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Role of feeding on lipase activity in gastric contents
Insights
Gastric lipase activity in neonates is higher at pH 5.5 and acid-resistant, differing from pancreatic lipase. This enzyme is present in fed infants and actively digests fats in the stomach.
Area of Science:
- Neonatal physiology
- Gastrointestinal biochemistry
- Enzymology
Background:
- Lipase activity in neonates is crucial for fat digestion.
- Gastric lipase characteristics in neonates are not fully understood.
- Distinguishing gastric lipase from pancreatic lipase is important for neonatal nutrition.
Purpose of the Study:
- To characterize gastric lipase activity in term and preterm neonates.
- To investigate the pH optimum and acid stability of neonatal gastric lipase.
- To assess the presence and activity of gastric lipase in relation to feeding patterns.
Main Methods:
- Collection of gastric contents from neonates.
- Assay of lipase activity at different pH levels (5.5 and 8.0).
- Assessment of lipase resistance to acid inactivation.
- Analysis of lipid substrate changes (triglycerides and diglycerides) during test meals.
Main Results:
- Lipase activity was detected in gastric contents of fed neonates, higher at pH 5.5 than pH 8.0.
- This gastric lipase exhibited greater resistance to acid inactivation compared to pancreatic lipase.
- Lipase activity increased significantly during test meals, with a decrease in triglycerides and an increase in diglycerides.
- Activity was absent in some infants before regular feeding was established.
Conclusions:
- Neonates possess a distinct gastric lipase with specific pH and acid stability properties.
- This gastric lipase plays an active role in intraluminal fat digestion in the neonatal stomach.
- Feeding status significantly influences the presence and activity of gastric lipase in neonates.
Abstract:
Lipase activity was recorded in gastric contents collected from healthy term and preterm neonates. In contrast to pancreatic lipase activity this lipase activity was higher at pH 5.5 than at pH 8.0 and it was more resistent to acid inactivation. Lipase activity was found in gastric contents from all infants who were regularly fed, but was not present in gastric contents from some infants when collected before regular feeding was established. During test meals lipase activity in gastric contents increased considerably in all infants studied. During such a test meal there was a progressive relative decrease in triglycerides whilst diglycerides showed a relative increase suggesting an active lipolytic process in the stomach. An assay procedure for determination of lipase activity in gastric contents is also described.