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PubMed2000

Lactose digestion capacity in Tokelauans: a case for the role of gene flow and genetic drift in establishing the lactose absorption allele in a Polynesian population.

Throughout the Pacific, lactose absorption occurs at rates of 0-46%. Most authors explain the current rate of lactose absorption in the Pacific in terms of gene flow with Europeans. However, researchers have not been able to determine the exact historical circumstances of the introduction of the lactose absorption gene. The availability of genealogical material, historical information, and mal/absorption frequencies for Tokelau (a Polynesian population) presents a unique opportunity to examine the role of gene flow in establishing lactose absorption in Pacific isolates. In an earlier study, Cheer and Allen ([1997] Am. J. Hum. Biol. 93:1-34) determined lactose digestion capacities for 58 Tokelauans. In the current study, we constructed pedigrees for the same 58 individuals, using the Tokelau Island Migrant Study genealogies (Wessen et al. [1992]). Results indicated that 8 of 13 lactose-absorbing individuals have European ancestors, compared with only 4 of 35 lactose malabsorbers (Chi(2) = 15.75, P < 0.01). Six lactose-absorbing individuals have either American or Portuguese ancestors dating back to the mid-1800s. Historical data were used to establish the contribution of Portuguese and American genetic material to the Tokelau population following massive depopulation after the Peruvian slave raids of 1863. This study provides clear evidence for the role of a population bottleneck followed by gene flow and genetic drift in establishing lactose absorption in the Tokelau population. Furthermore, it is the first study of a Pacific population to directly link lactose absorption with gene flow.

Absorption↗
PubMed1978

Estimation of the fraction of the lactose in a high lactose diet available for fermentation in the cecum and colon of the rat.

Experiments were conducted to determine the amount of lactose which passed into the large intestine and the lactase activity in the small intestine of rats (200 g) fed a control diet or a diet containing 30% lactose. The fraction of lactose consumed in a single 1-hour meal that escaped hydrolysis in the small intestine was estimated by measuring the area under a smooth curve of a plot of lactose:marker ratio in the terminal ileum expressed as a fraction of intake, against the fraction of the total marker that passed into the large intestine. This amounted to approximately 30% and 31.5% of the lactose consumed for the rats fed the control and 30% lactose diets, respectively. In another experiment in which the rats were fed a diet containing 30% lactose and the Cr-EDTA marker ad libitum for 1 week, approximately 43% of the lactose consumed became available for fermentation in the large intestine. This work suggests that a substantial fraction of the lactose ingested is available for fermentation in the large intestine. The lactase activity of homogenates of the small intestine of rats fed the control or high lactose diet was 106 +/- 5 or 115 +/- 4 mg lactose/30 minutes/rat (P less than 0.05), respectively. The lactase activity in the small intestine homogenate (mucosa + contents) was significantly higher than that actually available in vivo (110 +/- 7 versus 69 +/- 4 mg/30 minutes/rat).

Animals↗
PubMed1974

Characterization of lactose-fermenting revertants from lactose-negative Streptococcus lactis C2 mutants.

Partial lactose-fermenting revertants from lactose-negative (lac(-)) mutants of Streptococcus lactis C2 appeared on a lawn of lac(-) cells after 3 to 5 days of incubation at 25 C. The revertants grew slowly on lactose with a growth response similar to that for cryptic cells. In contrast to lac(+)S. lactis C2, the revertants were defective in the accumulation of [(14)C]thiomethyl-beta-d-galactoside, indicating that they were devoid of a transport system. Hydrolysis of o-nitrophenyl-beta-d-galactoside-6-phosphate by toluene-treated cells confirmed the presence of phospho-beta-d-galactosidase (P-beta-gal) in the revertant. However, this enzyme was induced only when the cells were grown in the presence of lactose; galactose was not an inducer. In lac(+)S. lactis C2, enzyme induction occurred in lactose- or galactose-grown cells. The revertants were defective in EII-lactose and FIII-lactose of the phosphoenolpyruvate-dependent phosphotransferase system. Galactokinase activity was detected in cell extracts of lac(+)S. lactis C2, but the activity was 9 to 13 times higher in extracts from the revertant and lac(-), respectively. This suggested that the lac(-) and the revertants use the Leloir pathway for galactose metabolism and that galactose-1-phosphate rather than galactose-6-phosphate was being formed. This may explain why lactose, but not galactose, induced P-beta-gal in the revertants. Because the revertant was unable to form galactose-6-phosphate, induction could not occur. This compound would be formed on hydrolysis of lactose phosphate. The data also indicate that galactose-6-phosphate may serve not only as an inducer of the lactose genes in S. lactis C2, but also as a repressor of the Leloir pathway for galactose metabolism.

