Sucrose Intolerance Research Articles

Sucrose intolerance in adults with common functional gastrointestinal symptoms

Sucrose intolerance is a form of carbohydrate malabsorption caused by sucrase-isomaltase deficiency that is more common than recognized. Its symptoms include postprandial cramping, bloating, gas, and diarrhea, which are difficult to distinguish from irritable bowel syndrome. The gold standard test for diagnosing sucrase deficiency is a sucrase enzyme assay of duodenal biopsies obtained by endoscopy. Hydrogen-methane or 13C-sucrose breath tests are noninvasive methods to screen for sucrose malabsorption. This chart review included 258 consecutive adults (47 men and 211 women) with chronic unexplained gastrointestinal symptoms and suspected sucrose intolerance who were screened with a hydrogen-methane or 13C-sucrose breath test. The incidence of sucrose malabsorption with two different hydrogen-methane breath tests was 34.4% (21/61) (Commonwealth Diagnostics International, Inc., Salem, MA) and 40% (20/50) (Aerodiagnostics, Concord, MA). The incidence of sucrose malabsorption with the 13C-sucrose breath test was 26.5% (39/147). In a subgroup of patients with positive breath tests and clinical follow-up, counseling regarding diet and/or enzyme replacement led to symptomatic improvement in 26/43 (60%). In conclusion, sucrose malabsorption may present with irritable bowel syndrome symptoms in a proportion of adult patients, and breath tests may be useful in identifying sucrose malabsorption and differentiating it from other gastrointestinal disorders.

S89 Is There More to Gas and Bloating, Abdominal Pain, and Diarrhea in Patients With Exocrine Pancreatic Insufficiency?

Introduction: Abdominal pain, diarrhea, and gas/bloating are among the most common gastrointestinal symptoms that bring patients to the clinic; comprising 21%, 25%, and 20% of presentations, respectively (1). Awareness of exocrine pancreatic insufficiency (EPI) has risen in recent years. Though some have underlying conditions such as cystic fibrosis, pancreatic surgeries, diabetes, chronic pancreatitis, and pancreatic cancer, most are idiopathic. In this study we reviewed 219 patients presenting with the aforementioned symptoms who were diagnosed with EPI without a predisposing condition. Previous reviews have discussed routine etiologies of gas/bloat syndrome with pain and perturbation of defecation (2,3). In this paper we describe the prevalence of comorbid disorders that contribute to this symptom complex. Methods: We identified 219 patients (147 female, 72 male) with idiopathic EPI in the outpatient clinic with any combination of gas/bloat, pain, and diarrhea. Ages ranged from 18-90 years (median 64). We obtained standard chemistries, CBC, thyroid profile, celiac panel, stool elastase, lactoferrin, and hydrogen breath testing for carbohydrate malabsorption and SIBO. If an elevated lactoferrin, suspicious celiac panel, or persistent diarrhea were observed, endoscopic examinations were performed. Patients were also evaluated for IBS using Rome IV criteria. Results: Of the 219 patients, we noted diagnoses that are associated with similar symptoms: 43 (19.6%) had SIBO, 43 (19.6 %) fructose intolerance, 28 (12.8%) lactose intolerance, 8 (3.7 %) with celiac, and 4 (1.8%) with sucrose intolerance. Notably, 14 (6.4 %) were diagnosed with microscopic colitis and 29 (13.2%) with IBS. Further analysis revealed that 24.7% had 2 conditions, 11% with 3, 6.8% with 4, and 2.3% with 5. Conclusion: EPI is a common and easily treated problem seen in clinic, but often is not a comprehensive diagnosis. A constellation of symptoms including gas/bloat, pain, and diarrhea are often indicative of a more complex and multifactorial phenomenon that requires meticulous evaluation.

Rare Hypomorphic Sucrase Isomaltase Variants in Relation to Irritable Bowel Syndrome Risk in UK Biobank

Rare Hypomorphic Sucrase Isomaltase Variants in Relation to Irritable Bowel Syndrome Risk in UK Biobank

Sucrose Intolerance Tests in the Neonates

Sucrose maldigestion is difficult to diagnose especially in newborn babies.
 Stool chromatography is the most useful tool to detect the type of saccharide maldigestion.
 Using the clinical symptoms as parameter, there were 3 out of 28 mabies suffering from sucrose maldigestion, in whom the blood glucose Level did not increase more than 40 mg % after the injection of sucrose.
 

