Results 31 to 40 of about 593 (163)

Molecular cloning of a cyclodextrin glucanotransferase gene from alkalophilic Bacillus sp. TS1-1 and characterization of the recombinant enzyme [PDF]

, 2006
A cyclodextrin glucanotransferase (CGTase) gene from Bacillus sp. TS1-1 was isolated and cloned into Escherichia coli. Starting from TTG codon, there was an open reading frame composed of 2163 bp (721 amino acids).
Abdul Rashid, Noor Aini, Hassan, Osman, Mohd Illias, Rosli, Nik Mahmood, Nik Azmi, Rahman, Kamalesh   +4 more
core   +1 more source

Comparative Study of the Cyclization Reactions of Three Bacterial Cyclomaltodextrin Glucanotransferases [PDF]

Applied and Environmental Microbiology, 2001
ABSTRACT The actions of cyclomaltodextrin glucanotransferases (CGTase; EC 2.4.1.19 ) from alkalophilic Bacillus sp. strain A2-5a (A2-5a CGTase), Bacillus macerans ( Bmac CGTase), and Bacillus stearothermophilus (
Y, Terada, H, Sanbe, T, Takaha, S, Kitahata, K, Koizumi, S, Okada   +5 more
openaire   +2 more sources

Mining for novel cyclomaltodextrin glucanotransferases unravels the carbohydrate metabolism pathway via cyclodextrins in Thermoanaerobacterales [PDF]

Scientific Reports, 2022
AbstractCarbohydrate metabolism via cyclodextrins (CM-CD) is an uncommon starch-converting pathway that thoroughly depends on extracellular cyclomaltodextrin glucanotransferases (CGTases) to transform the surrounding starch substrate to α-(1,4)-linked oligosaccharides and cyclodextrins (CDs).
Sara Centeno-Leija, Laura Espinosa-Barrera, Beatriz Velazquez-Cruz, Yair Cárdenas-Conejo, Raúl Virgen-Ortíz, Georgina Valencia-Cruz, Roberto A. Saenz, Yerli Marín-Tovar, Saúl Gómez-Manzo, Beatriz Hernández-Ochoa, Luz María Rocha-Ramirez, Rocío Zataraín-Palacios, Juan A. Osuna-Castro, Agustín López-Munguía, Hugo Serrano-Posada   +14 more
openaire   +3 more sources

Starch‐binding domain shuffling in Aspergillus niger glucoamylase [PDF]

, 2003
Aspergillus niger glucoamylase (GA) consists mainly of two forms, GAI [from the N‐terminus, catalytic domain + linker + starch‐binding domain (SBD)] and GAII (catalytic domain + linker).
Cornett, Catherine, Fang, Tsuei-Yun, Ford, Clark, Reilly, Peter, Reilly, Peter   +4 more
core   +3 more sources

Maintenance of glucose-sensitive insulin secretion of cryopreserved human islets with University of Wisconsin solution and ascorbic acid-2 glucoside [PDF]

, 2004
Normal human islet cells are an ideal source for pancreas-targeted cell therapies, but the availability of human donor pancreata for islet isolation is severely limited. To effectively utilize such scarce donor organs for cell therapies, it is crucial to
Arata, T, Fukazawa, T, Ikeda, H, Kobayashi, K, Kobayashi, N, Kosaka, Y, Lakey, JRT, Matsuoka, J, Narushima, M, Okitsu, T, Tanaka, N, Yamamoto, I, Yong, C   +12 more
core   +1 more source

Update of the list of qualified presumption of safety (QPS) recommended microbiological agents intentionally added to food or feed as notified to EFSA 19: Suitability of taxonomic units notified to EFSA until September 2023. [PDF]

EFSA J
Abstract The qualified presumption of safety (QPS) process was developed to provide a safety assessment approach for microorganisms intended for use in food or feed chains. The QPS approach is based on an assessment of published data for each taxonomic unit (TU), with respect to its taxonomic identity, the body of relevant knowledge and safety concerns.
EFSA Panel on Biological Hazards (BIOHAZ), Koutsoumanis K, Allende A, Alvarez-Ordóñez A, Bolton D, Bover-Cid S, Chemaly M, De Cesare A, Hilbert F, Lindqvist R, Nauta M, Nonno R, Peixe L, Ru G, Simmons M, Skandamis P, Suffredini E, Cocconcelli PS, Fernández Escámez PS, Prieto Maradona M, Querol A, Sijtsma L, Suarez JE, Sundh I, Barizzone F, Correia S, Herman L.   +26 more
europepmc   +2 more sources

Safety evaluation of the food enzyme mucorpepsin from the non-genetically modified Rhizomucor miehei strain M19-21. [PDF]