Carbon Radioisotopes↗
PubMed1977

Individual sensitivity to lactose in lactose malabsorption.

The clinical significance of lactose malabsorption and the individual sensitivity to lactose were investigated in 20 patients with verified lactose malabsorption. Thirteen patients were relieved of all symptoms while seven improved only on a lactose-free dth lactose-free milk but following provocation with increasing amounts of lactose, the tendency to diarrhea and abdominal discomfort increased considerably. Three patients experienced discomfort after provocation with only 5 gl lactose. On provocation with increasing amounts of lactose the seven patients who had not recovered also developed increased abdominal discomfort but none of them developed increased tendency to diarrhea. It is concluded that, in addition to lactose malabsorption, these patients must suffer from ittitable colon with tendency to constipation.

Abdomen↗
PubMed1998

Fourier transform infrared analysis of purified lactose permease: a monodisperse lactose permease preparation is stably folded, alpha-helical, and highly accessible to deuterium exchange.

The lactose permease, encoded by the lacY gene of Escherichia coli, is an integral membrane protein that functions as a proton and lactose symporter. In this study, we have characterized a novel monodisperse, purified preparation of lactose permease, as well as functionally reconstituted lactose permease, using spectroscopic techniques. The purification of monodisperse lactose permease has been aided by the development of a lacY gene product containing an amino-terminal six histidine affinity tag. In the novel purification method described here, lactose permease is purified from beta-dodecyl maltoside-solubilized membrane vesicles using three sequential column steps: hydroxyapatite, nickel-nitriloacetic acid (Ni-NTA) affinity, and cation-exchange chromatography. The hydroxyapatite step was shown to be essential in reducing aggregation of the final purified protein. Amino acid composition analysis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis support the conclusion that the protein has been purified to greater than 90% homogeneity. The protein has been successfully reconstituted and has been shown to be active for lactose transport. Fourier transform infrared (FT-IR) spectroscopy has been performed on monodisperse lactose permease and on proteoliposomes containing functional lactose permease. FT-IR spectroscopy supports the conclusion that the monodisperse lactose permease preparation is 80% alpha-helical and stably folded at 20 degreesC; thermal denaturation is first detected at 70 degreesC. Because the purified protein is also readily susceptible to 2H exchange, these results suggest that the protein is conformationally flexible and that 2H exchange is facilitated as the result of conformational fluctuations from the folded state.

Amino Acid Sequence↗
PubMed1996

How much lactose is low lactose?

OBJECTIVE: To test the hypothesis that complete elimination of lactose is not necessary to ensure tolerance by lactose maldigesters. DESIGN: Double-blind, randomized protocol in which challenge doses of 0, 2, 6, 12, and 20 g lactose in water were fed to subjects after a 12-hour fast. SUBJECTS: 13 healthy, free-living adults who were lactose maldigesters. MAIN OUTCOME MEASURES: Breath hydrogen production (a measure of maldigestion) and symptom response to each challenge dose. STATISTICAL ANALYSIS: Analysis of variance was done to determine overall differences in mean hydrogen gas production (peak and sum of hours 1 through 8). Friedman's test was used to determine overall differences in the mean ranks for each symptom. Fisher's least significant difference test was used for multiple comparisons for hydrogen and symptom and data. RESULTS: Hydrogen production after consumption of the 0- and 2-g lactose doses was not significantly different. Hydrogen production increased with the 6-g dose. Intensity of abdominal pain increased when the dose of lactose was 12 g. Episodes of flatulence did not increase until the dose reached 20 g. No significant differences in the occurrence of diarrhea were observed after the five treatments. CONCLUSIONS: No significant increase in breath hydrogen production or intolerance symptoms occurred after consumption of a 2-g dose of lactose. Up to 6 g was tolerated, even though maldigestion could be measured at the 6-g dose. Thus, lactose maldigesters may be able to tolerate foods containing 6 g lactose or less per serving, such as hard cheeses and small servings (120 mL or less) of milk.

