1998
DOI: 10.1093/jn/128.10.1716
|View full text |Cite
|
Sign up to set email alerts
|

Digestibility of Cooked and Raw Egg Protein in Humans as Assessed by Stable Isotope Techniques

Abstract: Egg proteins contribute substantially to the daily nitrogen allowances in Western countries and are generally considered to be highly digestible. However, information is lacking on the true ileal digestibility of either raw or cooked egg protein. The recent availability of stable isotope-labeled egg protein allowed determination of the true ileal digestibility of egg protein by means of noninvasive tracer techniques. Five ileostomy patients were studied, once after ingestion of a test meal consisting of 25 g o… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

4
85
1
2

Year Published

2001
2001
2022
2022

Publication Types

Select...
8
1

Relationship

0
9

Authors

Journals

citations
Cited by 125 publications
(94 citation statements)
references
References 31 publications
4
85
1
2
Order By: Relevance
“…Such susceptibility serves to increase the proportion of protein digested by the consumer compared to the proportion digested by gut bacteria; this result is especially important, because the products of microbial fermentation of protein seem to return little energy to the consumer (2). This mechanism is supported by evidence that heat-induced denaturation of egg protein contributed to increased ileal digestibility in humans (91-94% for cooked eggs compared with 51-65% for raw eggs) (28,29). Second, diet-induced thermogenesis may have been reduced because of the compromised structural integrity of cooked meat.…”
Section: Resultsmentioning
confidence: 94%
“…Such susceptibility serves to increase the proportion of protein digested by the consumer compared to the proportion digested by gut bacteria; this result is especially important, because the products of microbial fermentation of protein seem to return little energy to the consumer (2). This mechanism is supported by evidence that heat-induced denaturation of egg protein contributed to increased ileal digestibility in humans (91-94% for cooked eggs compared with 51-65% for raw eggs) (28,29). Second, diet-induced thermogenesis may have been reduced because of the compromised structural integrity of cooked meat.…”
Section: Resultsmentioning
confidence: 94%
“…The changes in the level of amino acid after heat application may be due to breaking of bonds in some proteins that are heat labile. The degree of lability depends on the type of protein, type of solution and the temperature profile [18]. Table 3 depicts the various levels and types of fatty acids in the extracted fats from different egg samples.…”
Section: Resultsmentioning
confidence: 99%
“…Esto es totalmente erróneo. En primer lugar, porque el calor desnaturaliza las proteínas del huevo haciendo que sean más fácilmente digestibles (21). En segundo lugar, porque con el calor se inactivan algunas proteínas como la avidina, que es un factor antibiotina (22).…”
Section: Errores Y Tópicos En Relación Al Huevo En El Deporteunclassified