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- Publisher
- Wiley
- Copyright
- Copyright © 1977 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 0022-1147
- eISSN
- 1750-3841
- DOI
- 10.1111/j.1365-2621.1977.tb14476.x
- Publisher site
- See Article on Publisher Site
Abstract
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.
Journal
Journal of Food Science – Wiley
Published: Sep 1, 1977