Abdominal Pain↗
PubMed1983

A new type of low-lactose milk. Tolerance by lactose malabsorbers and evaluation of protein nutritional value.

By ultrafiltration of skim milk a new low-lactose milk powder was developed whose lactose content was reduced by 86%. The lactose was replaced by malto-dextrin. In contrast to lactose-hydrolyzed milk powder, no protein-destroying processes (Maillard reactions) could be demonstrated during production or after storage at standard conditions. Tolerance of the new low-lactose milk versus regular skim milk was tested in 35 well-nourished, adult Latin Americans with lactose malabsorption. The ingestion of 500 ml of the low-lactose milk gave rise to significantly (p less than 0.05) fewer symptoms than regular skim milk. After the intake of 250 ml there a tendency to fewer symptoms after the low-lactose milk, although the difference was not significant (0.05 less than p less than 0.1). The new milk may be of potential usefulness in the treatment of protein calorie malnutrition in the developing countries, where lactose malabsorption is highly prevalent.

Animals↗
PubMed1979

Effect of O-sulphate groups in lactose and N-acetylneuraminyl-lactose on their enzymic hydrolysis.

1. Lactose 6'-O-sulphate, N-acetylneuraminyl-(alpha 2 leads to 3)-D-lactose 6'-O-sulphate, N-acetylneuraminyl ?-O-sulphate-(alpha 2 leads to 3)-D-lactose 6'0-O-sulphate, N-acetylneuraminyl ?-O-sulphate-(alpha 2 leads to 6)-D-lactose and N-acetylneuraminyl-(alpha 2 leads to 3)- and -(alpha 2 leads to 6))-lactose 6'-O-sulphate were prepared by chemical sulphation of lactose, N-acetylneuraminyl-lactose and tis isomers by using pyridine-SO3 reagent. 2. Significant kinetic differences were observed in the enzymic hydrolysis of the sulphated derivatives compared with unsubstituted substrates. 3. In the case of reactions catalysed by rat liver lysosomal and Clostridium perfringens neuraminidases (EC 3.2.1.18), the presence of an O-sulphate group in the N-acetylneuraminyl moiety affected the reaction by decreasing the Km and the Vmax, its presence in the galactosyl moiety affected the reaction by decreasing the Km and increasing the Vmax. and its presence in both N-acetylneuraminyl and galactosyl moieties decreased the Km and the Vmax. of the reaction. 4. Mixed-substrate reaction kinetic data indicated competition between the sulphated and unsubstituted substrates for the same active sites on the neuraminidase molecule. 5. Lactose 6'-O-sulphate neither behaved as a substrate nor acted as an inhibitor with respect to unsubstituted lactose and p-nitrophenyl beta-D-galactopyranoside when tested with lactase of suckling rat intestine and Escherichia coli beta-D-galactosidase (EC 3.2.1.23). 6. Preliminary investigation also indicated that, whereas glucose 6-O-sulphate and glucose 3-O-sulphate were were neither substrate nor inhibitor of glucose oxidase (EC 1.1.3.4), galactose 6-O-sulphate was oxidized half as fast as unsubstituted galactose by galactose dehydrogenase (EC 1.1.1.48).

Animals↗
PubMed1995

Kinetic analysis of lactose and proton coupling in Glu379 mutants of the lactose transport protein of Streptococcus thermophilus.