ChREBP-Knockout Mice Show Sucrose Intolerance and Fructose Malabsorption.

We have previously reported that 60% sucrose diet-fed ChREBP knockout mice (KO) showed body weight loss resulting in lethality. We aimed to elucidate whether sucrose and fructose metabolism are impaired in KO. Wild-type mice (WT) and KO were fed a diet containing 30% sucrose with/without 0.08% miglitol, an α-glucosidase inhibitor, and these effects on phenotypes were tested. Furthermore, we compared metabolic changes of oral and peritoneal fructose injection. A thirty percent sucrose diet feeding did not affect phenotypes in KO. However, miglitol induced lethality in 30% sucrose-fed KO. Thirty percent sucrose plus miglitol diet-fed KO showed increased cecal contents, increased fecal lactate contents, increased growth of lactobacillales and Bifidobacterium and decreased growth of clostridium cluster XIVa. ChREBP gene deletion suppressed the mRNA levels of sucrose and fructose related genes. Next, oral fructose injection did not affect plasma glucose levels and liver fructose contents; however, intestinal sucrose and fructose related mRNA levels were increased only in WT. In contrast, peritoneal fructose injection increased plasma glucose levels in both mice; however, the hepatic fructose content in KO was much higher owing to decreased hepatic Khk mRNA expression. Taken together, KO showed sucrose intolerance and fructose malabsorption owing to decreased gene expression.

Signal peptide-dependent protein translocation pathway is crucial for the sucrose sensitivity of SacB-expressing Escherichia coli

Escherichia coli expressing the levansucrase SacB gene cannot grow on LB plates containing 5% sucrose, therefore this gene has been used as a counter-selection marker in many studies. However, the mechanism of this phenomenon is still unclear. In this study, we compared the characteristics of E. coli strains expressing SacB with and without signal peptide. We observe that only SacB with signal peptide causes sucrose intolerance of E. coli. In addition, kinetic studies and product analyses indicated that the signal peptide exerts no obvious effect on the enzymatic properties of SacB. Therefore, the signal peptide-dependent protein translocation pathway is clearly crucial for the sucrose intolerance of SacB-expressing E. coli. Additionally, E. coli containing SacB minus signal peptide forms swollen colonies on sucrose-containing LB plates which may provide a convenient and high-throughput screening method for directed evolution of levansucrases.

Actionable Nutrigenetics for Genetically Based Diseases? A New Critical Path to P4 Medicine

Nutrigenomics and nutrigenetics are receiving growing attention from a diverse range of stakeholders including health care professionals, citizens, governments, insurers and industry. Currently there is special focus on research on how our food influences us and might cause discomfort or even symptoms of disease, but also the fact that several food intolerances are caused by genetic alterations. The strong interest expressed by certain segments of the general population for predictive and preventive diagnostic testing in relation to diet and ways in which this can improve overall health led to a fast growing market of nutrigenetic based tests. This puts pressures and challenges on governments and insurers for how best to reimburse new genetic tests. These discussions are best informed by a sound understanding of nutrigenetics science and technology, its promises and challenges, which are addressed in this paper. For example, some of the most common food intolerances caused by genetic variations are lactose intolerance, inherited fructose intolerance, congenital sucrase isomaltase deficiency (sucrose intolerance), celiac disease, glucose-6-phosphate deficiency (favism), alcohol intolerance and hemochromatosis. The increasing understanding of molecular mechanisms associated with these conditions is stimulating the development of a broad range of diagnostics allowing any person with adequate resources to have their genetic predispositions determined. However, many of the currently available tests cover only one of the above mentioned diseases or a small set of responsible mutations, which is in strong contrast to the evolution of medicine towards a more holistic approach as, for example, P4 medicine. Additionally, available tests are often not based on evidence or other guidelines for genetic test development as recommended by the ACCE evidentiary framework. In this paper we discuss the most common nutrigenetic diseases and their potential and demonstrated impacts on public health, as well as ways to devise personalized diet informed by human genomics variation in the future.

