Ingredient Library, Digestive Enzymes

Adaptive Regulation of Digestive Enzymes in Response to Dietary Substrate Availability and Nutritional Status

Animals have the ability to adapt their digestive enzymes to changing substrates that make up their diet. As an illustration of this, when starches are consumed in larger quantities, the result is typically increased levels of the pancreatic enzyme amylase and more efficient carbohydrate digestion and absorption. The adaptation of digestive enzymes allows for adjustments to be made to the amount of nutrients that enter the animal's system based on the amount of nutrients present in the diet. In situations where an animal is under-nourished or lacks sufficient levels of the enzymes needed to digest food, this type of adaptation allows for increased efficiency of nutrient use by allowing for increased compensatory digestive ability.

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Bromelain and Papain as Natural Proteolytic Alternatives for Teeth Whitening and Caries Removal

The use of bromelain and papain as aids in tooth whitening and as gentle means of removing carious tissue from teeth by degrading salivary proteins and protein components in damaged tissues is well-supported by research. Both protease enzymes appear to have good safety profiles and a wide scope for use as natural alternatives to hydrogen peroxide-based tooth-whitening agents.

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Bromelain and Papain Supplementation Enhances Protein Digestion and Modulates Gut Microbiota by Promoting Akkermansia and Reducing Proteobacteria

Bromelain and papain supplementation have been shown to improve protein digestion, support increased levels of the probiotic bacterium Akkermansia muciniphila, and suppress the overgrowth of potentially harmful groups of bacteria (e.g., Proteobacteria), resulting in an overall improvement in the gut microflora. In addition, supplementation with various proteases has been shown to enhance trypsin activity and improve intestinal mucosal function.

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Crude Lipase from Aspergillus niger for Efficient Degradation of Animal Fats: Biotechnological and Environmental Applications

Crude Aspergillus niger-generated lipases are stable and well-positioned to be utilized to degrade fat via efficient hydrolysis of oil and grease waste when acting under proper conditions. This lipase has a strong ability to degrade many different natural animal fats; specifically, this enzyme has been shown to degrade in excess of 90% of chicken fat as well as mutton fat over the span of 5 days. Therefore, the application of this enzyme may hold promise for industrial use within the food and environmental oil and grease remediation sectors.

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Fungal Lipase as an Acid-Stable Alternative to Porcine Pancreatic Lipase for Fat Digestion in Exocrine Pancreatic Insufficiency

This research looked at the ability of fungal lipase to break down fat (through use of a tiny-TIM) and compared this ability to that of porcine pancreatic lipase in patients with severe pancreatic exocrine insufficiency. A 14,000 Unit (U) fungal lipase supplement provided similar results as a 20,000 U porcine pancreatic lipase supplement in lipid digestion. Results from this study showed that the strong gastric acid resistance of fungal lipase allows it to work either in capsule or powder forms, and it has been shown to act similarly as traditional animal sources, providing an effective alternative to improving fat digestion and nutrition absorption for people with pancreatic insufficiency.

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α-Amylase: Structural Diversity, Catalytic Mechanisms, and Biotechnological Potential Across Glycoside Hydrolase Families

α-Amylase as an important glycoside hydrolases have a great impact on degrading carbohydrates; α-amylases hydrolyze a major portion of the carbohydrates by cleaving the α-1,4-glycosidic bonds in starch. In terms of classifications of α-amylases based on enzymes, most investigators have concluded that α-amylases are predominantly classified in the GH13 family; however, α-amylases are classified in a variety of GH families including GH57 and GH119. The variously defined structural domains and mechanism(s) of action of α-amylases enhance the vast assortment of substrates that α-amylases can readily accommodate resulting in a diverse variety of applications for α-amylase enzymes.

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Plant-Derived α-Amylase Inhibitors as Natural Adjuncts for Postprandial Glycemic Control in Diabetes

Antioxidant and anti-inflammatory effects of plant-derived α-amylase inhibitors suggest that they can be useful in delaying carbohydrate digestion and helping to control the increase in blood glucose levels after meals (postprandial), by decreasing α-amylase enzyme activities. The potential for using the natural products described here as adjunctive therapies for diabetes is promising.

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