Results 11 to 20 of about 3,689 (215)

Safety evaluation of the food enzyme glucose oxidase from the non-genetically modified <i>Aspergillus tubingensis</i> strain GOX. [PDF]

EFSA J
Abstract The food enzyme glucose oxidase (β‐d‐glucose: oxygen 1‐oxidoreductase, i.e. EC 1.1.3.4) is produced with the non‐genetically modified Aspergillus tubingensis strain GOX by DSM Food Specialties. The food enzyme was free from viable cells of the production organism. It is intended to be used in four food manufacturing processes. Dietary exposure
EFSA Panel on Food Enzymes (FEZ), Zorn H, Barat Baviera JM, Bolognesi C, Catania F, Gadermaier G, Greiner R, Mayo B, Mortensen A, Roos YH, Solano MLM, Sramkova M, Van Loveren H, Vernis L, Aguilera J, Andryszkiewicz M, Pesce F, Marini E, Criado A, Liu Y.   +19 more
europepmc   +4 more sources

Aspergillus tubingensis: A Rare Fungal Pathogen Complicating COVID-19 Case [PDF]

Case Reports in Infectious Diseases
Background Coronavirus disease 2019 (COVID‐19) has been associated with invasive fungal infection. Several COVID‐19 cases were complicated due to coinfection with Aspergillus, Rhizopus, and Mucor species. We present COVID‐19 with Aspergillus tubingensis coinfection.
Aiah M. Khateb, Fadwa S. Alofi, Abdullah Z. Almutairi, Mohammad A. Turkistani, Ziab Z. Alahmadey, Hessa A. Al-Sharif, Esam I. Azhar   +6 more
doaj   +3 more sources

Safety evaluation of an extension of use of the food enzyme non-reducing end α-l-arabinofuranosidase from the non-genetically modified Aspergillus tubingensis strain ARF. [PDF]

EFSA J
Abstract The food enzyme non‐reducing end α‐l‐arabinofuranosidase (α‐l‐arabinofura‑noside non‐reducing end α‐l‐arabinofuranosidase, EC 3.2.1.55) is produced with the non‐genetically modified Aspergillus tubingensis strain ARF by DSM Food Specialties B.V. A safety evaluation of this food enzyme was made previously, in which EFSA concluded that this food
EFSA Panel on Food Enzymes (FEZ), Zorn H, Barat Baviera JM, Bolognesi C, Catania F, Gadermaier G, Greiner R, Mayo B, Mortensen A, Roos YH, Solano MLM, Sramkova M, Van Loveren H, Vernis L, Sanmartín L, Liu Y.   +15 more
europepmc   +4 more sources

Efficacy of Aspergillus tubingensis GX3′ Fermentation against Meloidogyne enterolobii in Tomato (Solanum lycopersicum L.) [PDF]

Plants, 2023
Meloidogyne enterolobii is one of the most virulent root-knot nematodes (RKNs). Aspergillus tubingensis Raoul Mosseray, 1934, is used to produce bioactive substances, enzymes, and secondary metabolites.
Aatika Sikandar, Fukun Gao, Yixue Mo, Qian Chen, Rana Muhammad Kaleem Ullah, Haiyan Wu   +5 more
doaj   +2 more sources

Raw starch conversion by Saccharomyces cerevisiae expressing Aspergillus tubingensis amylases [PDF]

Biotechnology for Biofuels, 2013
Abstract Background Starch is one of the most abundant organic polysaccharides available for the production of bio-ethanol as an alternative transport fuel. Cost-effective utilisation of starch requires consolidated bioprocessing (CBP) where a single microorganism can produce the enzymes required for hydrolysis of ...
Marko Johann Viktor, Shaunita H. Rose, Willem H. van Zyl, Marinda Viljoen‐Bloom   +3 more
openalex   +5 more sources

Untargeted metabolomics and quantification analysis reveal the shift of chemical constituents between instant dark teas individually liquid-state fermented by Aspergillus cristatus, Aspergillus niger, and Aspergillus tubingensis [PDF]

Frontiers in Microbiology, 2023
Instant dark teas (IDTs) were individually liquid-state fermented using the fungi Aspergillus cristatus, Aspergillus niger, and Aspergillus tubingensis.
Si-yu Liao, Yi-qiao Zhao, Wen-bao Jia, Li Niu, Tunyaluk Bouphun, Pin-wu Li, Sheng-xiang Chen, Wei Chen, Dan-dan Tang, Yue-ling Zhao, Yao Zou, Ming-zhi Zhu, Wei Xu   +12 more
doaj   +2 more sources

Crystal structure of endo‐xylogalacturonan hydrolase from Aspergillus tubingensis [PDF]

The FEBS Journal, 2013
Endo‐xylogalacturonan hydrolase is a member of glycoside hydrolase family 28 (GH28) that hydrolyzes the glycosidic bond between two β‐xylose‐substituted galacturonic acid residues in pectin. Presented here is the X‐ray crystal structure of the endo‐xylogalacturonan hydrolase from Aspergillus tubingensis (XghA) at 1.75 Å resolution.
H.J. Rozeboom, G. Beldman, Henk A. Schols, Bauke W. Dijkstra   +3 more
openalex   +4 more sources

Identification of Aspergillus tubingensis in a primary skin infection

Journal de Mycologie Médicale, 2018
Aspergillus section Nigri comprises a group of related species that include Aspergillus niger, A. welwitschiae, A. carbonarius, A. brasiliensis and A. tubingensis. Some of these species are morphologically very similar to A. niger but exhibit different patterns of susceptibility to antifungal agents; such is the case for A. tubingensis. Therefore, when
María Guadalupe Frías‐De‐León, Einat Paz, Roberto Arenas, Carlos Atoche, Esperanza Duarte-Escalante, Dora Molina de Soschin, Gustavo Acosta‐Altamirano, M. R. Reyes-Montes   +7 more
openalex   +3 more sources

Overview and Diversity of Fungi of the Genus Aspergillus Section Nigri on Maize and Small Grains [PDF]

Foods
The presence of filamentous fungi with toxigenic ability from the Aspergillus genera is frequently found in maize kernels, and this can lead to decay and mycotoxin contamination of the kernels.
Milica Lučev, Jelena Stepanović, Vesna Kandić Raftery, Zoran Čamdzija, Ana Obradović, Milan Stevanović, Slavica Stanković   +6 more
doaj   +2 more sources

The frequency distribution of Aspergillus section Nigri from clinical and environmental samples in Iran [PDF]

BMC Microbiology
Background Aspergillus section Nigri is widely distributed in decaying plant materials in our environment. Although most of these species are known for food spoilage and some have industrial applications, some of these species, including Aspergillus ...
Sara Hamzehee, Maral Gharaghani, Seyed Hamid Borsi, Hadis Jafarian, Gholam Ali Jalaee, Maryam Kardooni, Ali Zarei-Mahmoudabadi   +6 more
doaj   +2 more sources