U/g protein. One patient had an isolated borderline trehalase deficiency. The thirty-one patients with villous atrophy had significantly reduced disaccharidase activities. With ingestion of a gluten-free diet, maltase, sucrase and trehalase activities recovered to normal in most patients, whereas lactase activity did not. The normal range and very low incidence of isolated enzyme deficiency is comparable with that described in populations from the USA and mainland Europe. Activity is significantly reduced in untreated coeliac disease and recovers with treatment with a gluten-free diet. There is no place for routine determination of trehalase activity in the UK population and there should be no concern over the introduction of trehalose-containing dried foods.

Keywords

DisaccharidaseCoeliac disease
Type
Research Article
Information
British Journal of Nutrition , Volume 83 , Issue 3 , March 2000 , pp. 241 - 245
Copyright
Copyright © The Nutrition Society 2000

References

Asp, N-G, Berg, NO, Dahlqvist, A, Jussilla, J and Salmi, H (1971) The activity of three different small-intestinal β-galactosidases in adults with and without lactase deficiency. Scandinavian Journal of Gastroenterology 6, 755–762.CrossRefGoogle Scholar
Asp, N-G, Gudmand-Høyer, E, Anderson, B, Berg, NO and Dahlqvist, A (1975) Distribution of disaccharidases, alkaline phosphatase, and some intracellular enzymes along the human small intestine. Scandinavian Journal of Gastroenterology 10, 647–651.CrossRefGoogle ScholarPubMed
Berg, NO, Dahlqvist, A, Lindberg, T and Nordén Å (1973) Correlation between morphological alterations and enzyme activities in the mucosa of the small intestine. Scandinavian Journal of Gastroenterology 8, 703–712.CrossRefGoogle ScholarPubMed
Bergoz, R (1971) Trehalose malabsorption causing intolerance to mushrooms. Gastroenterology 60, 909–912.CrossRefGoogle ScholarPubMed
Bergoz, R, Griessen, M, Infante, F, de Peyer, R and Vallotton, M-C (1981) Significance of duodenal disaccharidases. Digestion 22, 108–112.CrossRefGoogle ScholarPubMed
Bodé, S and Gudmand-Høyer, E (1988) Incidence and clinical significance of lactose malabsorption in adult coeliac disease. Scandinavian Journal of Gastroenterology 23, 484–488.CrossRefGoogle ScholarPubMed
Dahlqvist, A (1968) Assay of intestinal disaccharidases. Analytical Biochemistry 22, 99–107.CrossRefGoogle ScholarPubMed
Dissanayake, AS, Jerrome, DW, Offord, RE, Truelove, SC and Whitehead, R (1974) Identifying toxic fractions of wheat gluten and their effect on the jejunal mucosa in coeliac disease. Gut 15, 931–946.CrossRefGoogle ScholarPubMed
Duncan, A, Park, RPR, Lee, FD and Russell, RI (1994) A retrospective analysis of the clinical value of jejunal disaccharidase analysis. Scandinavian Journal of Gastroenterology 29, 1111–1116.CrossRefGoogle ScholarPubMed
Ferguson, A MacDonald DM and Brydon, WG (1984) Prevalence of lactase deficiency in British adults. Gut 25, 163–167.CrossRefGoogle ScholarPubMed
Gudmand-Høyer, E, Fenger, HJ, Skovbjerg, H, Kern-Hasen, P and Rørbæk Madsen, P (1988) Trehalase deficiency in Greenland. Scandinavian Journal of Gastroenterology 23, 775–778.CrossRefGoogle ScholarPubMed
Gudmand-Høyer, E and Skovbjerg, H (1996) Disaccharidase digestion and maldigestion. Scandinavian Journal of Gastroenterology 31 (Suppl. 216), 111–121.CrossRefGoogle Scholar
Hertzler, SR and Savaiano, DA (1996) Colonic adaptation to daily lactose feeding in lactose maldigestors reduces lactose intolerance. American Journal of Clinical Nutrition 64, 232–236.CrossRefGoogle Scholar
Jönsson, K-A, Bodemar, G, Tagesson, C and Walan, A (1986) Variation of disaccharidase activities in duodenal biopsy specimens. Scandinavian Journal of Gastroenterology 21, 51–54.CrossRefGoogle ScholarPubMed
Langman, JM and Rowland, R (1990) Activity of duodenal disaccharidases in relation to normal and abnormal mucosal morphology. Journal of Clinical Pathology 43, 537–540.CrossRefGoogle ScholarPubMed
Lowry, OH, Rosebrough, NJ, Farr, AL and Randall, RJ (1951) Protein estimation with the folin–phenol reagent. Journal of Biological Chemistry 193, 262–275.CrossRefGoogle Scholar
McIntyre, AS, Smith, JA, Amoah, J, Ng, D and Long, RG (1994) The use of small endoscopic biopsies in the measurement of disaccharidase activities and the effect of duodenal ulceration. European Journal of Gastroenterology and Hepatology 6, 229–234.CrossRefGoogle Scholar
Madzarovová-Nohejlova, J (1973) Trehalase deficiency in a family. Gastroenterology 65, 130–133.CrossRefGoogle ScholarPubMed
Malis, F, Lojda, Z, Fric, P and Jodl, J (1972) Disaccharidases in celiac disease and mucoviscidosis. Digestion 5, 40–48.CrossRefGoogle ScholarPubMed
Roser, B (1991) Trehalose, a new approach to premium dried foods. Trends in Food Science Technology 2, 166–169.CrossRefGoogle Scholar
Roser, B (1991) Trehalose drying, a novel replacement for freeze-drying. BioPharm 4, 47–52.Google Scholar
Roser, B and Colaco, C (1993) A sweeter way to fresher food. New Scientist 138, 24–28.Google Scholar
Smith, JA, Mayberry, JF, Ansell, ID and Long, RG (1989) Small bowel biopsy for disaccharidase levels: evidence that endoscopic forceps biopsy can replace the Crosby capsule. Clinica Chimica Acta 183, 317–322.CrossRefGoogle ScholarPubMed
Welsh, JD, Poley, JR, Bhatia, M and Stevenson, DE (1978) Intestinal disaccharidase activities in relation to age, race and mucosal damage. Gastroenterology 75, 847–855.CrossRefGoogle ScholarPubMed