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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1994-1-6
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pubmed:abstractText |
A feasibility study of the continuous enzymatic production of short oligopeptides was undertaken using the synthesis of [Leu5]-enkephalin pentapeptides as a model system. A three-stage bioreactor was designed to perform the independent syntheses of the constituent tri- and dipeptide fragments and their subsequent condensation. Both the N-terminal (N-X-L-Tyr.Gly.GlyOEt) and C-terminal (L-Phe.LeuNH2) peptides were prepared in 75-85% yield in column reactors packed with Celite-immobilized alpha-chymotrypsin. The enkephalin pentapeptide was obtained in up to 30% yield in the third bioreactor module containing Celite-immobilized proteinase K. The bioreactor was run continuously for over 1,000 h, producing, under steady-state conditions, up to 0.7 g day-1 of the pentapeptide.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
B
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0141-0229
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
928-35
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
pubmed-meshheading:7764252-Amino Acid Sequence,
pubmed-meshheading:7764252-Enkephalins,
pubmed-meshheading:7764252-Enzymes,
pubmed-meshheading:7764252-Feasibility Studies,
pubmed-meshheading:7764252-Kinetics,
pubmed-meshheading:7764252-Molecular Sequence Data,
pubmed-meshheading:7764252-Oligopeptides
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pubmed:year |
1993
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pubmed:articleTitle |
Continuous enzymatic production of oligopeptides: synthesis of an enkephalin pentapeptide in a multistage bioreactor.
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pubmed:affiliation |
Department of Biotechnology and Enzymology, AFRC Institute of Food Research, Reading, UK.
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pubmed:publicationType |
Journal Article
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