Abstract
ABSTRACT Peanut ( Arachis hypogaea L) seed were heated at 125C and 150C between 0 to 24 min and the seed proteins were extracted with 0.1 M sodium phosphate buffer, pH 2.5. The soluble and insoluble proteins were analyzed to determine changes in protein and polypeptide composition during heating. Acid soluble proteins were more susceptible to thermal breakdown than acid insoluble proteins. Within the acid soluble fraction, some proteins and polypeptides were more readily degraded than the others. In the acid insoluble fraction, except for the loss of a 70,000 Dalton polypeptide no other major changes were observed. Changes in protein composition were more rapid at 150C heating than at 125C heating. These data suggest that the proteins of the acid soluble fraction are highly sensitive to heating and thus may have a role in flavor volatile production during roasting of the peanut.
Abstract from the paper’s OpenAlex record, shown for indexing and research. Copyright remains with the authors or the publisher. Read at the source ↗
The text the model read, with the source record’s inline markup (italics, sub- and superscripts) rendered and its character entities decoded; quote offsets refer to the raw text.
Claims 5
Claim · model-written summary
Acid-soluble peanut seed proteins broke down more readily under heat than acid-insoluble proteins.
- Taxon
- PEANUT
Arachis hypogaeat0 - Treatment
- thermale0
- Outcome
- Acid soluble proteinse0
- Direction
- more susceptiblee0
- Comparator
- acid insoluble proteinse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Acid soluble proteins were more susceptible to thermal breakdown than acid insoluble proteins.”
t0“PEANUT SEED”
Claim · model-written summary
Some acid-soluble proteins and polypeptides degraded more readily than others.
- Taxon
- PEANUTArachis hypogaeat0
- Outcome
- proteins and polypeptidese0
- Direction
- more readily degradede0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Within the acid soluble fraction, some proteins and polypeptides were more readily degraded than the others.”
t0“PEANUT SEED”
Claim · model-written summary
A 70,000 Dalton polypeptide was lost from the acid-insoluble fraction.
- Taxon
- PEANUTArachis hypogaeat0
- Outcome
- polypeptidee0
- Direction
- losse0
- Value
- 70,000 Daltone0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“In the acid insoluble fraction, except for the loss of a 70,000 Dalton polypeptide no other major changes were observed.”
t0“PEANUT SEED”
Claim · model-written summary
No other major protein changes were observed in the acid-insoluble fraction.
- Taxon
- PEANUTArachis hypogaeat0
- Outcome
- major changese0
- Direction
- no other major changese0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“In the acid insoluble fraction, except for the loss of a 70,000 Dalton polypeptide no other major changes were observed.”
t0“PEANUT SEED”
Claim · model-written summary
Protein composition changed faster at 150C than at 125C.
- Taxon
- PEANUTArachis hypogaeat0
- Treatment
- 150C heatinge0
- Outcome
- Changes in protein compositione0
- Direction
- more rapide0
- Comparator
- 125C heatinge0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Changes in protein composition were more rapid at 150C heating than at 125C heating.”
t0“PEANUT SEED”
The same questions in other papers
heat · quality: protein · Arachis hypogaea (peanut)Positive and negative results
2 in the opposite direction
- negative
- negative
Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.