Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Altan Erarslan"'
Publikováno v:
Engineering in Life Sciences. 12:662-671
Alkaline proteases are one of the most important group of enzymes that are indispensable in a number of different industrial sectors. In this work, the effect of copper ions (Cu2+) was investigated for improving the thermostability and hydrolytic per
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::22a99f02cfd67f0beaed5de601f13a18
https://doi.org/10.1002/elsc.201200017
https://doi.org/10.1002/elsc.201200017
Autor:
Aziz Akin Denizci, Dilek Kazan, Francesco Secundo, Dario Grimoldi, Dilek Coşkuner Öztürk, Altan Erarslan
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 64:184-188
Proteases are largely employed in biocatalysis. In order to increase the number of their applications it is useful to shed light on the reasons that cause a non-optimal activity of these enzymes when used in inactivating experimental conditions (e.g.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::037c1571c95474ff2fdcbbb31cb3281c
https://doi.org/10.1016/j.molcatb.2009.02.017
https://doi.org/10.1016/j.molcatb.2009.02.017
Autor:
Hasan Umit Ozturk, Dilek Coşkuner Öztürk, Altan Erarslan, Hulya Bal, Aydan Salman Dilgimen, Dilek Kazan, Aziz Akin Denizci, Nurcin Celik Ozturk
Publikováno v:
Preparative Biochemistry and Biotechnology. 39:289-307
An alkali tolerant Bacillus strain having extracellular serine alkaline protease activity was newly isolated from compost and identified as Bacillus clausii GMBE 22. An alkaline protease (AP22) was 4.66-fold purified in 51.5% yield from Bacillus clau
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfbe02704182285f70ec69d844602e7d
https://doi.org/10.1080/10826060902953269
https://doi.org/10.1080/10826060902953269
Autor:
Halil Koçer, Altan Erarslan
Publikováno v:
Journal of Chemical Technology & Biotechnology. 55:79-84
Thermal inactivation kinetics of native and glutaraldehyde cross-linked forms of penicillin G acylase obtained from a mutant derivative of Escherichia coli ATCC 11105 were studied. Apparent activation energies for thermal inactivation of both native
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cc2f54df72f17125695d30713e64e01
https://doi.org/10.1002/jctb.280550113
https://doi.org/10.1002/jctb.280550113
Publikováno v:
Journal of Chemical Technology & Biotechnology. 51:27-40
A mutant strain with high penicillin G acylase activity was derived from Escherichia coli ATCC 11105 by chemical mutagenesis, using N-methyl-N′-nitro-N-nitrosoguanidine. Penicillin acylase was extracted from the mutant strain and highly purified by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f79838e500de6f61a8c5e946921cede
https://doi.org/10.1002/jctb.280510103
https://doi.org/10.1002/jctb.280510103
Publikováno v:
Journal of Industrial Microbiology & Biotechnology. 32:335-344
An extracellular serine alkaline protease of Bacillus clausii GMBAE 42 was produced in protein-rich medium in shake-flask cultures for 3 days at pH 10.5 and 37 degrees C. Highest alkaline protease activity was observed in the late stationary phase of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12b81b731d2e80cf1629574c71b007a3
https://doi.org/10.1007/s10295-005-0260-z
https://doi.org/10.1007/s10295-005-0260-z
Publikováno v:
World Journal of Microbiology and Biotechnology. 18:881-888
The stabilization of Escherichia coli penicillin G acylase (PGA) conjugated with carboxymethylcellulose (CMC) against temperature and pH was studied. The 2,3-dialdehyde derivative of CMC obtained by periodate oxidation was covalently conjugated to PG
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd78536947b0187d89162ba1ee3bc145
https://doi.org/10.1023/a:1021262826254
https://doi.org/10.1023/a:1021262826254
Publikováno v:
Biophysical Chemistry. 90:203-217
The problem, whether excited-state energy transfer occurs between Trp residues in a multi-tryptophan proteins and if it does, what kind of changes it induces in different parameters of protein fluorescence, is currently under active investigation. In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bf51ca02c60e7e41e8cb5d324e40aa1
https://doi.org/10.1016/s0301-4622(01)00141-7
https://doi.org/10.1016/s0301-4622(01)00141-7
Autor:
Altan Erarslan, Dilek Kazan
Publikováno v:
Journal of Chemical Technology & Biotechnology. 74:1157-1164
The stabilisation of Escherichia coli penicillin G acylase (PGA) by dextran polymers (of molecular weight 11.5, 37.7 and 71kDa) was studied. The inactivation of both the native and dextran-containing enzyme preparations obeyed first-order kinetics at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::93552da0bfbf5eed98da339a2ce4e356
https://doi.org/10.1002/(sici)1097-4660(199912)74:12<1157::aid-jctb165>3.0.co
https://doi.org/10.1002/(sici)1097-4660(199912)74:12<1157::aid-jctb165>3.0.co
Publikováno v:
Journal of Applied Polymer Science. 67:805-814
Crosslinked poly(N-isopropylacrylamide) (PNIPA) gels with different crosslink densities in the form of rods and beads were prepared by free-radical crosslink- ing copolymerization. Solution and inverse suspension polymerization techniques were used f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85e415391ffea47c82313b14611d2ff7
https://doi.org/10.1002/(sici)1097-4628(19980131)67:5<805::aid-app5>3.0.co
https://doi.org/10.1002/(sici)1097-4628(19980131)67:5<805::aid-app5>3.0.co