Congenital Sucrase‐Isomaltase Deficiency

Congenital Sucrase‐Isomaltase Deficiency

SUCROSE INTOLERANCE: AN ENZYMATIC DEFECT.

Journal Article Sucrose Intolerance: an Enzymatic Defect Get access Nutrition Reviews, Volume 23, Issue 4, April 1965, Pages 101–102, https://doi.org/10.1111/j.1753-4887.1965.tb02095.x Published: 01 April 1965

Hansenula polymorpha maltase gene promoter with sigma 70-like elements is feasible for Escherichia coli-based biotechnological applications: Expression of three genomic levansucrase genes of Pseudomonas syringae pv. tomato

P MAL1, the sigma 70-like sequences possessing promoter of the maltase gene of Hansenula polymorpha, was evaluated for its application in heterologous protein production in Escherichia coli. Levansucrases Lsc1, Lsc2 and Lsc3 of Pseudomonas syringae pv. tomato DC3000 were expressed from P MAL1 in E. coli as biotechnologically relevant model proteins. Production of soluble levansucrases with high specific activity confirmed appropriate strength of P MAL1 in a prokaryotic host. As about 90% of levansucrase activity was present in the cytoplasm of E. coli, no levan-synthesis related sucrose intolerance of bacteria was observed. All three levansucrases hydrolyzed and polymerized both, sucrose and raffinose. The raffinose-related activity of levansucrases has not been previously described in P. syringae. The P MAL1 expression system was used to produce Lsc3 protein in E. coli for purification. The purified levansucrase showed much higher affinity for sucrose cleavage ( K m = 21 mM) than the levansucrase from P. syringae pv. phaseolicola described in the literature with K m of 160 mM.

EVALUATION OF SMALL INTESTINE FUNCTION IN INFANTS WITH PERSISTENT DIARRHEA (PD) USING MONOCLONAL ANTIBODIES (MAbs)

MAbs against enzymes of the brush border provide a new approach to evaluate intestinal lesions in severe PD. The 10 patients with PD in whom a small bowel biopsy was performed during 1992 were evaluated by means of MAbs for lactese (L), sucrase (S), maltsse (M) and aminopeptidase (A); results were compared with those of light mi croscopy, histochemistry lor lactase, disacchandase activities (Dalqvist) and clinical history. Diagnosis was DP and severe malnutrition (MN) in 4 cases, congenital sucrose intolerance (CSI) 1, cow's milk protein intolerance (CMI) 2, celiac disease (CD) 1, sIgA deficiency 1 and cryptosporidias is (Crypt) 1. The latter was the only child with a positive ethiologic study. MAP ofr sucrase detected more enzyme than Dalqvist, which may be interpreted as tht MAP binds non-functional molecules. In patient with CSI, MAP for sucase detedted less enzyme than Dalqvist, which is in agreement with the production of a defective molecule.

Sucrose Intolerance in Birds: Simple Nonlethal Diagnostic Methods and Consequences for Assimilation of Complex Carbohydrates

Gray Catbirds (Dumetella carolinenisis, Mimidae) and Purple-headed Glossy-Star- lings (Lamprotornis purpureiceps, Sturnidae) showed depressed ingestion and increased fecal sugar contents when shifted from glucose and fructose to sucrose solutions. These species also exhibited no increases in plasma glucose after ingestion of sucrose, but an increase in plasma glucose after ingestion of equicaloric doses of a mixture of glucose and fructose. In vitro measurements of intestinal disaccharidase activities in D. carolinensis revealed insignif- icant sucrase activity, and low levels of maltase activities. These results support the hypothesis that sucrose intolerance is a shared-derived character of the monophyletic lineage that in- cludes starlings, mimids, and thrushes, and indicate that sucrose intolerance in birds can be easily diagnosed with a combination of behavioral and nonlethal physiological measure- ments. We suggest that, in birds, low intestinal maltase activity is correlated with the lack of sucrase activity. We further hypothesize that sucrose-intolerant birds are poor at assimi- lating complex carbohydrates. Received 1 March 1993, accepted 17 November 1993.