The role of Glu379 in the lactose-H+ symport protein (LacS) of Streptococcus thermophilus was studied by analyzing the kinetic mechanism of transport of wild-type and Ala379, Asp379, and Gln379 mutant proteins. Glu379 forms part of the sequence motif Lys-X-X-His-X-X-Glu that is present in a number of sugar transport proteins, including LacY of Escherichia coli. The E379A and E379Q mutants were defective in the uptake of lactose against a concentration gradient and lactose-dependent proton uptake, but catalyzed facilitated influx of lactose down a concentration gradient and equilibrium exchange with rates similar to that of the wild-type enzyme. The E379D mutant was partially defective in the coupled transport of lactose and protons. These results suggest that an acidic residue at position 379 is required for the coupled uptake of lactose and protons and are consistent with a mechanism in which lactose transport in the E379A and E379Q mutants occurs by uniport rather than proton symport. Lactose efflux down a concentration gradient in wild-type LacS and LacS-E379D increased with pH with apparent pK (pKa) values of > or = 8.5 and 8.0, respectively, whereas efflux in the E379Q mutant increased sigmoidally with a pKa of about 6.0. Imposition of an artificial membrane potential (inside negative) in membrane vesicles bearing wild-type LacS or LacS-E379Q not only inhibited the lactose efflux mediated by wild-type but also that of the mutant enzyme. To associate the role of Glu379 with specific step(s) in the translocation cycle of LacS, the properties of wild-type LacS and the Glu379 mutants have been evaluated by numerical analysis of simple kinetic schemes for translocation catalysis by solute H+ symport proteins. The properties of the wild-type enzyme are consistent with a mechanism in which the order of ligand binding on the inside is substrate first and proton last, whereas the order is random (or proton first, substrate last) at the outer surface of the membrane. The wild-type enzyme is asymmetric with regard to proton binding; the pK for proton binding on the outside is at least 4 units higher than the pK on the inside. The properties of the Glu379 mutants correspond with a lowering of the pK on the outside (pKOUT approximately pKIN), and the induction of a leak pathway in which the binary enzyme-substrate complex becomes mobile.

Amino Acid Sequence↗
PubMed1999

A K319N/E325Q double mutant of the lactose permease cotransports H+ with lactose. Implications for a proposed mechanism of H+/lactose symport.

In this study, we have examined the transport characteristics of the wild-type lactose permease, single mutants in which Lys-319 was changed to asparagine or alanine or Glu-325 was changed to glutamine or alanine, and the corresponding double mutant strains. The wild-type and Asn-319 mutant showed high levels of lactose uptake, with Km values of 0.42 and 1.30 mM and Vmax values of 102.6 and 48.3 nmol of lactose/min/mg of protein, respectively. The Asn-319/Gln-325 strain had a normal Km of 0.36 mM and a moderate Vmax of 18.5 nmol of lactose/min/mg of protein. By comparison, the single E325Q strain had a normal Km of 0.27 mM but a very defective Vmax of 1.3 nmol of lactose/min/mg of protein. A similar trend was observed among the alanine substitutions at these positions, although the Vmax values were lower for the Ala-319 mutations. When comparing the Vmax values between the single position 325 mutants with those of the double mutants, these results indicate that neutral 319 mutations substantially alleviate a defect in Vmax caused by neutral 325 mutations. With regard to H+/lactose coupling, the wild-type permease is normally coupled and can transport lactose against a gradient. The position 325 single mutants showed no evidence of H+ transport with lactose or thiodigalactoside (TDG) and were unable to facilitate uphill lactose transport. The single Asn-319 mutant and double Asn-319/Gln-325 mutant were able to transport H+ upon the addition of lactose or TDG. In addition, both of these strains catalyzed a sugar-dependent H+ leak that inhibited cell growth in the presence of TDG. These two strains were also defective in uphill transport, which may be related to their sugar-dependent leak pathway. Based on these and other results in the literature, a model is presented that describes how the interactions among several ionizable residues within the lactose permease act in a concerted manner to control H+/lactose coupling. In this model, Lys-319 and Glu-325 play a central role in governing the ability of the lactose permease to couple the transport of H+ and lactose.

Alanine↗
PubMed2002

Calcium and zinc absorption from lactose-containing and lactose-free infant formulas.

BACKGROUND: Calcium absorption is enhanced by the presence of lactose, but the quantitative significance of this effect in infant formulas is uncertain. It is also not known whether lactose affects zinc absorption. OBJECTIVE: We measured the absorption of calcium and zinc from infant formulas by using a multitracer, stable-isotope technique. DESIGN: Eighteen full-term infants (aged 8-12 wk at enrollment) were fed 2 partially hydrolyzed whey-protein-based formulas ad libitum for 2 wk per formula. The carbohydrate source was lactose in one formula and glucose polymers in the other (lactose-free). Infants were studied in a blinded crossover fashion after 2 wk of adaptation to each formula. Isotope absorption studies were conducted with a 4-tracer method in which (70)Zn and (44)Ca were provided orally and (67)Zn and (46)Ca intravenously. Zinc and calcium absorption was measured from the fractional excretion of the oral and intravenous isotopes in urine. RESULTS: Fractional and total calcium absorption was significantly greater from the lactose-containing formula than from the lactose-free formula. For total calcium absorption, the mean difference between formulas was 10.3% (P = 0.002) and 60 mg/d (P = 0.006). For zinc, fractional absorption (32 +/- 11%), total absorption, and intake did not differ significantly between the 2 formulas. CONCLUSIONS: The presence of lactose in a formula based on cow-milk protein increases absorption of calcium but not of zinc. Absorption of calcium from a lactose-free infant formula is, however, adequate to meet the calcium needs of full-term infants when the formula's calcium content is similar to that of lactose-containing, cow-milk-based infant formulas.

