Eintrag weiter verarbeiten
A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10: purification and properties
Gespeichert in:
| Veröffentlicht in: | International journal of molecular sciences 13(2012), 8, Seite 10505-10522 |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| Titel: | A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10: purification and properties/ Abdelnasser S. S. Ibrahim, Ali A. Al-Salamah, Mohamed A. El-Tayeb, Yahya B. El-Badawi and Garabed Antranikian |
| Format: | E-Book-Kapitel |
| Sprache: | Englisch |
| veröffentlicht: |
2012
|
| Gesamtaufnahme: |
: International journal of molecular sciences, 13(2012), 8, Seite 10505-10522
, volume:13 |
| Quelle: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
| LEADER | 05325caa a2200853 4500 | ||
|---|---|---|---|
| 001 | 0-89678701X | ||
| 003 | DE-627 | ||
| 005 | 20180626173759.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 170831s2012 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a urn:nbn:de:gbv:830-882w02166 |2 urn | |
| 024 | 7 | |a 10.3390%2Fijms130810505 |2 doi | |
| 024 | 7 | |a 10.15480/882.1420 |2 doi | |
| 024 | 7 | |a 11420/1423 |2 hdl | |
| 035 | |a (DE-627)89678701X | ||
| 035 | |a (DE-576)9896787018 | ||
| 035 | |a (DE-599)GBV89678701X | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rda | ||
| 041 | |a eng | ||
| 082 | 0 | |a 570: Biowissenschaften, Biologie | |
| 082 | 0 | 4 | |a 570 |
| 100 | 1 | |a Ibrahim, Abdelnasser S. S. |e VerfasserIn |0 (DE-588)1139127047 |0 (DE-627)896792765 |0 (DE-576)492929785 |4 aut | |
| 245 | 1 | 2 | |a A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10 |b purification and properties |c Abdelnasser S. S. Ibrahim, Ali A. Al-Salamah, Mohamed A. El-Tayeb, Yahya B. El-Badawi and Garabed Antranikian |
| 264 | 1 | |c 2012 | |
| 300 | |b Illustrationen | ||
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 520 | |a Screening for cyclodextrin glycosyltransferase (CGTase)-producing alkaliphilic bacteria from samples collected from hyper saline soda lakes (Wadi Natrun Valley, Egypt), resulted in isolation of potent CGTase producing alkaliphilic bacterium, termed NPST-10. 16S rDNA sequence analysis identified the isolate as Amphibacillus. CGTase was purified to homogeneity up to 22.1 fold by starch adsorption and anion exchange chromatography with a yield of 44.7%. The purified enzyme was a monomeric protein with an estimated molecular weight of 92 kDa using SDS-PAGE. Catalytic activities of the enzyme were found to be 88.8 U mg −1 protein, 20.0 U mg protein and 11.0 U mg protein for cyclization, coupling and hydrolytic activities, respectively. The enzyme was stable over a wide pH range from pH 5.0 to 11.0, with a maximal activity at pH 8.0. CGTase exhibited activity over a wide temperature range from 45 °C to 70 °C, with maximal activity at 50 °C and was stable at 30 °C to 55 °C for at least 1 h. Thermal stability of the purified enzyme could be significantly improved in the presence of CaCl and values were estimated using soluble starch as a substrate to be 1.7 ± 0.15 mg/mL and 100 ± 2.0 μmol/min, respectively. CGTase was significantly inhibited in the presence of Co, and 2-mercaptoethanol. To the best of our knowledge, this is the first report of CGTase production by Amphibacillus. The achieved high conversion of insoluble raw corn starch into cyclodextrins (67.2%) with production of mainly β-CD (86.4%), makes Amphibacillus NPST-10 desirable for the cyclodextrin production industry. | ||
| 700 | 1 | |a Al-Salamah, Ali A. |e VerfasserIn |4 aut | |
| 700 | 1 | |a El-Tayeb, Mohamed A. |e VerfasserIn |4 aut | |
| 700 | 1 | |a Elbadawi, Yahya B. |e VerfasserIn |0 (DE-588)1139127608 |0 (DE-627)896792730 |0 (DE-576)492930708 |4 aut | |
