2024-03-28T13:34:49Zhttp://repository.helmholtz-hzi.de/oai/requestoai:repository.helmholtz-hzi.de:10033/86292019-08-30T11:31:22Zcom_10033_6830com_10033_6826col_10033_6868
2003-07
urn:hdl:10033/8629
Gamma Interferon Responses Induced by a Panel of Recombinant and Purified Mycobacterial Antigens in Healthy, Non-Mycobacterium bovis BCG-Vaccinated Malawian Young Adults
Black, Gillian F.
Weir, Rosemary E.
Chaguluka, Steven D.
Warndorff, David
Crampin, Amelia C.
Mwaungulu, Lorren
Sichali, Lifted
Floyd, Sian
Bliss, Lyn
Jarman, Elizabeth
Donovan, Linda
Andersen, Peter
Britton, Warwick
Hewinson, Glyn
Huygen, Kris
Paulsen, Jens
Singh, Mahavir
Prestidge, Ross
Fine, Paul E. M.
Dockrell, Hazel M.
2007-02-20T13:27:58Z
2003-07
2007-02-20T13:27:58Z
2003-07
Clinical and Diagnostic Laboratory Immunology 2003 10(4):602-611
1071-412X
1098-6588
12853392
10.1128/CDLI.10.4.602-611.2003
http://hdl.handle.net/10033/8629
164276
en_US
Copyright © 2003, American Society for Microbiology
American Society for Microbiology
oai:repository.helmholtz-hzi.de:10033/86002019-08-30T11:24:25Zcom_10033_6826col_10033_6872
1982-07
urn:hdl:10033/8600
Formation, Location, and Regulation of Endo-1,4-β-Glucanases and β-Glucosidases from Cellulomonas uda
Stoppok, Waltraud
Rapp, Peter
Wagner, Fritz
2007-02-20T12:52:39Z
1982-07
2007-02-20T12:52:39Z
1982-07
Applied and Environmental Microbiology 1982 44(1):44-53
0099-2240
1098-5336
http://hdl.handle.net/10033/8600
241966
en_US
oai:repository.helmholtz-hzi.de:10033/86012019-08-30T11:24:25Zcom_10033_6826col_10033_6872
1981-04
urn:hdl:10033/8601
Formation and Location of 1,4-β-Glucanases and 1,4-β-Glucosidases from Penicillium janthinellum
Rapp, Peter
Grote, Elisabeth
Wagner, Fritz
2007-02-20T12:54:28Z
1981-04
2007-02-20T12:54:28Z
1981-04
Applied and Environmental Microbiology 1981 41(4):857-866
0099-2240
1098-5336
http://hdl.handle.net/10033/8601
243824
en_US
oai:repository.helmholtz-hzi.de:10033/86882019-08-30T11:24:27Zcom_10033_6831com_10033_6826col_10033_6869
1989-02
urn:hdl:10033/8688
Hydroxycinnamoyl-CoA:Putrescine Hydroxycinnamoyltransferase in Tobacco Cell Cultures with High and Low Levels of Caffeoylputrescine 1
Meurer-Grimes, Barbara
Berlin, Jochen
Strack, Dieter
2007-02-21T08:26:32Z
1989-02
2007-02-21T08:26:32Z
1989-02
Plant Physiology 1989 89(2):488-492
0032-0889
1532-2548
http://hdl.handle.net/10033/8688
1055868
en_US
oai:repository.helmholtz-hzi.de:10033/86892019-08-30T11:25:07Zcom_10033_6831com_10033_6826col_10033_6869
1989-04
urn:hdl:10033/8689
Characterization of a meta-Fluorotyrosine-Tolerant Cell Culture of Eschscholtzia californica Cham
Berlin, Jochen
van Huystee, Robert B.
Witte, Ludger
Bender, Jürgen
Jäger, Hans J.
Wray, Victor
2007-02-21T08:27:10Z
1989-04
2007-02-21T08:27:10Z
1989-04
Plant Physiology 1989 89(4):1299-1305
0032-0889
1532-2548
http://hdl.handle.net/10033/8689
1056012
en_US
oai:repository.helmholtz-hzi.de:10033/87022019-08-30T11:24:27Zcom_10033_6826col_10033_6872
2005-05-31
urn:hdl:10033/8702
Proteome analysis of a recombinant Bacillus megaterium strain during heterologous production of a glucosyltransferase
Wang, Wei
Hollmann, Rajan
Fürch, Tobias
Nimtz, Manfred
Malten, Marco
Jahn, Dieter
Deckwer, Wolf-Dieter
2007-02-21T08:41:52Z
2005-05-31
2007-02-21T08:41:52Z
2005-05-31
Proteome Science 2005 3:4
1477-5956
15927046
10.1186/1477-5956-3-4
http://hdl.handle.net/10033/8702
1175100
en_US
http://www.proteomesci.com/content/3/1/4
http://creativecommons.org/licenses/by/2.0
Copyright © 2005 Wang et al; licensee BioMed Central Ltd.
