IngredientsLipase, widely recognized as triacylglycerol ester hydrolase (EC 3.1.1.3), represents a form of serine hydrolase and pertains to the α/β foldase family. In practical terms, lipase is an enzyme that breaks down fats during digestion. The Enzyme Commission designation EC 3.1.1.3 places it within the hydrolase class, acting on ester bonds. Lipases (EC 3.1.1.3) are hydrolases that catalyze triglyceride hydrolysis into free fatty acids and glycerol. The enzyme is water-soluble but acts at the water–lipid interface; lipase enzyme is water-soluble, so it can act only on the surface of fat molecules.
Lipase is found in many plants, animals, bacteria, and molds. In mammals, the body naturally produces lipase in several locations, with the pancreas being the primary source; however, smaller amounts are also made in the mouth (lingual lipase) and stomach (gastric lipase). Specifically, lingual lipase is secreted by the serous glands in the back of the tongue, whereas gastric lipase is synthesized and secreted by the chief cells of the fundic mucosa of the stomach.
Lipases are primarily found in microorganisms, constituting approximately 66% of the total. Microbial lipase sources can be categorized into three groups: bacteria, yeast, and fungi. Bacterial sources of lipases include Bacillus subtilis, Pseudomonas aeruginosa, Staphylococcus aureus, Serratia marcescens, and Escherichia coli. Yeast sources include Candida and Saccharomyces cerevisiae, while fungal sources include Aspergillus niger, Penicillium, Rhizopus, Mucor, and Geotrichum albus.
In plant foods, lipase is present in notable quantities in certain fruits and fermented foods. Avocados contain the digestive enzyme lipase, which breaks down fat molecules into smaller fatty acids and glycerol. Kefir is a fermented food that contains a variety of digestive enzymes, including lipases, proteases, and lactases. Sauerkraut is a fermented cabbage dish and contains the digestive enzymes lipase, lactase, and protease.
Not all lipase enzymes are created equal. The body produces several different types, each with specific characteristics and optimal working conditions. Pancreatic lipase, the most abundant type, works best in the alkaline environment of the small intestine. Gastric lipase functions in the acidic environment of the stomach, while lingual lipase begins working in the mouth.
Acid lipases are enzymes that have maximal activities at acidic pH values and catalyze the hydrolysis of the ester bonds of triacylglycerols and/or cholesteryl esters. Two acid lipases, lingual lipase and gastric lipase, initiate the hydrolysis of dietary triacylglycerols in the stomach. Gastric and pancreatic lipases belong to two distinct structural families and display very different biochemical and kinetic properties. The pancreatic lipase family also includes lipoprotein lipase and hepatic lipase.
Lipase supplements are available in several forms derived from different source organisms. Lipase supplements can be derived from different sources, each with unique advantages. Animal-derived lipases, such as those from porcine (pig) pancreas, closely mimic human pancreatic lipase but require a prescription and work primarily in the alkaline environment of the small intestine. For vegan or over-the-counter products, in most cases, the lipase in these products is derived from Aspergillus niger, a fungus-based, fermented product rather than ox or hog bile, which is the usual extract used for animal-based lipase supplements.
Products that contain lipase also usually contain other enzymes that help digest carbohydrates and protein. In the U.S., pancreatin, which contains lipase, amylase, and proteases, is rated against a government standard. Each "X" unit of pancreatin contains 25 USP units of amylase, 2 USP units of lipase, and 25 USP units of proteolytic enzymes.
Because pancreatic enzymes are proteins that are quickly destroyed by gastric acids, some formulations are encapsulated with acid-resistant microspheres or microtablets. Non–enteric-coated formulations must be coadministered with acid suppressants such as PPIs or H2 antagonists.
Regarding regulatory classification, over-the-counter pancreatic enzyme supplements are available without a prescription. Since they are classified as dietary supplements rather than drugs, the FDA does not control their production. While manufacturers of over-the-counter supplements are required to ensure the safety of their products, there are no controls on manufacturing consistency from one batch to the next. By contrast, Creon, Zenpep, Pancreaze, Ultresa, Viokace, and Pertzye are currently the only FDA-approved digestive enzymes marketed in the United States.
