Linked Life Data

1820029

Source:http://linkedlifedata.com/resource/pubmed/id/1820029

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10-11
pubmed:dateCreated
1992-7-24
pubmed:abstractText
Synthesis of dipeptides benzoyl Arginine leucinamide and kyotorphin catalyzed by highly stabilized derivatives of trypsin and chymotrypsin have been performed. Extreme experimental conditions could be tested and parameters of industrial interest could be improved provided the high activity and stability of the derivatives in these unfavourable environments. Thermodynamically controlled synthesis catalyzed by trypsin could be optimized and 97% conversion was obtained in 90% organic cosolvents. 100% yields were achieved in kinetically controlled synthesis catalyzed by trypsin in aqueous medium in the presence of IM Ammonium Sulphate. Higher starting concentrations of poorly soluble substrates of chymotrypsin could be used in a reaction medium containing 50% DMF and 95% yield were obtained.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0232-766X
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
S110-3
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Immobilization-stabilization of proteases as a tool to improve the industrial design of peptide synthesis.
pubmed:affiliation
Instituto de Catálisis, CSIC, Campus Universidad Autónoma, Madrid, Spain.
pubmed:publicationType
Journal Article