Lingual Lipase Activity Research Articles

Exploring the Impact of α-Amylase Enzyme Activity and pH on Flavor Perception of Alcoholic Drinks.

The introduction of a drink in the mouth and the action of saliva and enzymes cause the perception of basic tastes and some aromas perceived in a retro-nasal way. Thus, this study aimed to evaluate the influence of the type of alcoholic beverage (beer, wine, and brandy) on lingual lipase and α-amylase activity and in-mouth pH. It was possible to see that the pH values (drink and saliva) differed significantly from the pH values of the initial drinks. Moreover, the α-amylase activity was significantly higher when the panel members tasted a colorless brandy, namely Grappa. Red wine and wood-aged brandy also induced greater α-amylase activity than white wine and blonde beer. Additionally, tawny port wine induced greater α-amylase activity than red wine. The flavor characteristics of red wines due to skin maceration and the contact of the brandy with the wood can cause a synergistic effect between beverages considered "tastier" and the activity of human α-amylase. We can conclude that saliva-beverage chemical interactions may depend on the saliva composition but also on the chemical composition of the beverage, namely its constitution in acids, alcohol concentration, and tannin content. This work is an important contribution to the e-flavor project, the development of a sensor system capable of mimicking the human perception of flavor. Furthermore, a better understanding of saliva-drink interactions allow us to comprehend which and how salivary parameters can contribute to taste and flavor perception.

Impact of food odors signaling specific taste qualities and macronutrient content on saliva secretion and composition

Olfactory food cues can induce appetite for similar food products in humans. Odors may thus signal essential information about a foods’ composition such as taste or even macronutrient content and may stimulate specific physiological responses in anticipation of food intake. Several studies have shown that sensory food cues could stimulate saliva secretion. However, potential differences between food odors in their effect on saliva secretion, or the effects of olfactory stimulation on changes in saliva composition remain to be elucidated. To gain more insight, we conducted two studies to determine the influence of various odors, representing different taste qualities (study 1) and macronutrients (study 2), on salivary biomarkers. In study 1, 36 participants were randomly exposed to no-odor, non-food, and odors signaling sweet, savory, and sour taste. In study 2, 60 participants were randomly exposed to no-odor, non-food, and odors signaling carbohydrates, protein, fat, and low-calorie food. For each condition, whole-mouth saliva was collected and saliva secretion rate determined. Furthermore, we determined mouth-watering perception (subjective salivation), visco-elasticity (study 1 only), mucin concentration, α-amylase and lingual lipase activity (study 2 only). For both studies, linear mixed model analyses showed that saliva secretion rate significantly increased by food odor exposure compared to no-odor and non-food conditions. However, no changes in salivary composition were observed. These findings indicate that food odors play a crucial role in anticipatory saliva responses and can thereby affect subsequent eating behavior.

Lingual lipase activity in the orosensory detection of fat by humans

Lingual lipase generates nonesterified fatty acids (NEFA) from dietary fats during oral processing by lipolysis. Lingual lipase in rodents has strong lipolytic activity and plays a critical role in oral detection of fats. The functional activity of lingual lipase during oral processing of high-fat foods in humans remains poorly characterized. Five commonly consumed high-fat foods varying in physical states and fatty acid composition (almond, almond butter, olive oil, walnut, and coconut) were masticated by 15 healthy human subjects at the rate of one chew per second with and without lipase inhibitor orlistat. Salivary NEFA concentrations were measured. To determine the role of lingual lipase in oral fat detection, sensory ratings were obtained from the same 15 human subjects for almond butter with and without orlistat. Lingual lipase was active during oral processing of almond and coconut. No activity of lingual lipase was detected during processing of almond butter. There was only weak evidence lingual lipase is a determinant of oral fat detection. Lingual lipase may only contribute to NEFA generation and oral fat detection of fatty foods that require stronger oral processing effort.