| 700 | 1 | |a Antranikian, Garabed |d 1951- |e VerfasserIn |0 (DE-588)109822382 |0 (DE-627)504156411 |0 (DE-576)289653886 |4 aut | |
| 710 | 2 | |a Technische Universität Hamburg |e Sonstige Körperschaft |0 (DE-588)1112763473 |0 (DE-627)866918418 |0 (DE-576)476770564 |4 oth | |
| 710 | 2 | |a Technische Universität Hamburg |b Institut für Technische Mikrobiologie |e Sonstige Körperschaft |0 (DE-588)113825794X |0 (DE-627)895586231 |0 (DE-576)492449171 |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |t International journal of molecular sciences |d Basel : Molecular Diversity Preservation International, 2000 |g 13(2012), 8, Seite 10505-10522 |h Online-Ressource |w (DE-627)316340715 |w (DE-600)2019364-6 |w (DE-576)281194653 |x 1422-0067 |7 nnns |
| 773 | 1 | 8 | |g volume:13 |g year:2012 |g number:8 |g pages:10505-10522 |
| 856 | 4 | 0 | |u https://doi.org/10.3390%2Fijms130810505 |x Resolving-System |3 Volltext |
| 856 | 4 | 0 | |u http://nbn-resolving.de/urn:nbn:de:gbv:830-882w02166 |x Resolving-System |z kostenfrei |3 Volltext |
| 856 | 4 | 0 | |u https://doi.org/10.15480/882.1420 |x Resolving-System |z kostenfrei |3 Volltext |
| 856 | 4 | 0 | |u http://hdl.handle.net/11420/1423 |x Resolving-System |z kostenfrei |3 Volltext |
| 935 | |i DSpace | ||
| 936 | u | w | |d 13 |j 2012 |e 8 |h 10505-10522 |
| 951 | |a AR | ||
| 856 | 4 | 0 | |u http://nbn-resolving.de/urn:nbn:de:gbv:830-882w02166 |9 LFER |
| 852 | |a LFER |z 2019-07-22T00:00:00Z | ||
| 970 | |c OD | ||
| 971 | |c EBOOK | ||
| 972 | |c EBOOK | ||
| 973 | |c Aufsatz | ||
| 935 | |a lfer | ||
| 900 | |a Ibrahim, Abdelnasser Salah Shebl | ||
| 900 | |a Elbadawi, Yahya | ||
| 900 | |a Elbadawi, Y. B. | ||
| 900 | |a El-Badawi, Yahya B. | ||
| 900 | |a Antranikian, G. | ||
| 900 | |a Antranikian, Garo | ||
| 910 | |a Hamburg University of Technology | ||
| 910 | |a Technical University | ||
| 910 | |a Hamburg | ||
| 910 | |a Université de Technologie de Hambourg | ||
| 910 | |a TU Hamburg | ||
| 910 | |a TUHH | ||
| 910 | |a University of Technology | ||
| 910 | |a Technische Universität Hamburg-Harburg | ||
| 910 | |a Institut für Technische Mikrobiologie | ||
| 910 | |a Technische Universität Hamburg | ||
| 910 | |a Institute of Technical Microbiology | ||
| 910 | |a Institute for Technical Microbiology | ||
| 910 | |a Technical Microbiology | ||
| 910 | |a V-7 | ||
| 910 | |a Studiendekanat Verfahrenstechnik | ||
| 951 | |b XB-SA | ||
| 980 | |a 89678701X |b 0 |k 89678701X |o 9896787018 |c lfer | ||
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=A+novel+cyclodextrin+glycosyltransferase+from+alkaliphilic+amphibacillus+sp.+NPST-10%3A+purification+and+properties&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rft.creator=Ibrahim%2C+Abdelnasser+S.+S.&rft.pub=&rft.format=Journal&rft.language=English&rft.issn=1422-0067 |
|---|
| _version_ | 1757992142803828736 |
|---|---|
| access_facet | Electronic Resources |
| author | Ibrahim, Abdelnasser S. S., Al-Salamah, Ali A., El-Tayeb, Mohamed A., Elbadawi, Yahya B., Antranikian, Garabed |
| author_corporate | Technische Universität Hamburg, Technische Universität Hamburg, Technische Universität Hamburg Institut für Technische Mikrobiologie, Technische Universität Hamburg Institut für Technische Mikrobiologie |
| author_corporate_role | oth, Sonstige Körperschaft, oth, Sonstige Körperschaft |
| author_facet | Ibrahim, Abdelnasser S. S., Al-Salamah, Ali A., El-Tayeb, Mohamed A., Elbadawi, Yahya B., Antranikian, Garabed, Technische Universität Hamburg, Technische Universität Hamburg, Technische Universität Hamburg Institut für Technische Mikrobiologie, Technische Universität Hamburg Institut für Technische Mikrobiologie |
| author_role | aut, aut, aut, aut, aut |
