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Use of the Protease Fluorescent Detection Kit to Determine Protease Activity
Published on: August 4, 2009
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Protease Inhibitors in Processed Plant Foods.
1Department of Nutritional Science, Mead Johnson Nutritional Group, Evansville, Indiana 47721.
Journal of Food Protection
|April 11, 2019
Summary
Plant protease inhibitors, especially from soybeans, affect nutritional quality and can impact animal health. However, processed plant proteins for human consumption have low, safe levels of these inhibitors.
Area of Science:
- Biochemistry
- Toxicology
- Nutrition
Background:
- Plants, particularly legumes like soybeans, contain various protease inhibitors.
- Serine protease inhibitors (trypsin, chymotrypsin) from legumes are well-studied.
- These inhibitors in unheated proteins have known biological effects.
Purpose of the Study:
- To summarize the known effects of plant protease inhibitors.
- To address the nutritional and toxicological significance of these compounds.
- To clarify the safety of processed plant proteins.
Main Methods:
- Literature review of studies on plant protease inhibitors.
- Analysis of effects on nutritional quality.
- Examination of toxicological impacts in animal models.
- Assessment of processed food safety.
Main Results:
- Unheated legume proteins with inhibitors impair nutritional quality.
- Inhibitors can induce pancreatic hypertrophy and enhance carcinogen action in specific animals.
- Some studies report pancreatic carcinogenicity and tumor inhibition.
- Commercially processed plant proteins have low, nutritionally insignificant inhibitor levels.
Conclusions:
- While unheated plant protease inhibitors have significant biological effects, their levels in processed foods are of no nutritional concern.
- Further research is needed on the physiological significance of residual inhibitors in processed foods.
- Plant-derived protease inhibitors warrant continued study for both their risks and potential benefits.
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