While lipase as a defined biochemical entity was not isolated or named until the modern era, fat-digesting enzymes in fermented foods have been in human use across many cultures for millennia. Fermentation is the chemical transformation of organic substances into simpler compounds by the action of enzymes, complex organic catalysts produced by microorganisms such as molds, yeasts, or bacteria. Enzymes act by hydrolysis, a process of breaking down or predigesting complex organic molecules to form smaller and, in the case of foods, more easily digestible compounds and nutrients. The enzyme lipase hydrolyzes complex fat molecules into simpler free fatty acids — a process exploited in the preparation of aged cheeses, fermented fish products, and cultured dairy.
Fermented foods, which naturally contain microbial enzymes including lipase, were widely used across cultures for improving digestion. Examples include fermented fish sauces in Southeast Asia, aged cheeses in Europe, and fermented grains or dairy in the Middle East and Central Asia.
By the early 20th century, lipase became a central focus in the study of digestion, and it was soon extracted and incorporated into medical treatments for pancreatic insufficiency and digestive disorders. Today, lipase remains an essential therapeutic enzyme for digestive health and is routinely used in functional medicine and clinical nutrition for people with impaired fat metabolism.
From a historical clinical standpoint, pancreatic lipase, which was for long the only lipase available for biochemical studies, remains an attractive enzyme with the development of lipase inhibitors for obesity treatment. It is also used for enzyme replacement therapy in case of exocrine pancreatic insufficiency.
The concept of digestive enzymatic "fire" in traditional Ayurvedic medicine in ancient India, while not explicitly defining lipase, recognized the importance of catalytic digestive forces. In Hinduism, digestive enzymes are analogous to Pachaka Pitta, crucial for food breakdown and digestion. Their secretion is controlled by the nervous system and gut microbiota, and is considered vital. Formal identification and extraction of lipase as a specific enzyme, however, belongs to the modern biochemical tradition, not ancient herbal medicine.
Lipase, widely recognized as triacylglycerol ester hydrolase (EC 3.1.1.3), represents a form of serine hydrolase pertaining to the α/β foldase family. In addition to its lipid hydrolysis capacity, lipase displays versatility by enabling reactions such as alcoholysis, esterification, transesterification, and amidation of triglycerides.
The primary catalytic function is the hydrolysis of triglycerides: lipase hydrolyzes dietary triglycerides to monoacylglycerols and free fatty acids. More precisely, pancreatic lipase releases fatty acids from carbons 1 and 3 of the triglyceride backbone, forming 2-monoglyceride plus two free fatty acids; since the fatty acid in position 2 usually remains intact, only small amounts of free glycerol are formed during intestinal lipid digestion.
In contrast to pancreatic lipase, yeast lipase is known to hydrolyze all three fatty acids at all stereospecific numbering (sn) positions of the glycerol molecule in a triglyceride, rather than the preferential sn-1 and sn-3 positions of pancreatic lipase. This difference in positional selectivity has implications for both digestion efficiency and supplement design.
Pancreatic lipase requires a protein cofactor for optimal activity in the intestinal environment. In order to overcome the inhibitory effect of bile salts present in the intestinal lumen, pancreatic lipase specifically requires the presence of a small pancreatic cofactor (colipase) which acts as an anchor for pancreatic lipase. Colipase also changes the pH optimum for lipase from 8.0 to 6.0. This is important because the small intestine typically operates at a near-neutral to slightly alkaline pH, and colipase helps optimize lipase function under these conditions.
Fat digestion is a sequential, anatomically distributed process involving multiple lipase types. In the mouth, lipid digestion begins as the glands of the tongue release lingual lipase, an enzyme that starts the process of breaking down large fats, such as triglycerides, the most abundant dietary type. Lingual lipase has a pH optimum of 3.5–6.0 and is not activated until chewed food enters the acidic environment of the stomach.
Together, gastric lipase and lingual lipase account for 10–30% of lipid hydrolysis that occurs in human adults, with gastric lipase contributing the most. Given the low concentrations of pancreatic lipase and bile salts in the neonatal phase, the acidic lipases are critical for lipid digestion and account for 50% of lipid hydrolysis in neonates.
In the small intestine, bile augments pancreatic lipase activity: bile contains bile salts, lecithin, and cholesterol-derived substances, so it acts as an emulsifier in the duodenum of the small intestine. The emulsification of fat droplets in the duodenum increases their surface area over a thousand-fold, thus making them more accessible to pancreatic lipases. Lipase works with bile from the liver to break down fat molecules so they can be absorbed and used by the body.