Effect of 24 hours light on circadian rhythms of secretory enzymes and morphology of rat von Ebner’s glands

Von Ebner’s glands of the rat are minor salivary serous glands in the posterior portion of the tongue. They secrete two digestive enzymes, lingual lipase and amylase. In this investigation, circadian rhythm in feeding was established under a normal 12 h light/12 h dark cycle, with the rats eating primarily during the dark period. At lights on, the size of the acinar cells and the area of the inclusive secretory granules, and the amount of digestive enzyme activity (lingual lipase and amylase) remaining in the gland was significantly less than in the mid-afternoon, after very little daylight food consumption. However, after 7 days of continuous light the circadian rhythm was altered: the food consumption during the normal night-time hours (5 p.m. to 8 a.m.) went from 88% of total 24 h food consumption to 45%, and during normal daylight hours (8 a.m. to 5 p.m.) from 12% to 55%. These changes were correlated with histometric findings of a near reversal of the areas of acinar cells and secretory granules of a.m. and p.m. samples under continuous light. Lingual lipase activity in the glands went from 35% under 12 h light to 61% under continuous light in the a.m. and from 65% to 39% in the p.m. Amylase activity also showed nearly a reversal in activity remaining in the gland, from 36% at 12 h light to 58% at 24 h light in the a.m. and 64% to 41% for the p.m. samples. These results indicate that the von Ebner’s glands of the rat have a circadian rhythm of secretion and storage of secretory proteins that is subject to light entrainment similar to that seen in other exocrine glands such as the parotid and pancreas.

Protein Analysis of Human von Ebner Saliva and a Method for its Collection from the Foliate Papillae

The lingual serous glands of von Ebner are located close to the foliate and circumvallate papillae. Saliva secreted by these glands provides the immediate environment of the taste buds, and it has been hypothesized that it modulates taste perception. The purpose of this study was to develop a technique for collection of unstimulated and stimulated saliva from human von Ebner glands. Saliva was collected under resting conditions and after application of various gustatory stimuli (sweet, sour, salt, and bitter) by insertion of periostrips into the folds of the foliate papillae of healthy human volunteers. Stimulated saliva was also collected in glass microcapillaries or micropipettes. The flow-rates of unstimulated von Ebner saliva were 2.3 +/- 0.6 (S.E.) microL/min and 4.5 +/- 1.2 (S.E.) microL/min with 1% citric acid stimulation. The protein content was 2.5 +/- 0.5 (S.E.) mg/mL. The SDS gel electrophoretic profile of von Ebner saliva revealed two protein bands of Mr 18,000 that were identified on Western blots as von Ebner gland (VEG) proteins. Although lingual lipase activity was detected at very low levels by enzyme assay, this protein was not detected on Western blots. This collection technique should prove useful for analysis of specific functions associated with secretion from von Ebner glands.

The effects of histamine, pyrilamine, cimetidine, and ranitidine on secretion of lingual lipase and amylase from rat von Ebner's glands.

Minced von Ebner's glands of rat tongue were incubatedin vitro with histamine and histamine receptor antagonists. At various time intervals, media and homogenates of the tissue were assayed for lingual lipase and amylase activity and percentage secretion calculated. Histamine elicited moderate secretion (≈10%) of lingual lipase and amylase. In contrast, pyrilamine, and H1 receptor antagonist, elicited>60% secretion. There were statistically significant differences between the percentage secretion of lingual lipase and amylase for basal secretion, as well as for histmine-and pyrilamine-evoked secretion of lingual lipase and amylase for basal secretion, as well as for histamine-and pyrilamine-evoked secretion above basal. The H2 receptor inhibitors, cimetidine and ranitidine, stimulated secretion of only amylase, but not lingual lipase. When combined with histamine, these antagonists partially inhibited only the secretion of histamine-evoked lingual lipase, but not amylase. The differences in percentage secretion between the two enzymes indicate that exocytosis may not be the only process involved in protein secretion. The anomalous effects of the H1 and H2 receptor antagonists necessitate a more detailed characterization of the receptors of von Ebner's glands.

Developmental Delay of Lingual Lipase Expression after Guanethidine-Induced Sympathectomy

Rat lingual lipase increases during postnatal development. To evaluate the role of the sympathetic nervous system in the control of lingual lipase during development, suckling rats were chemically sympathectomized by chronic treatment with guanethidine. This treatment was found to be effective in suppressing the developmental increase of lingual lipase. The effect was age dependent and also related to the dose of guanethidine given (i.e., the higher the dose, the more effective the suppression is, up to 40 micrograms/g body wt). The effect of guanethidine on lingual lipase suppression was not a result of induced stress, since simultaneous treatment with RU-38486, a known glucocorticoid receptor antagonist, did not prevent the decrease in lingual lipase activity. Ephedrine, a known sympathomimetic agent, restored the lingual lipase to a near normal level in guanethidine-treated animals, confirming that guanethidine acts through the sympathetic nerves. Furthermore, histochemical studies showed that guanethidine-treatment resulted in the reduction or elimination of catecholaminergic fibers in the von Ebner's glands. The effect of guanethidine was found to be transient, in that the lingual lipase activity showed complete recovery upon withdrawal of the treatment for 1 week. Together, the results indicated that sympathetic nerves have an important regulatory role in lingual lipase in rat pups during development.

