Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Open Access Guideline
Open Access Guideline
Postgraduate Thesis Guideline
Postgraduate Thesis Guideline
Communities & Collections
Communities & Collections
Help
Help
Frequently Asked Questions
Frequently Asked Questions
Guides
Guides
Thesis submission
Thesis submission
MS without thesis term project submission
MS without thesis term project submission
Publication submission with DOI
Publication submission with DOI
Publication submission
Publication submission
Supporting Information
Supporting Information
General Information
General Information
Copyright, Embargo and License
Copyright, Embargo and License
Contact us
Contact us
Cloning and heterologous expression of the extracellular alpha-galactosidase from Aspergillus fumigatus in Aspergillus sojae under the control of gpdA promoter
Date
2010-07-01
Author
Gurkok, Suemeyra
Soyler, Betuel
Biely, Peter
Ögel, Zümrüt Begüm
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
185
views
0
downloads
Cite This
Aspergillus fumigatus is highly pathogenic especially for immunocompromised people however it can efficiently produce many industrially important enzymes. The gene coding et-galactosidase enzyme (aglB) of A. fumigatus IMI 385708 has been cloned onto pAN52-4 fungal expression vector and expressed in a GRAS organism, Aspergillus sojae ATCC11906 under the control of constitutive glyceraldehyde-3-phosphate dehydrogenase (gpdA) promoter. pAN52-4 fungal expression system allowed high level alpha-galactosidase production in media with simple sugar glucose as the sole carbon source and without a requirement for an inducer with a yield of 2.45 U/ml which is nearly 3-fold higher than the yield obtained from A. fumigatus grown in locust bean gum containing medium.
Subject Keywords
Process Chemistry and Technology
,
Biochemistry
,
Bioengineering
,
Catalysis
URI
https://hdl.handle.net/11511/56499
Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
DOI
https://doi.org/10.1016/j.molcatb.2009.09.012
Collections
Graduate School of Natural and Applied Sciences, Article
Suggestions
OpenMETU
Core
Optimal conditions for enhanced beta-mannanase production by recombinant Aspergillus sojae
Ozturk, Bengu; Çekmecelioğlu, Deniz; Ogel, Zumrut Begum (Elsevier BV, 2010-07-01)
Optimization of the growth conditions for maximum P-mannanase production in shake flasks by using recombinant Aspergillus sojae ATCC11906 (AsT1) was carried out by Box-Behnken design of response surface methodology. The highest beta-mannanase activity on the fourth day of cultivation at 30 degrees C was obtained as 363 U/ml in the optimized medium consisting of 7% sugar beet molasses, 0.43% NH(4)NO(3), 0.1% K(2)HPO(4) and 0.05% MgSO(4) (by weight per volume) at 207 rpm. On the sixth day of cultivation under...
Enantioselective synthesis of 4,5,6,7-tetrahydro-4-oxo-benzofuran-5-yl acetate and 1-benzyl-4,5,6,7-tetrahydro-4-oxo-1(H)-indol-5-yl acetate using chemoenzymatic methods
Demir, Ayhan Sıtkı; Caliskan, Zerrin; Sahin, Ertan (Elsevier BV, 2007-03-01)
The chemoenzymatic synthesis of both of the enantiomers of pharmacologically interesting compounds such as 4,5,6,7-tetrahydro-4-oxobenzofuran-5-yl acetate (2a), 4,5,6,7-tetrahydro-4-oxo-6,6-dimethylbenzofuran-5-yl acetate (2b), and their hydroxy derivatives 3a, 3b, 1-benzyl4,5,6,7-tetrahydro-4-oxo-1(H)-indol-5-yl acetate (5), starting from 6,7-dihydrobenzofuran-4(5H)-one (la), 6,7-dihydro-6,6-dimethylbenzofuran4(5H)-one (7b), and 1-benzyl-6,7-dihydro-1 H-indol-4(5H)-one (4) are reported. Manganese(III) acet...
Selective oxidation of propylene to propylene oxide using combinatorial methodologies
Miyazaki, T; Ozturk, S; Onal, I; Senkan, S (Elsevier BV, 2003-06-30)
Direct oxidation of propylene by oxygen to propylene oxide (PO) has been studied through the application of the techniques of combinatorial catalysis. Catalytic materials containing single and binary metal components were prepared by impregnating standard gamma-Al2O3 pellets. In the first stage, 34 single component catalytic materials at three different metal loading levels were prepared and screened for PO activity and selectivity using array channel microreactors and mass spectrometry. Experiments were co...
Isolation and immunological characterization of theta class glutathione-s-transferase gstt2-2 from bovine liver
İşgör, Sultan Belgin; Çoruh, Nursen; Department of Biochemistry (2004)
The glutathione-S-transferases (GSTs) (EC.2.5.1.18) are enzymes that participate in cellular detoxification of endogenous as well as foreign electrophilic compounds, function in the cellular detoxification systems and are evolved to protect cells against reactive oxygen metabolites by conjugating the reactive molecules to the nucleophile scavenging tripeptide glutathione (GSH, ?-glu-cys-gly). The GSTs are found in all eukaryotes and prokaryotic systems, in the cytoplasm, on the microsomes, and in the mitoch...
Fusarium roseum and Aspergillus oryzae-mediated enantioselective reduction of benzils to benzoins
Elmir, Ayhan S.; Ayhan, Peruze; Demirtas, Umut; Erkilic, Umut (Elsevier BV, 2008-11-01)
Aspergillus oryzae OUT5048 and Fusarium roseum OUT4019 were found to be effective biocatalysts in the reduction of benzils to optically active benzoins. Easily available symmetrical benzil derivatives were reduced to the corresponding benzoins [(S)-2-hydroxy-1,2-diphenylethanones] by A. oryzae OUT5048 with tip to 94% ee and by F roseum OUT4019 with up to 98% ee, respectively. In this Work. first general method for whole-cell-mediated selective reduction of benzils to benzoins is reported. It is also shown t...
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
S. Gurkok, B. Soyler, P. Biely, and Z. B. Ögel, “Cloning and heterologous expression of the extracellular alpha-galactosidase from Aspergillus fumigatus in Aspergillus sojae under the control of gpdA promoter,”
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
, pp. 146–149, 2010, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/56499.