EFSA J
Abstract The food enzyme mucorpepsin (EC 3.4.23.23) is produced with the non‐genetically modified Rhizomucor miehei strain M19‐21 by Meito Sangyo Co., Ltd. The native enzyme can be chemically modified to produce a more thermolabile form. The food enzyme was considered free from viable cells of the production organism.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Lambré C, Barat Baviera JM, Bolognesi C, Cocconcelli PS, Crebelli R, Gott DM, Grob K, Lampi E, Mengelers M, Mortensen A, Rivière G, Steffensen IL, Tlustos C, Van Loveren H, Vernis L, Zorn H, Roos Y, Andryszkiewicz M, Fernàndez-Fraguas C, Kovalkovicova N, Liu Y, Peluso S, Chesson A.   +24 more
europepmc   +2 more sources

Combination of extrusion and cyclodextrin glucanotransferase treatment to modify wheat flours functionality [PDF]

, 2016
This research aims to vary functional properties of native and extruded wheat flours combining cyclodextrin glucanotransferase and extrusion treatments.
Durá, Ángela, Gómez, Manuel, Martínez, Mario M., Román, Laura, Rosell, Cristina M.   +4 more
core   +1 more source

Influence of culture medium pH on the production of CGTase by Bacillus firmus Strain No. 37 - doi: 10.4025/actascitechnol.v35i3.15882

Acta Scientiarum: Technology, 2013
The enzyme cyclomaltodextrin-glucanotransferase (CGTase) is a transglicosidase able to convert corn starch into cyclodextrin (CD). CDs are widely applied in industry given the ability to form inclusion complexes with a great variety of organic molecules.
Jéssica Bravin Carmello, Gisella Maria Zanin, José Eduardo Olivo   +2 more
doaj   +1 more source

Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications [PDF]

, 2009
Cyclodextrin glucanotransferases (CGTases) are industrially important enzymes that produce cyclic α-(1,4)-linked oligosaccharides (cyclodextrins) from starch. Cyclodextrin glucanotransferases are also applied as catalysts in the synthesis of glycosylated
A Avci, A Biwer, A Englbrecht, A Homann, A Nakamura, AA Markosyan, AD Blackwood, AK Schmidt, B Zhekova, BA Veen van der, BA Veen van der, BA Veen van der, BE Norman, BK Dalmia, BL Cantarel, BN Gawande, C Klein, C Klein, C Moriwaki, CL Lawson, D Li, D Penninga, D Penninga, D Vetter, DE Hill, EMM Martin Del Valle, F Binder, F Fava, G Astray, G Matioli, G Matioli, G Parsiegla, G Schmid, H Bender, H Costa, H Leemhuis, H Leemhuis, H Leemhuis, H Leemhuis, H Leemhuis, H Leemhuis, H Leemhuis, H Leemhuis, H Leemhuis, H Nakano, H Nakano, H-K Jun, Hans Leemhuis, HF Alves-Prado, HF Alves-Prado, HJ Chung, HY Chang, I Pishtiyski, J Kaulpiboon, J Szejlti, JA Rendleman Jr, JAR Gaston, JC Uitdehaag, JCM Uitdehaag, JH Shim, JH Shim, K Buchholz, K Haga, K Hirano, K Kamaruddin, K Kimura, K Ohdan, K Okada, K Rahman, K Shimoda, K Shimoda, K Shimoda, K Sin, K Sugimoto, K Yoshinaga, KA Sin, KH Park, KM Goh, L Beier, L Bornaghi, L Greffe, L Nitschke, L Szente, LR Marechal, Lubbert Dijkhuizen, M Alcalde, M Alcalde, M Faijes, M Machovic, M Pajatsch, M Takada, M Zheng, MH Kim, MH Lee, MJEC Maarel van der, MR Stam, MT Martin, MT Martin, MT Martin, MT Reetz, N Atanasova, N Doukyu, N Kitamoto, N Rashid, N Sato, OL Radu, P Itkor, P Yampayont, Q Qi, Q Qi, R Charoensakdi, R Charoensakdi, R Kanai, R Mosi, RD Wind, RE Vollu, RF Martins, RF Martins, RM Kelly, RM Kelly, RM Kelly, RM Kelly, RM Kelly, RM Ong, Ronan M. Kelly, S Fujiwara, S Jemli, S-W Jung, SA Ferrarotti, SH Lee, SH Yoon, SH Yoon, SH Yoon, SH Yoon, SK Arya, ST Jørgensen, T Hamamoto, T Kaneko, T Kaper, T Loftsson, T Takano, V Rimphanitchayakit, V Thiemann, VGH Eijsink, VT Kochikyan, W Kim, Y Hashimoto, Y Nakagawa, Y Terada, YD Lee, YH Go, YH Kim, YJ Son, Z Li, Z Li   +154 more
core   +4 more sources