Lipase and Pepsin Activities in the Stomach Mucosa of the Suckling Dog

The origin of preduodenal lipases was investigated in the suckling dog. In this species, gastric lipase is the main (or only) preduodenal lipase (activity range 1.03-8.32 U/mg protein), lingual-lipase activity being absent or amounting to traces only (0.77-2.3 mU/mg tissue). The localization of lipase activity in the stomach was mapped and compared to that of pepsin. The data show that the highest lipase activity was found in biopsy specimens of gastric mucosa from the cardia area (5.32 +/- 1.29-8.32 +/- 0.93 U/mg protein), and the lowest in the antrum (1.03 +/- 0.16-1.94 +/- 0.43 U/mg protein). Activity was also significantly higher in the mucosa along the greater rather than the lesser curvature of the stomach. Pepsin activity was highest in the cardia and gastric body areas (26.2 +/- 0.89-89 +/- 23.61 and 26.83 +/- 15.98-69.51 +/- 9.82, respectively). Contrary to lipase activity, considerable pepsin activity was present in the antrum (18.17 +/- 4.12-23.07 +/- 5.60 U/mg protein). No difference in pepsin activities was found in the greater as compared to the lesser curvature. The data show similar origin and tissue distribution of gastric digestive enzymes in the suckling dog and human infant. The role of the newborn dog as an animal model for fat digestion in the human infant is discussed.

Adaptation of Lingual Lipase to Dietary Fat in Rats

To study the adaptive response of lingual lipase and pancreatic lipase to dietary fat, three sets of experiments were performed in adult male rats. In the first experiment, rats were fed for 3 wk a low fat diet (4.5% fat) or a 10, 20 or 30% fat diet. In the second, rats were fed a 4.5% fat diet for 4 wk or a 20% fat diet for 1, 2 or 4 wk. In the third, rats were fed for 3 wk a 10% fat diet with various sources of fat (lard, sunflower oil, olive oil, peanut oil, butter, soybean oil, corn oil or salmon oil). The results demonstrated that 10% dietary fat was sufficient to promote a maximum significant increase in lingual lipase activity (expressed in units/g tissue and in units/mg protein), whereas pancreatic lipase responded steadily to 20 and 30% fat diets. After 1 wk of feeding 20% dietary fat, both enzyme specific activities had reached their maximum values. The fatty acid composition of dietary triglyceride molecules (chain length, number and location of double bonds) had no specific effect on the adaptation of lingual lipase. The physiological implications of these findings are discussed in regard to the role of intragastric lipolysis in fat digestion.

Gastric Lipase: Localization in the Human Stomach

The aim of this study was to determine the range of activity and the location of lipase in the human stomach. The range of lipase activity in gastric mucosa of surgical specimens from the fundic area of 22 subjects was 594 to 3350 mU [mean, 1598 +/- 144 mU tri[3H]olein, (1 mU-1 nmol [3H]oleic acid released from tri[3H]olein per minute per milligram protein)]. For localization of activity, pinch biopsy specimens of gastric mucosa from 6 subjects were taken from the greater and lesser curvatures within 2 cm of the gastroesophageal junction (upper greater curvature and upper lesser curvature) and within 2 cm of the pylorus (lower greater curvature and lower lesser curvature). Lipase activity was higher in the upper greater curvature (405 +/- 92 mU) than in the upper lesser curvature (32 +/- 13 mU) and lowest in the antral area (16 +/- 9 mU in the lower lesser curvature and 10 +/- 2 mU in the lower greater curvature). The data show that in the human, lipase activity is localized primarily in the fundic area of the stomach. Comparison of the lipase activity levels in the gastric mucosa with lingual lipase activity levels in specimens of lingual serous glands indicates that in humans, gastric lipase is the main lipase active in the stomach.