| author_sort | Ibrahim, Abdelnasser S. S. |
| author_variant | a s s i ass assi, a a a s aaa aaas, m a e t mae maet, y b e yb ybe, g a ga |
| callnumber-sort | |
| collection | lfer |
| container_reference | 13(2012), 8, Seite 10505-10522 |
| container_title | International journal of molecular sciences |
| contents | Screening for cyclodextrin glycosyltransferase (CGTase)-producing alkaliphilic bacteria from samples collected from hyper saline soda lakes (Wadi Natrun Valley, Egypt), resulted in isolation of potent CGTase producing alkaliphilic bacterium, termed NPST-10. 16S rDNA sequence analysis identified the isolate as Amphibacillus. CGTase was purified to homogeneity up to 22.1 fold by starch adsorption and anion exchange chromatography with a yield of 44.7%. The purified enzyme was a monomeric protein with an estimated molecular weight of 92 kDa using SDS-PAGE. Catalytic activities of the enzyme were found to be 88.8 U mg −1 protein, 20.0 U mg protein and 11.0 U mg protein for cyclization, coupling and hydrolytic activities, respectively. The enzyme was stable over a wide pH range from pH 5.0 to 11.0, with a maximal activity at pH 8.0. CGTase exhibited activity over a wide temperature range from 45 °C to 70 °C, with maximal activity at 50 °C and was stable at 30 °C to 55 °C for at least 1 h. Thermal stability of the purified enzyme could be significantly improved in the presence of CaCl and values were estimated using soluble starch as a substrate to be 1.7 ± 0.15 mg/mL and 100 ± 2.0 μmol/min, respectively. CGTase was significantly inhibited in the presence of Co, and 2-mercaptoethanol. To the best of our knowledge, this is the first report of CGTase production by Amphibacillus. The achieved high conversion of insoluble raw corn starch into cyclodextrins (67.2%) with production of mainly β-CD (86.4%), makes Amphibacillus NPST-10 desirable for the cyclodextrin production industry. |
| ctrlnum | (DE-627)89678701X, (DE-576)9896787018, (DE-599)GBV89678701X |
| dewey-full | 570:BIOWISSENSCHAFTEN,BIOLOGIE, 570 |
| dewey-hundreds | 500 - Science |
| dewey-ones | 570 - Life sciences; biology |
| dewey-raw | 570: Biowissenschaften, Biologie, 570 |
| dewey-search | 570: Biowissenschaften, Biologie, 570 |
| dewey-sort | 3570 BIOWISSENSCHAFTEN BIOLOGIE |
| dewey-tens | 570 - Life sciences; biology |
| doi_str_mv | 10.3390%2Fijms130810505, 10.15480/882.1420 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie, Medizin |
| fincclass_txtF_mv | science-biology |
| format | ElectronicBookComponentPart |
| format_access_txtF_mv | Article, E-Article |
| format_de105 | Ebook |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_del152 | Buch |
| format_detail_txtF_mv | text-online-monograph-child |
| format_dezi4 | e-Book |
| format_finc | Article, E-Article |
| format_legacy | ElectronicBookPart |
| format_strict_txtF_mv | E-Article |
| geogr_code | not assigned |
| geogr_code_person | Saudi Arabia |
| hierarchy_parent_id | 0-316340715 |
| hierarchy_parent_title | International journal of molecular sciences |
| hierarchy_sequence | 13(2012), 8, Seite 10505-10522 |
| hierarchy_top_id | 0-316340715 |
| hierarchy_top_title | International journal of molecular sciences |
| id | 0-89678701X |
| illustrated | Not Illustrated |
| imprint | 2012 |
| imprint_str_mv | 2012 |
| institution | DE-D117, DE-105, LFER, DE-Ch1, DE-15, DE-14, DE-Zwi2 |
| is_hierarchy_id | 0-89678701X |
| is_hierarchy_title | A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10: purification and properties |
| isil_str_mv | LFER |
| issn | 1422-0067 |
| kxp_id_str | 89678701X |
| language | English |
| last_indexed | 2023-02-16T12:52:32.969Z |
