A MULTIENZYME TECHNIQUE FOR ESTIMATING PROTEIN DIGESTIBILITY
Abstract
An in vitro method using a multienzyme system for the estimation of protein digestibility has been developed. The multienzyme system consists of trypsin, chymotrypsin and peptidase. It was found that the pH of a protein suspension immediately after 10 min digestion with the multienzyme solution was highly correlated with the in vivo apparent digestibility of rats. Regression analyses of 23 samples tested showed that the correlation coefficient between pH at 10 min and in vivo apparent digestibility was 0.90 with a standard error of estimate of 2.23. The regression equation was Y = 210.464 ‐ 18.103, where “X” was the pH of protein suspension immediately after the 10 min digestion with the multienzyme solution. The most significant advantage of this in vitro method for predicting apparent protein digestibility was that it can be completed within 1 hr and with a high degree sensitivity. The method can detect the effects of trypsin inhibitor, chlorogenic acid, and heat treatment on protein digestibility. Strong buffer salts may affect the measurement of protein digestibility, but the buffering effects found in general food proteins and products tested did not create any problem with the procedure.
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The pH of a protein suspension immediately after 10 min digestion with the multienzyme solution at 37°C, or after an additional 10 min incubation with microbial protease at 55°C, was highly correlated with the in vivo apparent faecal digestibility of rats (0.90 with standard error of estimate 2.23 for the first study).
“The pH of a protein suspension immediately after 10 min digestion with the multienzyme solution at 378C (55) , or after an additional l0 min incubation with microbial protease at 558C (56) was highly correlated with the in vivo apparent faecal digestibility of rats (0•90 with a standard error of estimate of 2•23 for the first study).”
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- Authors
- HSU, H. W., VAVAK, D. L., SATTERLEE, L. D., & MILLER, G. A.
- Affiliations
- University of Nebraska–Lincoln (US)
- Venue
- Journal of Food Science
- Publisher
- Wiley
- Published
- 1977-09
- Volume
- 42
- Issue
- 5
- Pages
- 1269-1273
- ISSN
- 0022-1147 (ISSN-L)
- 1750-3841
- OpenAlex
- W2039285085
- Cited by
- 981
- References
- 0
- Citations by year
- 2026: 24 · 2025: 40 · 2024: 44 · 2023: 44 · 2022: 49 · 2021: 42 · 2020: 34 · 2019: 31 · 2018: 35 · 2017: 24 · 2016: 34 · 2015: 25 · 2014: 19 · 2013: 26 · 2012: 43
- FWCI
- 20.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Food Science (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Keywords
- protein digestibility, in vitro digestibility, trypsin, chymotrypsin, proteolytic enzymes, apparent digestibility, trypsin inhibitor, chlorogenic acid, heat treatment (food and biological processing), buffer salts, food proteins
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