Administration, Oral↗
PubMed1999

Metabolism of lactose-[13C]ureide and lactose-[15N,15N]ureide in normal adults consuming a diet marginally adequate in protein.

Oral lactose-ureide is resistant to human digestive enzymes, but is fermented by the colonic microflora. Nine normal adults consuming a diet which provided 36 g of protein/day were given oral doses of lactose-[(13)C]ureide and lactose-[(15)N,(15)N]ureide. The appearance on breath of (13)CO(2) derived from lactose-[(13)C]ureide was followed for 48 h. The fate of (15)N derived from lactose-[(15)N, (15)N]ureide was determined by measuring the recovery of (15)N in stools and urine in various forms. About 80% of the label given as lactose-[(13)C]ureide was recovered on the breath, and about 80% of label given as lactose-[(15)N,(15)N]ureide was not recovered in stool, indicating that 80% of the dose was completely fermented. At least 5% of the labelled urea was absorbed and excreted as the intact molecule. Of the (15)N derived from lactose-[(15)N, (15)N]ureide and available for further metabolic interaction, 67% was retained and 33% was excreted in urine. The time taken for [(15)N,(15)N]urea to appear in urine was similar for all subjects, but the appearance of either (13)CO(2) on the breath or [(15)N, (14)N]urea in urine varied. It is concluded that the hydrolysis of the sugar-urea bond may reflect oro-caecal transit time, but that other factors related to colonic bacterial metabolism determine the duration and extent of hydrolysis of urea by urease enzymes. Lactose-ureide can be used to probe the metabolic activity of the colonic microflora in normal individuals.

Adult↗
PubMed1991

Colonization control of lactose-fermenting Salmonella typhimurium in young broiler chickens by use of dietary lactose.

Inclusion of lactose in the diets of chickens has been determined to reduce cecal colonization with Salmonella typhimurium. We hypothesized, therefore, that dietary lactose may be a practical means for reducing the prevalence of Salmonella contamination of chicken products. Because some strains of Salmonella are atypical and ferment lactose, we investigated the effects of dietary lactose on cecal colonization with lactose-fermenting S typhimurium. Broiler chicks were inoculated intracloacally with Lac+ S typhimurium selected for resistance to novobiocin and rifampicin. The chicks also were inoculated orally with certain anaerobes that do not effectively inhibit colonization by S typhimurium, but do appear essential for lactose mediated inhibition of cecal colonization. Control chicks were not given dietary lactose, and chicks in the experimental group were fed a diet containing 7% lactose. Enumeration of Lac+ S typhimurium in cecal contents revealed dietary lactose to be effective at controlling this organism. Control was correlated with changes in cecal pH and increases in undissociated volatile fatty acids, especially propionic acid.

Animals↗
PubMed1980

Gut transit time and lactose malabsorption during phototherapy. I. A study using lactose-free human mature milk.

Sixty newborn infants with normal birth weight suffering from uncomplicated hyperbilirubinemia were studied. They were fed human mature milk from which lactose had been eliminated, whereafter either sucrose ("sucrose milk") or lactose ("lactose milk") was added. 30 infants received ordinary phototherapy and 30 intensive phototherapy (blue double light). 15 in each group had "sucrose milk" and 15 "lactose milk". There was no significant difference between the increase in blood glucose (delta BS) by lactose tolerance tests performed before phototherapy (LTT1) and by those performed during phototherapy (LTT11), neither in infants treated with ordinary nor with intensive phototherapy. All infants had normal delta BS-LTT11, except one receiving ordinary phototherapy. There was no significant difference in gut transit time between infants having "sucrose milk" and infants having "lactose milk", neither in those treated with ordinary nor with intensive phototherapy. Gut transit time was significantly shorter in infants treated with intensive phototherapy than in infants treated with ordinary phototherapy without there being any significant difference in delta BS-LTT11. The infant with flat LTT11 may have developed lactose malabsorption during the phototherapy. Thus, lactose malabsorption is not the usual cause of the reduced gut transit time during phototherapy and must be a rare complication in phototherapy.