BioMed Central
oai:repository.helmholtz-hzi.de:10033/124292019-08-30T11:33:55Zcom_10033_6826col_10033_6872
2007-06-25T14:20:33Z
urn:hdl:10033/12429
Systembiotechnologische Ansätze zur Prozessentwicklung
Deckwer, Wolf-Dieter
Jahn, Dieter
Zeng, An-Ping
Hempel, Deitmar C.
2007-06-25T14:20:33Z
2007-06-25T14:20:33Z
2007-06-25T14:20:33Z
Article
Chemie Ingenieur Technik 2006, 78:3,193-208
0009286X,15222640
10.1002/cite.200500156
http://hdl.handle.net/10033/12429
de
oai:repository.helmholtz-hzi.de:10033/5612612019-08-30T11:28:23Zcom_10033_6826col_10033_6872
2015-07-30T12:13:03Z
urn:hdl:10033/561261
Production and Properties of Xylan-Degrading Enzymes from Cellulomonas uda.
Rapp, P
Wagner, F
Gesellschaft fur Biotechnologische Forschung mbH, D-38124 Braunschweig, Germany.
Xylan degradation and production of beta-xylanase and beta-xylosidase activities were studied in cultures of Cellulomonas uda grown on purified xylan from birchwood. beta-Xylanase activity was found to be associated with the cells, although in various degrees. The formation of beta-xylanase activity was induced by xylotriose and repressed by xylose. beta-Xylosidase activity was cell bound. Both constitutive and inducible beta-xylosidase activities were suggested. beta-Xylanase and beta-xylosidase activities were inhibited competitively by xylose. beta-Xylanase activity had a pronounced optimum pH of 5.8, whereas the optimum pH of beta-xylosidase activity ranged from 5.4 to 6.1. The major products of xylan degradation by a crude preparation of beta-xylanase activity, in decreasing order of amount, were xylobiose, xylotriose, xylose, and small amounts of xylotetraose. This pattern suggests that beta-xylanase activity secreted by C. uda is of the endosplitting type. Supernatants of cultures grown on cellulose showed not only beta-glucanase but also beta-xylanase activity. The latter could be attributed to an endo-1,4-beta-glucanase activity which had a low beta-xylanase activity.
2015-07-30T12:13:03Z
2015-07-30T12:13:03Z
1986-04
Article
Production and Properties of Xylan-Degrading Enzymes from Cellulomonas uda. 1986, 51 (4):746-52 Appl. Environ. Microbiol.
0099-2240
16347038
http://hdl.handle.net/10033/561261
Applied and environmental microbiology
en
oai:repository.helmholtz-hzi.de:10033/6210312019-08-30T11:27:46Zcom_10033_6826col_10033_6872
2017-08-02T08:47:45Z
urn:hdl:10033/621031
High yield recombinant penicillin G amidase production and export into the growth medium using Bacillus megaterium
Yang, Yang
Biedendieck, Rebekka
Wang, Wei
Gamer, Martin
Malten, Marco
Jahn, Dieter
Deckwer, Wolf-Dieter
Abstract Background During the last years B. megaterium was continuously developed as production host for the secretion of proteins into the growth medium. Here, recombinant production and export of B. megaterium ATCC14945 penicillin G amidase (PGA) which is used in the reverse synthesis of β-lactam antibiotics were systematically improved. Results For this purpose, the PGA leader peptide was replaced by the B. megaterium LipA counterpart. A production strain deficient in the extracellular protease NprM and in xylose utilization to prevent gene inducer deprivation was constructed and employed. A buffered mineral medium containing calcium ions and defined amino acid supplements for optimal PGA production was developed in microscale cultivations and scaled up to a 2 Liter bioreactor. Productivities of up to 40 mg PGA per L growth medium were reached. Conclusion The combination of genetic and medium optimization led to an overall 7-fold improvement of PGA production and export in B. megaterium. The exclusion of certain amino acids from the minimal medium led for the first time to higher volumetric PGA activities than obtained for complex medium cultivations.
2017-08-02T08:47:45Z
2017-08-02T08:47:45Z
2006-11-28
2015-09-04T08:23:14Z
Journal Article
Microbial Cell Factories. 2006 Nov 28;5(1):36
http://dx.doi.org/10.1186/1475-2859-5-36
http://hdl.handle.net/10033/621031
en
Yang et al.