Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Johanna C. Rotticci-Mulder"'
Publikováno v:
Bioprocess and Biosystems Engineering. 24:385-393
A fusion protein composed of a cellulose binding domain from Neocallimastix patriciarum cellulase A and Candida antarctica lipase B (CBD-lipase) was produced by Pichia pastoris methanol utilization plus phenotype in high cell-density cultures. The ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bdf6aab37bbde2e2cab9d80445ed6ddb
https://doi.org/10.1007/s00449-001-0274-5
https://doi.org/10.1007/s00449-001-0274-5
Publikováno v:
Protein Science. 10:1769-1774
Entropy was shown to play an equally important role as enthalpy for how enantioselectivity changes when redesigning an enzyme. By studying the temperature dependence of the enantiomeric ratio E of an enantioselective enzyme, its differential activati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df27a10cd25cac1b29f9b456bbe4b75d
https://doi.org/10.1110/ps.13501
https://doi.org/10.1110/ps.13501
Publikováno v:
Chembiochem : a European journal of chemical biology. 6(6)
This thesis describes the use of rational redesign to modify the properties of the enzyme Candida antarctica lipase B. Through carefully selected single-point mutations, we were able to introduce substrate-assisted catalysis and to alter the reaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4450c4e0038766551584c4aedbaca6e9
https://pubmed.ncbi.nlm.nih.gov/15883973
https://pubmed.ncbi.nlm.nih.gov/15883973
Publikováno v:
Protein expression and purification. 21(3)
Candida antarctica lipase B (CALB) and C. antarctica lipase B fused to a cellulose-binding domain (CBD-CALB) were expressed functionally in the methylotrophic yeast Pichia pastoris. The cellulose-binding domain originates from cellulase A of the anae
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8d2033bd00e2ff5966620c63f1bbc34
https://pubmed.ncbi.nlm.nih.gov/11281712
https://pubmed.ncbi.nlm.nih.gov/11281712
Publikováno v:
ChemBioChem. 2:766
A model based on two different binding modes for alcohol enantiomers in the active site of a lipase allowed rational redesign of its enantioselectivity. 1-Halo-2-octanols were poorly resolved by Candida antarctica lipase B. Interactions between the s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44c5303610890cd4cab98702c34c43f8
https://doi.org/10.1002/1439-7633(20011001)2:10<766::aid-cbic766>3.0.co
https://doi.org/10.1002/1439-7633(20011001)2:10<766::aid-cbic766>3.0.co