pubmed-article:8100130 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8100130 | lifeskim:mentions | umls-concept:C0544170 | lld:lifeskim |
pubmed-article:8100130 | lifeskim:mentions | umls-concept:C0054943 | lld:lifeskim |
pubmed-article:8100130 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
pubmed-article:8100130 | lifeskim:mentions | umls-concept:C0005198 | lld:lifeskim |
pubmed-article:8100130 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
pubmed-article:8100130 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:8100130 | pubmed:dateCreated | 1993-7-21 | lld:pubmed |
pubmed-article:8100130 | 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. | lld:pubmed |
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pubmed-article:8100130 | pubmed:language | eng | lld:pubmed |
pubmed-article:8100130 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8100130 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8100130 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8100130 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8100130 | pubmed:month | May | lld:pubmed |
pubmed-article:8100130 | pubmed:issn | 0099-2240 | lld:pubmed |
pubmed-article:8100130 | pubmed:author | pubmed-author:KoningsW NWN | lld:pubmed |
pubmed-article:8100130 | pubmed:author | pubmed-author:BruinsA PAP | lld:pubmed |
pubmed-article:8100130 | pubmed:author | pubmed-author:ZuurendonkP... | lld:pubmed |
pubmed-article:8100130 | pubmed:author | pubmed-author:TanP SPS | lld:pubmed |
pubmed-article:8100130 | pubmed:author | pubmed-author:van KesselT... | lld:pubmed |
pubmed-article:8100130 | pubmed:author | pubmed-author:van de... | lld:pubmed |
pubmed-article:8100130 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8100130 | pubmed:volume | 59 | lld:pubmed |
pubmed-article:8100130 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8100130 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8100130 | pubmed:pagination | 1430-6 | lld:pubmed |
pubmed-article:8100130 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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pubmed-article:8100130 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8100130 | pubmed:articleTitle | Degradation and debittering of a tryptic digest from beta-casein by aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2. | lld:pubmed |
pubmed-article:8100130 | pubmed:affiliation | Department of Microbiology, University of Groningen, Haren, The Netherlands. | lld:pubmed |
pubmed-article:8100130 | pubmed:publicationType | Journal Article | lld:pubmed |
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