Pancreatic lipase is the only source for the enzymatic digestion of fat in the small intestine. Lipase hydrolyzes dietary triglycerides to monoacylglycerols and free fatty acids. Deficiency of pancreatic lipase results in serious fat malabsorption.
Because lipase is required to liberate free fatty acids from dietary fats, it is also indispensable for the absorption of fat-soluble vitamins. When lipase activity is deficient, the resulting fat malabsorption carries with it a deficit in vitamins A, D, E, and K. This is demonstrated clinically: lack of needed fats and fat-soluble vitamins is among the consequences of lipase deficiency.
Emerging research suggests that exogenous lipase supplementation may have effects beyond digestion. Recent studies show that consuming proteases and lipases can increase the levels of beneficial bacteria and short-chain fatty acids in rodent gut. These findings led researchers to hypothesize that intestinal lipases play beneficial roles by enriching beneficial bacteria. However, information on the effects of exogenous digestive enzymes on gut health and disease remains limited, and human clinical data in this area is lacking.
This is the most thoroughly studied and best-established indication for lipase-containing preparations, specifically in the form of pancreatic enzyme replacement therapy (PERT). Regardless of its etiology, the clinical standard for the management of pancreatic exocrine insufficiency (PEI) is pancreatic enzyme replacement therapy (PERT).
Evidence Level: Strong (multiple RCTs and a meta-analysis). A 2017 meta-analysis published in Oncotarget systematically reviewed the clinical evidence. PubMed, Medline, and the Cochrane library were searched for prospective randomized controlled trials (RCTs) published before December 2016; seven RCTs randomizing a total of 282 patients were identified and assessed. PERT significantly increased the coefficient of fat absorption (CFA) compared to both baseline (WMD: 26.56, 20.35 to 32.76; I² = 79.6%; P < 0.001) and placebo (WMD: 17.97, 12.61 to 23.34; I² = 76.7%; P < 0.001). Meanwhile, coefficients of nitrogen absorption, stool fat excretion, stool nitrogen excretion, and stool weight were significantly improved with no statistical differences in adverse events.
A double-blind, placebo-controlled RCT of pancreatin enteric-coated minimicrospheres (Creon 40000 MMS) in patients with pancreatic exocrine insufficiency due to chronic pancreatitis similarly confirmed efficacy. The results provided evidence for the efficacy of pancreatin (Creon 40000 MMS) in patients with pancreatic exocrine insufficiency due to chronic pancreatitis, confirming that this formulation is well tolerated with a good safety profile at the dose administered.
EPI is associated with various underlying conditions. There are multiple causes of pancreatic exocrine insufficiency including chronic pancreatitis, cystic fibrosis and pancreatic cancer.
Limitations: The meta-analysis identified considerable heterogeneity (I² up to 79.6%) across RCTs, likely reflecting differences in formulations, dosing regimens, underlying etiology, and outcome measurement. Most trials had relatively small sample sizes.
Most cystic fibrosis patients will experience pancreatic insufficiency. The pancreatic enzymes in pancrelipase catalyze the hydrolysis of fats to monoglycerides, glycerol, and free fatty acids, proteins into peptides and amino acids, and starch into dextrins and short chain sugars such as maltose and maltriose in the duodenum and proximal small intestine, thereby mimicking digestive enzymes physiologically secreted by the pancreas.
It has been proposed that a possible treatment option for exocrine pancreatic insufficiency would be enzyme replacement therapy using lingual lipase, increasing the amount of dietary fat absorption and decreasing the risk of malnutrition. The proposed mechanism of lingual lipase preferentially cleaving short and medium chain triacylglycerols provides a means for absorption without the need for micelle formation and chylomicrons. Short and medium chain free fatty acids can be absorbed directly through the mucosal cells into the bloodstream and hence play a crucial role in nutrition for CF patients and neonates.
Evidence Level: Strong for approved prescription pancrelipase products. Zenpep (pancrelipase) is an FDA-approved drug for the treatment of exocrine pancreatic insufficiency. Post-marketing data has been available on pancrelipase since 2009. Regarding the safety of newer microbial lipase formulations, a randomized controlled clinical trial published in The Journal of Pediatrics assessed the safety and efficacy of a novel microbial lipase in patients with exocrine pancreatic insufficiency due to cystic fibrosis.