Lingual and gastric lipases: species differences in the origin of prepancreatic digestive lipases and in the localization of gastric lipase

The source of the lipase(s) acting in the stomach was investigated in five animal species: rat, mouse (rodents), rabbit (lagomorphs), guinea pig (caviidae), baboon and human (primates). The activity of lingual and gastric lipases was quantitated in homogenates of lingual serous glands and of gastric mucosa, respectively, by the hydrolysis of tri[ 3H]oleylglycerol and is expressed in units/g ( 1 U = 1 μ mol [ 3H]moleic acid released/min) per g tissue wet weight, mean ± S.E. There were marked differences in the activity level of lingual and gastric lipases among species: mouse and rat had high levels of lingual lipase activity (250 ± 20 and 824 ± 224 U/g) and only traces of gastric lipase activity (4.5 ± 0.9 and 0.04 U/g, respectively), whereas rabbit and guinea pig had no lingual lipase activity and only gastric lipase activity (78 ± 48 and 27 ± 7.4 U/g, respectively). In the baboon and human, gastric lipase was the predominant enzyme (109 ± 20 U/g and 118 ± 8.8 U/g, respectively), whereas lingual lipase activity was present in trace amounts only (0.04 U/g and 0.3 U/g, respectively). In addition to species differences in the origin of the preduodenal lipases, there were also species differences in the distribution of gastric lipase in the stomach. Thus, while in the rabbit, gastric lipase was localized exclusively in the cardia and body of the stomach, it was diffusely distributed in the entire stomach of the guinea pig and baboon. A comparison between the level of activity of lipase and pepsin (the two chief digestive enzymes secreted by the stomach), showed differences in their localization in the species studied. The difference in source (tongue vs. stomach) and site (cardia-body vs. entire stomach) of lipase secretion must be taken into account in future studies of these digestive enzymes. Although the exact contribution of lingual and gastric lipases individually to fat digestion in species which contain both enzymes cannot yet be evaluated, the markedly higher levels of gastric lipase activity in the baboon and human suggests that, in primates, gastric lipase is probably the major non-pancreatic digestive lipase.

Secretion of lingual lipase and amylase from rat lingual serous glands

The effects of various secretagogues on the release of lingual lipase and amylase from rat lingual serous glands was examined in vitro and in vivo. After incubation, the media and tissues were assayed for lingual lipase and amylase activity to determine percent of secretion. In vitro secretion of lingual lipase and amylase stimulated by the cholinergic agonist, carbamylcholine chloride (carbachol), was 28.3 +/- 1.7, 48.0 +/- 3.2, and 55.9 +/- 2.4% and 18.1 +/- 1.7, 26.4 +/- 3.0, and 28.0 +/- 2.5%, respectively, for 30-, 60-, and 90-min incubations. The beta-adrenergic agonist, isoproterenol, and the adenylate cyclase activator, forskolin, elicited very little secretion in vitro; the 90-min values with isoproterenol were 16.8 +/- 7.1% lingual lipase and 6.0 +/- 2.6% amylase. The alpha-adrenergic agonist, phenylephrine, did not stimulate enzyme secretion. Morphological assessment of incubated tissues revealed that carbachol induced a rapid and extensive degranulation of the acinar cells, while isoproterenol caused only minimal exocytosis. In vivo stimulation by the cholinergic agonist, pilocarpine, caused rapid secretion, with maximal secretion occurring by 1 h. In vivo secretion stimulated by isoproterenol was slow, but by 4 h secretion was comparable to that induced by pilocarpine. In vitro, there was a significant difference between the percentages of lingual lipase and amylase secreted, which could not be accounted for by the presence of proteases or microbial products or the lack of stability of the enzymes during the incubation period. Neurotransmitter regulation of protein secretion by the lingual serous (minor salivary) glands appears to be principally cholinergic in contrast to the beta-adrenergic stimulation of protein secretion by the parotid (major salivary) gland.

Rat lingual lipase: effect of proteases, bile, and pH on enzyme stability.

