rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
5
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pubmed:dateCreated |
1993-7-21
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pubmed:abstractText |
The mode of action of purified aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2 on a complex peptide mixture of a tryptic digest from bovine beta-casein was analyzed. The oligopeptides produced in the tryptic digest before and after aminopeptidase N treatment were identified by analysis of the N- and C-terminal amino acid sequences and amino acid compositions of the isolated peptides and by on-line liquid chromatography-mass spectrometry. Incubation of purified peptides with aminopeptidase N resulted in complete hydrolysis of many peptides, while others were only partially hydrolyzed or not hydrolyzed. The tryptic digest of beta-casein exhibits a strong bitter taste, which corresponds to the strong hydrophobicity of several peptides in the tryptic digest of beta-casein. The degradation of the "bitter" tryptic digest by aminopeptidase N resulted in a decrease of hydrophobic peptides and a drastic decrease of bitterness of the reaction mixture.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8100130-1352755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8100130-1367548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8100130-14907713,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8100130-16347329,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8100130-8320375
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0099-2240
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1430-6
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:8100130-Amino Acid Sequence,
pubmed-meshheading:8100130-Aminopeptidases,
pubmed-meshheading:8100130-Antigens, CD13,
pubmed-meshheading:8100130-Biodegradation, Environmental,
pubmed-meshheading:8100130-Caseins,
pubmed-meshheading:8100130-Chromatography, High Pressure Liquid,
pubmed-meshheading:8100130-Food Microbiology,
pubmed-meshheading:8100130-Humans,
pubmed-meshheading:8100130-Hydrolysis,
pubmed-meshheading:8100130-Lactococcus lactis,
pubmed-meshheading:8100130-Molecular Sequence Data,
pubmed-meshheading:8100130-Peptide Fragments,
pubmed-meshheading:8100130-Taste,
pubmed-meshheading:8100130-Trypsin
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pubmed:year |
1993
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pubmed:articleTitle |
Degradation and debittering of a tryptic digest from beta-casein by aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2.
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pubmed:affiliation |
Department of Microbiology, University of Groningen, Haren, The Netherlands.
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pubmed:publicationType |
Journal Article
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