Lipase is used for indigestion (dyspepsia), heartburn, and other gastrointestinal problems, but there is no good scientific evidence to support these uses as a standalone supplement. However, when lipase is combined with other digestive enzymes in multi-enzyme complexes, some controlled evidence exists.
A randomized, double-blind, placebo-controlled study published on PubMed (PMC6249666) evaluated a multi-enzyme complex (DigeZyme®) containing α-amylase, protease, cellulase, lactase, and lipase in patients with functional dyspepsia. The safety and efficacy of DigeZyme®, a proprietary multienzyme complex (MEC), was evaluated as a dietary supplement in FD patients. In this randomized, double-blind, placebo-controlled, parallel-group study, 40 patients were randomly assigned (1:1 ratio) to receive either MEC (50 mg, TID; n = 20) or placebo (n = 20) for 60 days. The enzyme supplement group showed statistically significant improvements in digestive symptoms including bloating, fullness, and postprandial distress compared to placebo.
A separate controlled study specifically examined lipase supplementation before a high-fat meal. The aim was to evaluate the effects of acid-resistant lipase on upper gastrointestinal symptoms, including fullness and bloating, as well as on gastric myoelectrical activity after healthy subjects ingested a high-fat, liquid meal. This study utilized a double-blind, placebo-controlled, crossover design with 16 healthy volunteers who ingested either a capsule containing 280 mg of acid-resistant lipase or a placebo immediately before a fatty meal (355 calories, 55% fat). Participants rated their stomach fullness, bloating, and nausea before and at timed intervals for 60 minutes after the meal.
Deficiency in digestive enzymes is also believed to be one of the contributing factors for functional dyspepsia, although the possible role of enzyme deficiency in its etiopathogenesis remains unclear. A few studies have suggested that therapy with multienzyme preparations is beneficial for reducing symptoms of flatulence, bloating, belching, fullness, and postprandial distress in patients with functional dyspepsia.
Evidence Level: Preliminary and limited. Most studies testing lipase for dyspepsia have tested it as part of a multi-enzyme blend rather than lipase alone, making it impossible to attribute effects specifically to lipase. Sample sizes have been very small (e.g., n=40 for the DigeZyme® trial), and the number of RCTs remains limited. The overall evidence is insufficient to make definitive conclusions.
A secondary analysis of a multicenter randomized trial published in 2025 found that around 20% of polymorbid older patients had plasma lipase concentrations below the reference range, suggesting exocrine pancreatic insufficiency, which placed them at a greater risk for failing to meet nutritional targets; however, they also demonstrated a pronounced improvement from nutritional support. EPI may play a significant role in the development of malnutrition, a condition commonly seen in elderly patients with multiple health issues. While the use of pancreatic enzyme replacement therapy in patients with diagnosed EPI is well established, there is a lack of studies investigating patients with malnutrition regarding EPI and potential benefit of such a treatment.
Evidence Level: Preliminary. This area is under-studied and the above finding is from secondary analysis, requiring further dedicated RCTs.
Research has investigated whether some patients with irritable bowel syndrome (IBS) may harbor undiagnosed exocrine pancreatic insufficiency. Research has shown that some patients with irritable bowel syndrome may have exocrine pancreatic insufficiency, which is the inability to properly digest food due to a lack of digestive enzymes made by the pancreas. A 2010 study looked at the prevalence of exocrine pancreatic insufficiency in diarrhea-predominant IBS patients and found that insufficiency was detected in at least 6.1 percent of patients studied.
People with celiac disease or Crohn's disease, and perhaps some people suffering from indigestion, may be deficient in pancreatic enzymes including lipase.
Evidence Level: Weak to preliminary. While EPI may coexist with IBS in a subset of patients, there are no high-quality dedicated RCTs of lipase supplementation specifically for IBS. Evidence linking lipase supplementation to improved outcomes in celiac disease or Crohn's disease remains indirect and insufficiently studied in humans.