In addition to initiating fat digestion in the stomach, lingual lipase may play a significant digestive role in the upper small intestine. By in vitro incubation techniques, the stability of rat lingual lipase at various physiological pH values, as well as the effects of pure proteases, rat gastric juice, bile, pancreatic juice, and mixed duodenal contents, on enzyme activity was explored. There were no changes in base-line activity of porcine pepsin, bovine carboxypeptidase-treated lipase, or heat-denatured proteases compared with controls after incubation at pH 2-6 at 37 degrees C for up to 1 h. In contrast, porcine trypsin-treated lipase demonstrated a significant loss from base-line activity to 59 +/- 12% (mean +/- SE) at pH 4, 34 +/- 11% at pH 6, and 41 +/- 4% at pH 8, and bovine chymotrypsin caused a loss in lipase activity to 11 +/- 7% at pH 8. Rat gastric juice containing 5,000 U pepsin reduced lipase activity to 17 +/- 5% of initial activity at pH 2 and to 45 +/- 3% at pH 4. Rat bile alone diminished activity only 35%, but rat pancreatic juice or mixed duodenal juice reduced lingual lipase activity to 1-12% of initial activity after 60 min at pH 6. Lingual lipase is particularly important in fat digestion in the stomach; however, its role in quantitative fat digestion under small intestinal conditions may be limited.

Lingual lipase in cystic fibrosis. Quantitation of enzyme activity in the upper small intestine of patients with exocrine pancreatic insufficiency.

We have measured the level of lingual lipase activity in gastric and duodenal aspirates of five patients with cystic fibrosis (CF) and pancreatic insufficiency. Lingual lipase activity (measured in vitro by the hydrolysis of long-chain triglyceride, tri-[3H]olein, at pH 4.2 and expressed in nanomoles FFA released per milliliter aspirate per minute) and pH in gastric and duodenal aspirates were measured at 10-min intervals during a a 30-min basal period and at 15-min intervals during a 2-h period after the ingestion of a test meal. In gastric aspirates, lingual lipase activity decreased from basal levels of 200 +/- 34 nmol FFA released per milliliter per minute (similar to values reported previously in normal subjects (Hamosh M., H. L. Klaeveman, R. O. Wolf, and R. O. Scow, 1975, J. Clin. Invest., 55:908-913) to 79 +/- 15 nmol FFA/ml per min during the first postprandial hour and returned to basal levels during the second postprandial hour, (206 +/- 39 nmol FFA/ml per min). Duodenal aspirates, obtained during basal conditions, had lingual lipase activity similar to that in the stomach, 178 +/- 63 nmol FFA/ml per min. Enzyme activity levels were 56 +/- 14 and 113 +/- 29 during the first and second postprandial hours. Measurements of total lipase activity delivered to the ligament of Treitz showed that lingual lipase amounted to 91.22 +/- 4.06% of the total lipase activity in the upper small intestine during the 150-min study period. The basal and postprandial gastric pH levels in the five CF patients studied (3.2 +/- 0.44, 4.0 +/- 0.16, and 4.4 +/- 0.4 for basal and first and second postprandial hours, respectively) did not differ from previously reported values for normal subjects. The pH of duodenal aspirates was however significantly lower (P less than 0.001) in CF patients, both under basal conditions (5.0 +/- 0.26) and during the first and second postprandial hours (4.9 +/- 0.13 and 4.4 +/- 0.36, respectively), than in normal subjects. The low postprandial duodenal pH enables lingual lipase to act not only in the stomach but to continue the hydrolysis of dietary fat in the upper small intestine of CF patients. The data presented show that lingual lipase remains fully active in CF and accounts for greater than 90% of total lipase activity in the upper small intestine. We suggest that, because of low intestinal pH in CF, enzyme replacement therapy containing lingual lipase could improve fat absorption in CF patients to a greater extent than the pancreatic preparations now in use.

Gastric lipolysis in the developing rat ontogeny of the lipases active in the stomach

The first step in fat digestion occurs in the stomach, where 10–30% of dietary triacylglycerols are hydrolyzed to partial (di- and mono-) acylglycerols and free fatty acids. Preduodenal fat digestion is an important compensatory mechanism in the newborn because of immature pancreatic (lipase) and hepatic (bile acid synthesis) function. Since hydrolysis of fat in the stomach can be catalyzed by enzymes of lingual (Hamosh, M. (1979) Pediatr. Res. 13, 615–622) and possibly gastric origin, we have studied the developmental patter and quantitative contribution of these two enzymes to intragastric fat digestion by measuring lipase activity in homogenates of lingual glands and gastric mucosa of rats from birth until 60 days of age. Total lipolytic activity in rat gastric mucosa was only 2–10% of that in the lingual glands throughout the entire period studied. Lingual lipase activity increased steadily from birth until day 50, whereas the activity in the gastric mucosa reached peak levels at 17–20 days and declined sharply after weaning. Throughout the period of study - suckling, weaning, and young adulthood - lingual and gastric lipase had very similar characteristics: pH optimum in the range of 5.0–6.0 and 2.5–5.0-fold higher activity on medium-chain (tri[14C]octanoin than long-chain (tri[3H]olein) triacylglycerols. In the lingual glands, lipase activity was higher during fasting, probably because of accumulation of enzyme (without depletion during meals), whereas in the gastric mucosa lipase levels were higher after feeding, suggesting adsorption of lingual lipase (which reaches the stomach with the ingested food) onto the gastric mucosa. From birth to weaning, there was rapid and extensive hydrolysis of triacylglycerol in the stomach (decrease from 98 mol% in rat milk to 33.6–48.9 mol% in the stomach contents half an hour after feeding). The intragastric lipolysis remained almost constant from birth until day 20, in spite of a marked increase in food consumption, probably because of the continued rise of lingual lipase levels. The direct relationship between high intragastric lipolysis and high lingual lipase activity suggests that lingual lipase is the major digestive enzyme in the newborn.

