2024-03-28T19:32:38Zhttp://repository.helmholtz-hzi.de/oai/requestoai:repository.helmholtz-hzi.de:10033/86002019-08-30T11:24:25Zcom_10033_6826col_10033_6872
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Applied and Environmental Microbiology 1982 44(1):44-53
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241966
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Formation, Location, and Regulation of Endo-1,4-β-Glucanases and β-Glucosidases from Cellulomonas uda
YES
2018-06-12T22:16:22Z
ORIGINAL
Stoppok et al_final.pdf
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free text from BMCs free repository PubMed Central
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THUMBNAIL
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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Rapp, Peter
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Grote, Elisabeth
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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
Formation and Location of 1,4-β-Glucanases and 1,4-β-Glucosidases from Penicillium janthinellum
YES
2018-06-12T23:59:49Z
ORIGINAL
rapp et al_final.pdf
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free text from PubMedCentral
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rapp et al_final.pdf.txt
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Extracted Text
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THUMBNAIL
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/87022019-08-30T11:24:27Zcom_10033_6826col_10033_6872
Wang, Wei
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Hollmann, Rajan
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Deckwer, Wolf-Dieter
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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
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1175100
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BioMed Central
http://www.proteomesci.com/content/3/1/4
http://creativecommons.org/licenses/by/2.0
Copyright © 2005 Wang et al; licensee BioMed Central Ltd.
Proteome analysis of a recombinant Bacillus megaterium strain during heterologous production of a glucosyltransferase
YES
2018-06-12T22:17:18Z
ORIGINAL
Wang et al_final.pdf
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MD5
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Wang et al_final.pdf.txt
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2019-08-30 11:24:27.427
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/124292019-08-30T11:33:55Zcom_10033_6826col_10033_6872
Deckwer, Wolf-Dieter
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Hempel, Deitmar C.
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2007-06-25T14:20:33Z
2007-06-25T14:20:33Z
2007-06-25T14:20:33Z
Chemie Ingenieur Technik 2006, 78:3,193-208
0009286X,15222640
10.1002/cite.200500156
http://hdl.handle.net/10033/12429
210881 bytes
13543424 bytes
application/pdf
application/vnd.ms-powerpoint
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de
Systembiotechnologische Ansätze zur Prozessentwicklung
Article
2018-06-13T01:07:37Z
ORIGINAL
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Abb zu CIT Paper 07.09.05.ppt
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figures in Powerpoint presentation
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LICENSE
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MD5
3
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TEXT
Deckwer_CIT.pdf.txt
Deckwer_CIT.pdf.txt
Extracted Text
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https://hzi.openrepository.com/bitstream/10033/12429/8/Deckwer_CIT.pdf.txt
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MD5
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Abb zu CIT Paper 07.09.05.ppt.txt
Abb zu CIT Paper 07.09.05.ppt.txt
Extracted text
text/plain
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THUMBNAIL
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Generated Thumbnail
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MD5
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Deckwer_CIT.pdf.jpg
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2019-08-30 11:33:55.101
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/5612612019-08-30T11:28:23Zcom_10033_6826col_10033_6872
Rapp, P
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Wagner, F
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Gesellschaft fur Biotechnologische Forschung mbH, D-38124 Braunschweig, Germany.
2015-07-30T12:13:03Z
2015-07-30T12:13:03Z
1986-04
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
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.
en
Production and Properties of Xylan-Degrading Enzymes from Cellulomonas uda.
Article
2018-06-13T05:27:33Z
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.
ORIGINAL
Rapp and Wagner_final.pdf
Rapp and Wagner_final.pdf
allowed publisher's PDF
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LICENSE
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TEXT
Rapp and Wagner_final.pdf.txt
Rapp and Wagner_final.pdf.txt
Extracted Text
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MD5
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THUMBNAIL
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oai:hzi.openrepository.com:10033/561261
2019-08-30 11:28:23.914
Helmholtz Zentrum für Infektionsforschung Repository
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oai:repository.helmholtz-hzi.de:10033/6210312019-08-30T11:27:46Zcom_10033_6826col_10033_6872
Yang, Yang
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Biedendieck, Rebekka
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Wang, Wei
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Gamer, Martin
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Malten, Marco
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Jahn, Dieter
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Deckwer, Wolf-Dieter
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2017-08-02T08:47:45Z
2017-08-02T08:47:45Z
2006-11-28
2015-09-04T08:23:14Z
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
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.
High yield recombinant penicillin G amidase production and export into the growth medium using Bacillus megaterium
Journal Article
en
Yang et al.
2018-06-12T22:08:31Z
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.
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2019-08-30 11:27:46.658
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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