Interestingly, lipase inhibition — rather than supplementation — has been validated as a therapeutic approach for obesity. Lipase inhibitors bind to gastric and pancreatic lipases in the intestine, preventing hydrolysis of dietary triglycerides into monoglycerides and fatty acids and the absorption of dietary fat. Currently, orlistat is the only drug approved by the FDA as a lipase inhibitor. Orlistat (Alli, Xenical) is a nonsystemic gastric lipase inhibitor that reduces intestinal absorption of dietary fat by approximately 30%. Pancreatic lipase inhibitor therapy has been validated as an efficacious way for preventing and treating obesity and overweight. This pharmacological context is important because it confirms the central physiological role of lipase in fat absorption.
A 2025 review published in PMC explored a novel potential role for exogenous lipases. Recent studies show that consuming proteases and lipases can increase the levels of beneficial bacteria and short-chain fatty acids in rodent gut. These findings led researchers to hypothesize that intestinal lipases play beneficial roles by enriching beneficial bacteria. However, information on their health benefits has remained limited. Understanding the effects of exogenous digestive enzymes could provide valuable insights into the health benefits of fermented foods and digestive enzyme supplements.
Evidence Level: Very preliminary; currently animal/preclinical data only. No human clinical trials have evaluated lipase for this purpose.
Lipase activity is measured in lipase units (LU) or United States Pharmacopeia units (USP units). Doses are titrated based on patient age and weight, extent of pancreatic insufficiency, and dietary fat intake.
Lipase seems to be safe for most people. It can cause some side effects such as nausea, cramping, and diarrhea. For prescription-grade pancrelipase, the common adverse drug reactions to pancrelipase treatment include headache, abdominal cramping, nausea, diarrhea, bloating, and constipation. Other common adverse drug reactions include vomiting, dizziness, cough, irritability, dysglycemia, and nasopharyngitis.
For over-the-counter standalone lipase supplements, there is not enough reliable information to know if lipase is safe or what the side effects might be.
The most clinically significant documented safety concern associated with high-dose lipase-containing products is fibrosing colonopathy. High doses of pancreatic enzyme replacement therapy are associated with the risk of fibrosing colonopathy. Colonic strictures have been reported in pediatric patients with cystic fibrosis who received dosages greater than 6,000 lipase units/kg for every meal. This rare but serious complication of enzyme replacement is characterized by GI obstruction, bloody diarrhea, abdominal pain, and poor weight gain. Patients with a history of fibrosing colonopathy should be closely monitored during treatment, as they may be at risk of progressing to colonic stricture.
Dose-response data on this risk come from a large case-control study published in the New England Journal of Medicine. After adjustment for a history of gastrointestinal complications and relevant medications, the relative risk of fibrosing colonopathy associated with a dose of 24,001 to 50,000 units of lipase per kilogram per day, compared with a dose of 0 to 24,000 units per kilogram per day, was 10.9 (95% CI, 1.6 to 71.8), and that associated with a dose of more than 50,000 units per kilogram per day was 199.5 (95% CI, 9.9 to 4026.0).
A study examining fibrosing colonopathy in cystic fibrosis patients found a strong dose-response relationship: there was a strong relationship between very high doses of pancreatic enzyme supplementation and formation of fibrosing colonopathy. These very high doses do not appear to be needed for adequate nutrient absorption and growth. Importantly, all 75 patients on at least 6,000 U lipase/kg/meal were able to tolerate a significant reduction in dose while achieving clinically acceptable nutrient absorption, with no change over one year in height and weight z scores.
In the contemporary era of dosing guidelines and reformulated products, the incidence of fibrosing colonopathy in people with cystic fibrosis is very low. A large prospective cohort study found a confirmed fibrosing colonopathy incidence rate of 0.0242 per 1,000 person-years exposed. Fibrosing colonopathy is a severe intestinal fibrotic process associated with very high doses of PERT in CF patients; therefore, care should be taken to avoid exceeding recommended doses (less than 10,000 lipase units per kg per day).
Chronic high doses of digestive enzyme products may cause fibrosing colonopathy, a condition that thickens the colon walls, narrowing the colon passage. Many patients show improvement with a decrease in supplemental digestive enzymes, but some may need resection of the narrowed portions of the colon.
No adequate human and animal reproduction studies for pancrelipase exist. According to the literature review, pancreatic enzymes are probably safe during pregnancy and delivery; administer cautiously.
At the time of published reviews, there were no well-known supplement or food interactions with lipase as a supplement. No reported interactions between this supplement and medicines were found. It is possible that unknown interactions exist. However, interactions involving the broader context of lipase inhibition are well-documented pharmacologically. Orlistat, a lipase inhibitor, reduces the absorption of fat-soluble vitamins and medicines that require fat for absorption. This is relevant because supplemental lipase and lipase inhibitors work in opposing directions.