Bilirubin↗
PubMed1999

Ibuprofen augments gastrointestinal symptoms in lactose maldigesters during a lactose tolerance test.

BACKGROUND: Clinical symptoms during lactose tolerance test mimic those seen after therapeutic administration of prostaglandins, and resemble inflammatory processes. AIM: To investigate the possibility that lactose-induced gastrointestinal symptoms are associated with prostaglandins and/or nitric oxide. METHODS: After an overnight fast, nine maldigesters ingested lactose or sucrose with or without an inhibitor of prostaglandin synthesis (ibuprofen), in a randomised double-blind crossover trial. Gastrointestinal symptoms, concentrations of PGE2-M in blood and urine, and urinary 6-keto PGF1alpha (as indicators of prostaglandin synthesis), and urinary nitrate and nitrite as well as cyclic GMP excretions (as indicators of nitric oxide formation), were measured. RESULTS: Ibuprofen increased the first 3-h symptom scores (flatulence + borborygmi + abdominal bloating + pain) caused by lactose (P=0.008) but not sucrose. The concentrations of PGE2-M in the plasma and in the urine were unaffected. Lactose increased the urinary excretion of 6-keto PGF1alpha by about 30% (P=0.17), which was inhibited by ibuprofen (P=0.02). The production of nitric oxide was unaffected by lactose or ibuprofen. CONCLUSION: The inhibition of prostaglandin synthesis intensified gastrointestinal symptoms in lactose maldigesters, suggesting a negligible role for prostanoids in lactose-induced symptoms.

Adult↗
PubMed2003

Kefir improves lactose digestion and tolerance in adults with lactose maldigestion.

OBJECTIVE: Kefir is a fermented milk beverage that contains different cultures than yogurt. The objective of this study was to determine whether kefir improves lactose digestion and tolerance in adults with lactose maldigestion. DESIGN: Randomized block design. SUBJECTS: Fifteen healthy, free-living adults with lactose maldigestion. MAIN OUTCOME MEASURES: Breath hydrogen excretion and lactose intolerance symptoms were monitored hourly for 8 hours after each test meal. INTERVENTION: Subjects were fed test meals consisting of 20 g lactose portions of milk (2% reduced fat), plain and raspberry flavored kefir, and plain and raspberry flavored yogurt, each following an overnight (12 hour) fast. STATISTICAL ANALYSIS: Mixed model ANOVA was performed on raw or transformed data, followed by Tukey HSD post hoc tests (when appropriate). Significance was defined as P<.05. RESULTS: The breath hydrogen area under the curve (AUC) for milk (224+/-39 ppm x h) was significantly greater than for the plain yogurt (76+/-14 ppm x h, P<.001), the plain kefir (87+/-37 ppm x h, P<.001), and the flavored yogurt (76+/-14 ppm x h, P=.005). The flavored kefir had an intermediate response (156+/-26 ppm x h). The yogurts and kefirs all similarly reduced the perceived severity of flatulence by 54% to 71% relative to milk. Abdominal pain and diarrhea symptoms were negligible among the five treatments. APPLICATIONS/CONCLUSION: Because kefir improved lactose digestion and tolerance in this study, its use may be another potential strategy for overcoming lactose intolerance. Further studies of other types of kefir for improving lactose digestion are warranted.

Adult↗
PubMed1991

Lactose digestion from yogurt: influence of a meal and additional lactose.

Lactose in yogurt is better digested than lactose in other dairy foods by lactase-deficient individuals, in part because of intraintestinal activity of yogurt microbial beta-galactosidase (beta-gal). The survival and activity of yogurt beta-gal depend on gastrointestinal transit, pH, and viability of the yogurt culture. To evaluate the ability of yogurt beta-gal to digest lactose when yogurt is consumed with food or with additional lactose, 22 healthy lactose-maldigesting individuals were fed 10 test meals. Results of breath-hydrogen expiration, incidence of symptoms, and enzyme and lactose content of gastric aspirates indicate that the consumption of a meal with yogurt does not inhibit, and may slightly improve, lactose digestion from yogurt. However, yogurt beta-gal appears unable to assist in the digestion of additional lactose beyond that normally present in yogurt.

Adult↗