A study of the molecular pathology of sucrase-isomaltase deficiency. A defect in the intracellular processing of the enzyme.

The intestinal brush-border enzyme sucrase-isomaltase splits sucrose into its component monosaccharides, glucose and fructose. A deficiency of the enzyme leads to sucrose intolerance. We studied the synthesis and intracellular processing of sucrase-isomaltase, using human intestinal explants in organ culture. Pulse-chase experiments with [35S]methionine followed by immunoprecipitation, sodium dodecyl sulfate-polyacrylamide-gel electrophoresis, and fluorography of labeled sucrase-isomaltase demonstrated that the molecule was initially recognized as a protein with a relative molecular weight (Mr) of 205,000. This was apparently converted to a species of 225,000 Mr within two hours. We studied the glycosylation of the protein using endo-beta-N-acetylglucosaminidase H and peptide-N4-(N-acetyl-beta-glucosaminyl)-asparagine amidase digestion of oligosaccharide side chains of the two forms of sucrase-isomaltase. The results showed that the early-appearing 205-kd (kilodalton) molecule contained high-mannose asparagine-linked oligosaccharides, and that the later-appearing, 225-kd molecule contained highly processed (mature) carbohydrate chains. Studies in a patient with primary sucrase-isomaltase deficiency demonstrated normal translation and high-mannose glycosylation of the precursor but a failure in further processing of the oligosaccharides, with subsequent intracellular degradation of the glycoprotein and undetectable enzymatic activity of intestinal sucrase. Abnormal intracellular processing of the enzyme was the probable mechanism of enzyme deficiency in this patient.

Tolerance to glucose polymers in malnourished infants with diarrhea and disaccharide intolerance

The response of infants with diarrhea and lactose intolerance to feedings containing soy protein and sucrose (Sobee), and/or to a carbohydrate free formula (RCF), to which glucose polymers (GP) were added, was assessed in twenty patients. They all were less than ten months of age and had varying degrees of malnutrition. Eleven had acute diarrhea and nine had chronic diarrhea. None of them had classical enteropathogenic strains and parasites in the stools. All had lactose intolerance when feedings were begun with cow's milk formula and some also had sucrose intolerance when fed sucrose containing soy formulas. They had persistent loose stools and excreted feces with an acid pH and with carbohydrates, thus they were given dietary treatment with RCF with GP. There were 9 patients with acute diarrhea and lactose intolerance (1 of them also had sucrose intolerance), who improved on RCF with GP feedings; but 2 patients (lactose and sucrose intolerant) failed to respond to this diet. There were six patients with chronic diarrhea and lactose intolerance (four of them also had sucrose intolerance), who improved on RCF with GP formula, but there were three patients who failed on this treatment. These data show that some infants with diarrhea, malnutrition, and lactose-sucrose intolerance may also develop intolerance to GP and require further dietary management with glucose as the source of carbohydrate in the diet.

Immunoelectrophoretic studies on human small intestinal brush border proteins. The residual isomaltase in sucrose intolerant patients.

Small intestinal biopsies from three patients with sucrose intolerance (sucrase-isomaltase deficiency) were studied by means of immunoelectrophoresis and enzymatic assays. All patients lacked sucrase activity (less than 1 unit/g protein). One of the patients had a substantial isomaltase activity (7.8 unit/g protein). Immunoelectrophoresis revealed the presence of the isomaltase polypeptide of the sucrase-isomaltase in this patient. None of the biopsies showed any precipitate that might represent a modified inactive sucrase protein.

Recurrent Abdominal Pain in Children: Lactose and Sucrose Intolerance, A Prospective Study

Thirty-eight consecutive children with recurrent abdominal pain underwent lactose tolerance tests; 28 of these were also given sucrose tolerance tests. Abdominal pain and abnormal lactose tolerance tests were noted in 11 of 38, while none of the 28 had an abnormal sucrose tolerance test; however, 1 had abdominal pain. Elimination diet for 4 weeks produced significant or total pain relief in 10 of 11 (lactose free) and 0 of 1 children (sucrose free). Lactose intolerance seems to play a contributory role in recurrent abdominal pain in children, while sucrose intolerance does not.