Regarding formulation-specific handling: inadequate response to enteric-coated formulations may be caused by insufficient mixing of granules with food and/or slow dissolution and release of enzymes. This represents a practical, clinically relevant consideration rather than a drug interaction per se.
Over-the-counter pancreatic enzyme supplements are available without a prescription. Since they are classified as dietary supplements rather than drugs, the FDA does not control their production. While manufacturers of over-the-counter supplements are required to ensure the safety of their products, there are no controls on manufacturing consistency from one batch to the next. This distinction between OTC supplement-grade lipase and FDA-approved prescription pancrelipase is of substantial clinical importance.
The global market for digestive enzyme supplements was valued at USD 699.4 million in 2021 and is projected to reach USD 1.64 billion by 2031, underscoring the increasing consumer use of lipase-containing products. Consumers and practitioners should be aware that quality and potency may vary significantly across unregulated products.
Health conditions that Lipase may help support.
Supplemental lipase has been studied for postprandial abdominal discomfort including fullness and bloating. A double-blind, placebo-controlled crossover RCT showed acid-resistant lipase significantly reduced stomach fullness after a high-fat meal in healthy subjects. A 2023 RCT of a lipase-containing multi-enzyme blend in functional dyspepsia (n=120) demonstrated significant reductions in abdominal pain and improved quality of life.
Pancreatic exocrine insufficiency (PEI) is a recognized possible cause of persistent symptoms in celiac disease despite a gluten-free diet. A prospective, randomized, double-blind, placebo-controlled crossover trial of pancrelipase (lipase-containing preparation) in non-responsive celiac disease found no significant improvement in gastrointestinal symptom scores compared to placebo.
Lipase deficiency from exocrine pancreatic insufficiency causes steatorrhea — oily, malodorous, loose stools — by preventing adequate fat hydrolysis in the small intestine. Supplemental lipase (via PERT) reduces steatorrhea and associated diarrhea in this population. The evidence is mechanistically robust and confirmed by multiple RCTs.
Lipase is a core digestive enzyme catalyzing hydrolysis of triglycerides into fatty acids and glycerol. It is a principal component of FDA-regulated PERT for pancreatic exocrine insufficiency and is broadly used in digestive supplement formulations. Deficiency leads to steatorrhea and fat malabsorption.
Lipase catalyzes hydrolysis of dietary fats and is a standard component of digestive enzyme therapy for fat maldigestion-related food sensitivity, particularly in conditions of pancreatic insufficiency. Clinical evidence (PMC4923703) and recognized medical guidelines support lipase supplementation for improving fat digestion and reducing GI symptoms in enzyme-deficient and intolerant individuals.
There is limited but emerging clinical evidence for digestive enzyme blends containing lipase in IBS, particularly overlapping with IBD. A controlled study in 43 IBD-IBS overlap patients found that a combination supplement including digestive enzymes reduced bloating, flatulence, and abdominal pain. Evidence specific to lipase as an isolated agent in IBS is not established.
Digestive enzyme blends including lipase have been tested in IBD patients with overlapping IBS symptoms. A controlled trial in 43 IBD-IBS patients found that adding a digestive enzyme supplement to standard therapy reduced bloating, flatulence, and abdominal pain. Additionally, EPI can develop secondary to IBD, creating a clinical rationale for lipase supplementation in a subset of IBD patients.
Chronic pancreatitis destroys pancreatic acinar cells, reducing lipase output and causing exocrine pancreatic insufficiency (EPI). Lipase-containing pancreatic enzyme replacement therapy (PERT) is the established treatment. Multiple RCTs and meta-analyses confirm that PERT significantly improves fat absorption and reduces steatorrhea in chronic pancreatitis patients. Recommended dosing is 25,000–40,000 lipase units per meal using enteric-coated microspheres.
Bile from the gallbladder is required to emulsify dietary fats before pancreatic lipase can hydrolyze them. Gallbladder dysfunction or removal impairs this process, theoretically necessitating compensatory lipase support. Direct clinical evidence that lipase supplementation improves outcomes in gallstone disease is lacking; the relationship is physiological and rationale-based.
Body systems that Lipase may help support.
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