| marc024a_ct_mv | urn:nbn:de:gbv:830-882w02166, 10.3390%2Fijms130810505, 10.15480/882.1420, 11420/1423 |
| match_str | ibrahim2012anovelcyclodextringlycosyltransferasefromalkaliphilicamphibacillusspnpst10purificationandproperties |
| mega_collection | Verbunddaten SWB, Lizenzfreie Online-Ressourcen |
| misc_de105 | EBOOK |
| multipart_link | 281194653 |
| multipart_part | (281194653)13(2012), 8, Seite 10505-10522 |
| names_id_str_mv | (DE-588)1139127047, (DE-627)896792765, (DE-576)492929785, (DE-588)1139127608, (DE-627)896792730, (DE-576)492930708, (DE-588)109822382, (DE-627)504156411, (DE-576)289653886, (DE-588)1112763473, (DE-627)866918418, (DE-576)476770564, (DE-588)113825794X, (DE-627)895586231, (DE-576)492449171 |
| physical | Illustrationen |
| publishDate | 2012 |
| publishDateSort | 2012 |
| publishPlace | |
| publisher | |
| record_format | marcfinc |
| record_id | 9896787018 |
| recordtype | marcfinc |
| rvk_facet | No subject assigned |
| source_id | 0 |
| spelling | Ibrahim, Abdelnasser S. S. VerfasserIn (DE-588)1139127047 (DE-627)896792765 (DE-576)492929785 aut, A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10 purification and properties Abdelnasser S. S. Ibrahim, Ali A. Al-Salamah, Mohamed A. El-Tayeb, Yahya B. El-Badawi and Garabed Antranikian, 2012, Illustrationen, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Screening for cyclodextrin glycosyltransferase (CGTase)-producing alkaliphilic bacteria from samples collected from hyper saline soda lakes (Wadi Natrun Valley, Egypt), resulted in isolation of potent CGTase producing alkaliphilic bacterium, termed NPST-10. 16S rDNA sequence analysis identified the isolate as Amphibacillus. CGTase was purified to homogeneity up to 22.1 fold by starch adsorption and anion exchange chromatography with a yield of 44.7%. The purified enzyme was a monomeric protein with an estimated molecular weight of 92 kDa using SDS-PAGE. Catalytic activities of the enzyme were found to be 88.8 U mg −1 protein, 20.0 U mg protein and 11.0 U mg protein for cyclization, coupling and hydrolytic activities, respectively. The enzyme was stable over a wide pH range from pH 5.0 to 11.0, with a maximal activity at pH 8.0. CGTase exhibited activity over a wide temperature range from 45 °C to 70 °C, with maximal activity at 50 °C and was stable at 30 °C to 55 °C for at least 1 h. Thermal stability of the purified enzyme could be significantly improved in the presence of CaCl and values were estimated using soluble starch as a substrate to be 1.7 ± 0.15 mg/mL and 100 ± 2.0 μmol/min, respectively. CGTase was significantly inhibited in the presence of Co, and 2-mercaptoethanol. To the best of our knowledge, this is the first report of CGTase production by Amphibacillus. The achieved high conversion of insoluble raw corn starch into cyclodextrins (67.2%) with production of mainly β-CD (86.4%), makes Amphibacillus NPST-10 desirable for the cyclodextrin production industry., Al-Salamah, Ali A. VerfasserIn aut, El-Tayeb, Mohamed A. VerfasserIn aut, Elbadawi, Yahya B. VerfasserIn (DE-588)1139127608 (DE-627)896792730 (DE-576)492930708 aut, Antranikian, Garabed 1951- VerfasserIn (DE-588)109822382 (DE-627)504156411 (DE-576)289653886 aut, Technische Universität Hamburg Sonstige Körperschaft (DE-588)1112763473 (DE-627)866918418 (DE-576)476770564 oth, Technische Universität Hamburg Institut für Technische Mikrobiologie Sonstige Körperschaft (DE-588)113825794X (DE-627)895586231 (DE-576)492449171 oth, Enthalten in International journal of molecular sciences Basel : Molecular Diversity Preservation International, 2000 13(2012), 8, Seite 10505-10522 Online-Ressource (DE-627)316340715 (DE-600)2019364-6 (DE-576)281194653 1422-0067 nnns, volume:13 year:2012 number:8 pages:10505-10522, https://doi.org/10.3390%2Fijms130810505 Resolving-System Volltext, http://nbn-resolving.de/urn:nbn:de:gbv:830-882w02166 Resolving-System kostenfrei Volltext, https://doi.org/10.15480/882.1420 Resolving-System kostenfrei Volltext, http://hdl.handle.net/11420/1423 Resolving-System kostenfrei Volltext, http://nbn-resolving.de/urn:nbn:de:gbv:830-882w02166 LFER, LFER 2019-07-22T00:00:00Z |