Hydrolysis of triacylglycerol emulsions by lingual lipase a microscopic study

The effect of lingual lipase on four different triacylglycerol emulsions was observed by light microscopy at pH 5–6. The extent of hydrolysis on the microscope slide was determined with the aid of radioactive emulsions or by analyzing the products by gas-liquid chromatography. Artificial emulsions that had been stabilized with amphiphilic lipids gradually coalesced during the unstirred lipase reactions. Gum arabic-stabilized emulsions and human milk fat droplets did not stick to each other or coalesce during lingual lipase hydrolysis. No visible liquid-crystalline product phases, as are seen with pancreatic lipase (Patton, J.S. and Carey, M.C. (1979) Science 204, 145–148), were observed with lingual lipase. The products of lingual lipase activity, protonated fatty acid and diacylglycerol, appear to remain dissolved in the oil phase of the triacylglycerol particle.

Gastric lipase in the newborn rat.

A substantial portion of rat milk triglycerides was hydrolyzed in the ligated stomach of suckling rats with excised lingual gland and pancreas, due to the action of gastric lipase. Free fatty acids were the main lipolytic products. There were some diglycerides and traces of monoglycerides. Medium chain length (C8-C12) fatty acids were predominantly recovered in the free fatty acid fraction, whereas the remaining tri- and diglycerides became richer in long chain (greater than or equal to C14) fatty acids suggesting a preferential lipolysis of medium chain fatty acid ester bonds. The lipase activity in extracts of stomach wall and sublingual gland tissue was more stable at acid pH and more resistant to the action of pepsin than the activity of pancreatic lipase. Trypsin strongly affected lingual lipase activity but only moderately reduced gastric and pancreatic lipase activity. Presence of sodium taurocholate made the lingual and gastric lipases less sensitive to proteolytic attack. It was also found that the activity of gastric lipase, related to the tissue protein content, decreased with the age of rats, whereas that of lingual lipase increased. The joint capacity of the stomach and lingual gland lipases amounted to about 50% of the total digestive lipolytic capacity 6 days after rat birth but decreased to about 20% at 60 days of life. This was due mainly to the considerable increase in the pancreatic gland size.

Gastric emptying and lingual lipase activity in cystic fibrosis.

To identify gastric factors likely to contribute to fat maldigestion and malabsorption in cystic fibrosis (CF), gastric emptying time, secretion rate, and preduodenal lipolytic activity were studied. Gastric emptying of a liquid test meal and gastric acid secretion were determined in five CF teenagers with pancreatic insufficiency and in five healthy controls. During the first hr, the rate of gastric emptying exhibited a linear pattern in both CF patients and controls. Neither the emptying time nor the gastric secretion rate was different. Lingual lipase activity was measured in eight other CF patients with pancreatic insufficiency and in eight controls. Lipase activity was higher (P less than 0.05) in CF patients than in controls with values (mean +/- S.E.) of 34.48 +/- 11.59 and 12.65 +/- 5.60 mumole butyric acid min-1 ml-1, respectively. No correlation with age or body surface was observed. Intragastric lipolysis of a butterfat triglyceride test meal was fast in both groups, but more extensive (P less than 0.05) in CF patients than in controls. The data show that in CF with pancreatic insufficiency, gastric factors contributing to the first step of fat digestion are preserved. In fact, lingual lipase activity was found to be increased, and a more complete intragastric lipolysis was documented.