Acid-active proteases to optimize dietary protein digestibility: a step towards sustainable nutrition

IntroductionHistorically, prioritizing abundant food production often resulted in overlooking nutrient quality and bioavailability, however, environmental concerns have now propelled sustainable nutrition and health efficacy to the forefront of global attention. In fact, increasing demand for protei...

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Main Authors: Wai Shun Mak, Chloe P. Jones, Kevin E. McBride, Emily A. P. Fritz, Julie Hirsch, J. Bruce German, Justin B. Siegel
Format: Article
Language:English
Published: Frontiers Media S.A. 2024-02-01
Series:Frontiers in Nutrition
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fnut.2024.1291685/full
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author Wai Shun Mak
Wai Shun Mak
Chloe P. Jones
Kevin E. McBride
Emily A. P. Fritz
Julie Hirsch
J. Bruce German
Justin B. Siegel
Justin B. Siegel
Justin B. Siegel
Justin B. Siegel
author_facet Wai Shun Mak
Wai Shun Mak
Chloe P. Jones
Kevin E. McBride
Emily A. P. Fritz
Julie Hirsch
J. Bruce German
Justin B. Siegel
Justin B. Siegel
Justin B. Siegel
Justin B. Siegel
author_sort Wai Shun Mak
collection DOAJ
description IntroductionHistorically, prioritizing abundant food production often resulted in overlooking nutrient quality and bioavailability, however, environmental concerns have now propelled sustainable nutrition and health efficacy to the forefront of global attention. In fact, increasing demand for protein is the major challenge facing the food system in the 21st century with an estimation that 70% more food is needed by 2050. This shift has spurred interest in plant-based proteins for their sustainability and health benefits, but most alternative sources of protein are poorly digestible. There are two approaches to solve digestibility: improve the digestibility of food proteins or improve the digestive capacity of consumers. Enhancing nutrient digestibility and bioavailability across diverse protein sources is crucial, with proteases presenting a promising avenue. Research, inspired by the proteases of human breast milk, has demonstrated that exogenous microbial proteases can activate within the human digestive tract and substantially increase the digestion of targeted proteins that are otherwise difficult to fully digest.MethodsHere, we introduce the use of an acid-active family of bacterial proteases (S53) to improve the digestibility and nutritional quality of a variety of protein sources, evaluated using the INFOGEST 2.0 protocol.ResultsResults from in vitro digestibility indicate that the most effective protease in the S53 family substantially improves the digestibility of an array of animal and plant-derived proteins—soy, pea, chickpea, rice, casein, and whey. On average, this protease elevated protein digestibility by 115% during the gastric phase and by 15% in the intestinal phase, based on the degree of hydrolysis.DiscussionThe widespread adoption of these proteases has the potential to enhance nutritional value and contribute to food security and sustainability. This approach would complement ongoing efforts to improve proteins in the food supply, increase the quality of more sustainable protein sources and aid in the nourishment of patients with clinically compromised, fragile intestines and individuals like older adults and high-performance athletes who have elevated protein needs.
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spelling doaj.art-8d9e0b28537a4f3c91432f7a8d0603a72024-02-08T04:29:18ZengFrontiers Media S.A.Frontiers in Nutrition2296-861X2024-02-011110.3389/fnut.2024.12916851291685Acid-active proteases to optimize dietary protein digestibility: a step towards sustainable nutritionWai Shun Mak0Wai Shun Mak1Chloe P. Jones2Kevin E. McBride3Emily A. P. Fritz4Julie Hirsch5J. Bruce German6Justin B. Siegel7Justin B. Siegel8Justin B. Siegel9Justin B. Siegel10Department of Chemistry, University of California, Davis, Davis, CA, United StatesDigestiva, Inc., Davis, CA, United StatesDigestiva, Inc., Davis, CA, United StatesDigestiva, Inc., Davis, CA, United StatesEmpowered Science, LLC, South Barrington, IL, United StatesDigestiva, Inc., Davis, CA, United StatesDepartment of Food Science and Technology, University of California, Davis, Davis, CA, United StatesDepartment of Chemistry, University of California, Davis, Davis, CA, United StatesDigestiva, Inc., Davis, CA, United StatesGenome Center, University of California, Davis, Davis, CA, United StatesDepartment of Biochemistry and Molecular Medicine, University of California, Davis, Davis, CA, United StatesIntroductionHistorically, prioritizing abundant food production often resulted in overlooking nutrient quality and bioavailability, however, environmental concerns have now propelled sustainable nutrition and health efficacy to the forefront of global attention. In fact, increasing demand for protein is the major challenge facing the food system in the 21st century with an estimation that 70% more food is needed by 2050. This shift has spurred interest in plant-based proteins for their sustainability and health benefits, but most alternative sources of protein are poorly digestible. There are two approaches to solve digestibility: improve the digestibility of food proteins or improve the digestive capacity of consumers. Enhancing nutrient digestibility and bioavailability across diverse protein sources is crucial, with proteases presenting a promising avenue. Research, inspired by the proteases of human breast milk, has demonstrated that exogenous microbial proteases can activate within the human digestive tract and substantially increase the digestion of targeted proteins that are otherwise difficult to fully digest.MethodsHere, we introduce the use of an acid-active family of bacterial proteases (S53) to improve the digestibility and nutritional quality of a variety of protein sources, evaluated using the INFOGEST 2.0 protocol.ResultsResults from in vitro digestibility indicate that the most effective protease in the S53 family substantially improves the digestibility of an array of animal and plant-derived proteins—soy, pea, chickpea, rice, casein, and whey. On average, this protease elevated protein digestibility by 115% during the gastric phase and by 15% in the intestinal phase, based on the degree of hydrolysis.DiscussionThe widespread adoption of these proteases has the potential to enhance nutritional value and contribute to food security and sustainability. This approach would complement ongoing efforts to improve proteins in the food supply, increase the quality of more sustainable protein sources and aid in the nourishment of patients with clinically compromised, fragile intestines and individuals like older adults and high-performance athletes who have elevated protein needs.https://www.frontiersin.org/articles/10.3389/fnut.2024.1291685/fullsustainabilityin vitro digestionacid proteasesustainable nutritionnutrition securityprotein digestibility
spellingShingle Wai Shun Mak
Wai Shun Mak
Chloe P. Jones
Kevin E. McBride
Emily A. P. Fritz
Julie Hirsch
J. Bruce German
Justin B. Siegel
Justin B. Siegel
Justin B. Siegel
Justin B. Siegel
Acid-active proteases to optimize dietary protein digestibility: a step towards sustainable nutrition
Frontiers in Nutrition
sustainability
in vitro digestion
acid protease
sustainable nutrition
nutrition security
protein digestibility
title Acid-active proteases to optimize dietary protein digestibility: a step towards sustainable nutrition
title_full Acid-active proteases to optimize dietary protein digestibility: a step towards sustainable nutrition
title_fullStr Acid-active proteases to optimize dietary protein digestibility: a step towards sustainable nutrition
title_full_unstemmed Acid-active proteases to optimize dietary protein digestibility: a step towards sustainable nutrition
title_short Acid-active proteases to optimize dietary protein digestibility: a step towards sustainable nutrition
title_sort acid active proteases to optimize dietary protein digestibility a step towards sustainable nutrition
topic sustainability
in vitro digestion
acid protease
sustainable nutrition
nutrition security
protein digestibility
url https://www.frontiersin.org/articles/10.3389/fnut.2024.1291685/full
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