NONINVASIVE DIAGNOSIS OF SUCROSE INTOLERANCE IN CHILDHOOD BY INTERVAL BREATH HYDROGEN DETERMINATION

Elevated breath hydrogen levels resulting from colonic bacterial fermentation of nonabsorbed carbohydrate identifies disaccharidase deficiency in adults. This principle was validated in children with sucrose intolerance by interval breath sampling using a nasal prong, thus permitting simple, noninvasive collection of expired air for H2 analysis by gas chromatography. Six symptomatic children (ages 6-11 yrs) with congenital sucrose intolerance (4 proven sucrase deficient by jejunal biopsy and 2 sibs) were compared with 6 normal controls (ages 5-8 yrs) and 2 children with biopsy-proven acquired sucrase deficiency now clinically well (ages 3 and 10). Expired air was collected before and at 30, 60, 90, 120 and 180 min after orally administered sucrose (2 gmAg; max 50 gm). Peak H2 excretion was significantly elevated in sucrose intolerant patients: 114±63 (meant S.D.) parts per million above baseline (Δppm), versus 2±2 Δppm (p<0.001) in controls and patients who had recovered. Best discrimination occurred at 90 minutes post-ingestion (range 28-203 vs. 0-3 Δppm). Breath H2 determination provides a sensitive, reliable means for detection of sucrose malabsorption. The nasal prong technique permits convenient application of this methodology to young children, and offers the opportunity to screen, diagnose, and evaluate therapy for malabsorption of specific carbohydrates in the pediatric age group.

Congenital maltase-sucrase and maltase-isomaltase deficiency in an adult.

The observation of a woman, aged 21 years, having congenital sucrose intolerance is reported. The tests used for diagnosis are recalled as well as the mechanism of diarrhea due to disaccharidase defic

The sedimentation properties of the intestinal alpha-glucosidases of normal human subjects and of patients with sucrose intolerance.

The maltase‐isomaltase, maltase‐sucrase and glucoamylase of the human intestinal mucosa have been solubilized by Triton X‐100 and submitted to centrifugation in a mannitol gradient. Under these conditions, the three enzymes sediment together in a 10 S fraction; with one normal mucosa out of 10 which were investigated a supplementary 13 S peak of both glucoamylase and maltase‐isomaltase was observed.Several experimental conditions, like treatment of the extracts at 45° or solubilization of the α‐glucosidases by papain in the absence of potassium ions, induced an important inactivation of the maltase‐isomaltase and deep alterations in the sedimentation profile of the 3 glucosidases: the glucoamylase and the residual maltase‐isomaltase were distributed in 3 fractions with 13 S, 10 S and 6–7 S sedimentation coefficient, whereas the maltase‐sucrase was mostly present as a 7 S structure. In sucrose intolerance, the maltase‐sucrase is absent and the activities of the maltase‐isomaltase and glucoamylase are significantly reduced. The residual enzymes were ‐recovered as 13 S and 6 S structures instead of the normal 10 S species.These observations allow the conclusion that the three α‐glucosidases are naturally linked to each other in the normal mucosa and that the alteration of one of them induces a structural rearrangement of the 3 enzymes. The absence of maltase‐sucrase in patients with congenital intolerance to sucrose can be regarded as the result of a single mutation of the corresponding structural gene and as the cause of a reorganization of the two other α‐glucosidases; this reorganization can explain a partial loss of the enzymatic activity.

Letters to the Editor

I regret that my comments on dietary management of sucrose intolerance may have lacked sufficient detail. Apart from sucrose itself all cakes, candy, soft drinks, chocolate, ice-cream, fruit preserves, jellies, syrups, and sweetened condensed milks are likely to contain large amounts of sucrose and should be avoided or restricted. Enquiries should be made of the manufacturer where doubt exists about the sucrose content of commercial products. Common fruits and vegetables which contain significant amounts of sucrose include sugar beets, sweet potatoes, bananas, dates, and pineapples.