| spellingShingle | Ibrahim, Abdelnasser S. S., Al-Salamah, Ali A., El-Tayeb, Mohamed A., Elbadawi, Yahya B., Antranikian, Garabed, A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10: purification and properties, Screening for cyclodextrin glycosyltransferase (CGTase)-producing alkaliphilic bacteria from samples collected from hyper saline soda lakes (Wadi Natrun Valley, Egypt), resulted in isolation of potent CGTase producing alkaliphilic bacterium, termed NPST-10. 16S rDNA sequence analysis identified the isolate as Amphibacillus. CGTase was purified to homogeneity up to 22.1 fold by starch adsorption and anion exchange chromatography with a yield of 44.7%. The purified enzyme was a monomeric protein with an estimated molecular weight of 92 kDa using SDS-PAGE. Catalytic activities of the enzyme were found to be 88.8 U mg −1 protein, 20.0 U mg protein and 11.0 U mg protein for cyclization, coupling and hydrolytic activities, respectively. The enzyme was stable over a wide pH range from pH 5.0 to 11.0, with a maximal activity at pH 8.0. CGTase exhibited activity over a wide temperature range from 45 °C to 70 °C, with maximal activity at 50 °C and was stable at 30 °C to 55 °C for at least 1 h. Thermal stability of the purified enzyme could be significantly improved in the presence of CaCl and values were estimated using soluble starch as a substrate to be 1.7 ± 0.15 mg/mL and 100 ± 2.0 μmol/min, respectively. CGTase was significantly inhibited in the presence of Co, and 2-mercaptoethanol. To the best of our knowledge, this is the first report of CGTase production by Amphibacillus. The achieved high conversion of insoluble raw corn starch into cyclodextrins (67.2%) with production of mainly β-CD (86.4%), makes Amphibacillus NPST-10 desirable for the cyclodextrin production industry. |
| swb_id_str | 9896787018 |
| title | A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10: purification and properties |
| title_auth | A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10 purification and properties |
| title_full | A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10 purification and properties Abdelnasser S. S. Ibrahim, Ali A. Al-Salamah, Mohamed A. El-Tayeb, Yahya B. El-Badawi and Garabed Antranikian |
| title_fullStr | A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10 purification and properties Abdelnasser S. S. Ibrahim, Ali A. Al-Salamah, Mohamed A. El-Tayeb, Yahya B. El-Badawi and Garabed Antranikian |
| title_full_unstemmed | A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10 purification and properties Abdelnasser S. S. Ibrahim, Ali A. Al-Salamah, Mohamed A. El-Tayeb, Yahya B. El-Badawi and Garabed Antranikian |
| title_in_hierarchy | A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10: purification and properties / Abdelnasser S. S. Ibrahim, Ali A. Al-Salamah, Mohamed A. El-Tayeb, Yahya B. El-Badawi and Garabed Antranikian, |
| title_short | A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10 |
| title_sort | novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp npst 10 purification and properties |
| title_sub | purification and properties |
| url | https://doi.org/10.3390%2Fijms130810505, http://nbn-resolving.de/urn:nbn:de:gbv:830-882w02166, https://doi.org/10.15480/882.1420, http://hdl.handle.net/11420/1423 |
| urn | urn:nbn:de:gbv:830-882w02166 |