Linked Life Data

17625234

Source:http://linkedlifedata.com/resource/pubmed/id/17625234

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-7-12
pubmed:abstractText
The high-density fermentation of recombinant Pichia pastoris was carried out in a 1-L fermentor. After 60 h of fermentation, the activities of D-amino acid oxidase (DAAO) and catalase assayed with the permeabilized cells attained 12,532 and 684,800 U/L, respectively. Additionally, the stability of DAAO and catalase within the permeabilized cells was relatively high. The half-life of the two enzymes reached 14.5 and 4.0 d at 30 degrees C, respectively. Furthermore, these permeabilized cells could convert D-phenylalanine into 99% phenylpyruvate within 100 min and could be efficiently reused up to 13 cycles. After being treated with base and heating, these treated permeabilized cells could be reused up to three cycles in a batchwise conversion of cephalosporin C, and about 90% 7-beta-(4-carboxybutanamido)-cephalosporanic acid was ultimately obtained at each cycle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0273-2289
pubmed:author
pubmed:issnType
Print
pubmed:volume
136
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
279-89
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Characterization and application of D-amino acid oxidase and catalase within permeabilized Pichia pastoris cells in bioconversions.
pubmed:affiliation
State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai 200237, P.R. China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't