Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Marco Malten"'
Publikováno v:
Bioresource Technology. 102:2897-2903
Calculation of true sugar yields in high solids enzymatic hydrolysis of biomass is challenging due to the varying liquid density and liquid volume resulting from solid solubilization. Ignoring these changes in yield calculations can lead to significa
Autor:
Marco Malten, Boyke Bunk, Evelyne Deery, Jan-Henning Martens, Helen K. Leech, Martin J. Warren, Dieter Jahn, Rebekka Biedendieck, Heiko Barg
Publikováno v:
Microbial Biotechnology. 3:24-37
Cobalamin (vitamin B(12)) production in Bacillus megaterium has served as a model system for the systematic evaluation of single and multiple directed molecular and genetic optimization strategies. Plasmid and genome-based overexpression of genes inv
Autor:
Marco Malten, Stephanie Bringer-Meyer, Andreas Roth, Dieter Jahn, Martin Follmann, Carsten Bäumchen, Rebekka Biedendieck, Hermann Sahm
Publikováno v:
Biotechnology Journal. 2:1408-1416
An in vivo system was developed for the biotransformation of D-fructose into D-mannitol by the expression of the gene mdh encoding mannitol dehydrogenase (MDH) from Leuconostoc pseudomesenteroides ATCC12291 in Bacillus megaterium. The NADH reduction
Autor:
Dieter Jahn, Rebekka Biedendieck, Marco Malten, W.-D. Deckwer, Rajan Hollmann, Yang Yang, Wei Wang
Publikováno v:
Engineering in Life Sciences. 6:470-474
The production of biocatalysts is usually carried out in a few well-characterized microorganisms like E. coli or, in the case of pharmaceuticals, in animal cell culture. Although well known as an established system, protein production in E. coli is r
Autor:
Rebekka Biedendieck, Rajan Hollmann, Marco Malten, Yang Yang, Dieter Jahn, Wei Wang, Wolf-Dieter Deckwer
Publikováno v:
Chemie Ingenieur Technik. 78:289-294
During the past years plasmid systems for recombinant protein production using Bacillus megaterium were developed. These systems are based on multicopy plasmids with functional elements for cloning in Escherichia coli and induced gene expression in B
Autor:
Gilles P.M. Borrelly, Stephen E. J. Rigby, Helen K. Leech, Peter Heathcote, Evelyne Raux, Kirsty J. McLean, Dieter Jahn, Martin J. Warren, Nigel J. Robinson, Andrew W. Munro, Marco Malten
Publikováno v:
Journal of Biological Chemistry. 278:41900-41907
CbiX is a cobaltochelatase required for the biosynthesis of vitamin B12 and is found in Archaea as a short form (CbiXS containing 120-145 amino acids) and in some bacteria as a longer version (CbiXL containing 300-350 amino acids). Purification of ei
Autor:
Soon-Il Yun, Ahmad RM Yahya, Marco Malten, Doug Cossar, William A Anderson, Jeno M Scharer, Murray Moo-Young
Publikováno v:
Canadian Journal of Microbiology. 47:1137-1140
The influence of peptidases on human interleukin-3 (rhIL-3) production by a recombinant Streptomyces lividans strain was investigated. The bacterium produced several general peptidases and tripeptidyl peptidases compromising the authenticity of rhIL-
Autor:
Ahmad R. M. Yahya, William A. Anderson, Doug Cossar, Jeno M. Scharer, Marco Malten, Soon-Ii Yun, Murray Moo-Young
Publikováno v:
Canadian Journal of Microbiology. 47:1137-1140
The influence of peptidases on human interleukin-3 (rhIL-3) production by a recombinant Streptomyces lividans strain was investigated. The bacterium produced several general peptidases and tripeptidyl peptidases compromising the authenticity of rhIL-
Publikováno v:
Methods in enzymology. 510
An example of a rapid microtiter plate assay (fluorescence cellulose decay, FCD) that determines the conversion of cellulose in a washed biomass substrate is reported. The conversion, as verified by HPLC, is shown to correlate to the monitored FCD in
An example of a rapid microtiter plate assay (fluorescence cellulose decay, FCD) that determines the conversion of cellulose in a washed biomass substrate is reported. The conversion, as verified by HPLC, is shown to correlate to the monitored FCD in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a62c960ce3397560258f8fd8ac463bfa
https://doi.org/10.1016/b978-0-12-415931-0.00002-1
https://doi.org/10.1016/b978-0-12-415931-0.00002-1