Results 11 to 20 of about 1,016,840 (120)

Exploration of Alkaliphilic Bacteria Alkalitalea saponilacus Identifies Glycoside Hydrolases With Biotechnological Potential. [PDF]

open access: yesMicrob Biotechnol
Soda lakes represent an excellent resource in the search for microbes adapted to alkaline and hypersaline conditions. In this study we demonstrate the ability of Alkalitalea saponilacus to degrade multiple carbon sources representing a promising bacterium for biotechnological applications where performance under alkaline or strongly ionic conditions is
Stephen A   +9 more
europepmc   +2 more sources

Safety evaluation of the food enzyme glucan 1,4-α-maltohydrolase from the genetically modified <i>Bacillus licheniformis</i> strain DP-Dzb115. [PDF]

open access: yesEFSA J
Abstract The food enzyme glucan 1,4‐α‐maltohydrolase (4‐α‐d‐glucan α‐maltohydrolase, EC 3.2.1.133) is produced with the genetically modified Bacillus licheniformis strain DP‐Dzb115 by Genencor International B.V. The production strain meets the requirements for the qualified presumption of safety (QPS) approach.
EFSA Panel on Food Enzymes (FEZ)   +15 more
europepmc   +2 more sources

Safety evaluation of the food enzyme glucan 1,4-alpha-glucosidase from Aspergillus niger

open access: yes, 2022
[EN] The food enzyme glucan 1,4-alpha-glucosidase (4-alpha-D-glucan glucohydrolase, EC 3.2.1.3) is produced with a non-genetically modified strain of Aspergillus niger by Beijing Shifa Technology & Trade Co., Ltd.
van Loveren, Henk   +14 more
core   +2 more sources

Safety evaluation of the food enzyme glucan 1,4 alpha-glucosidase from the genetically modified Aspergillus niger strain NZYM-BR [PDF]

open access: yes, 2022
[EN] The food enzyme glucan 1,4-alpha-glucosidase (4-alpha-D-glucan glucohydrolase, EC 3.2.1.3) is produced with the genetically modified Aspergillus niger strain NZYM-BR by Novozymes A/S.
Rivière, Gilles   +14 more
core   +1 more source

Amylosucrase as a Versatile Biocatalyst for Next-Generation Functional Ingredients: Starch Modification and Glycoside Synthesis. [PDF]

open access: yesCompr Rev Food Sci Food Saf
ABSTRACT Amylosucrase (ASase, E.C. 2.4.1.4) is a transglucosidase that catalyzes α‐glucan synthesis and transglycosylation reactions using sucrose as the sole substrate. Unlike Leloir glycosyltransferases requiring expensive nucleotide sugars, ASases utilize readily available sucrose as a cost‐effective glucose donor, offering economic advantages for ...
Seo DH, Lee BH, Yoo SH.
europepmc   +2 more sources

The SD1 locus affects primary seed dormancy in winter malting barley. [PDF]

open access: yesPlant Genome
Abstract Preharvest sprouting (PHS) resistance and seed dormancy are key targets for malting barley (Hordeum vulgare L.) in environments with a high probability of rain events at harvest. Characterization has been limited in winter malting barley compared to spring malting barley in the United States.
Kunze KH   +3 more
europepmc   +2 more sources

Safety evaluation of the food enzyme glucan 1,4-alpha-glucosidase from the genetically modified Aspergillus niger strain NZYM-BE [PDF]

open access: yes, 2022
[EN] The food enzyme glucan 1,4-alpha-glucosidase (4-alpha-D-glucan glucohydrolase EC 3.2.1.3) is produced with the genetically modified Aspergillus niger strain NZYM-BE by Novozymes A/S. The genetic modifications do not give rise to safety concerns. The
Rivière, Gilles   +14 more
core   +1 more source

Safety evaluation of the food enzyme containing endo-1,3(4)-β-glucanase, endo-1,4-β-xylanase and cellulase activities from the non-genetically modified <i>Rasamsonia emersonii</i> strain FGB. [PDF]

open access: yesEFSA J
Abstract The food enzyme containing endo‐1,3(4)‐β‐glucanase (3‐(1,3;1,4)‐β‐d‐glucan 3(4)‐glucanohydrolase; EC 3.2.1.6), endo‐1,4‐β‐xylanase (4‐β‐d‐xylan xylanohydrolase; EC 3.2.1.8) and cellulase (4‐(1,3;1,4)‐β‐d‐glucan‐4‐glucanohydrolase EC 3.2.1.4) is produced with the non‐genetically modified Rasamsonia emersonii strain FGB by DSM Food Specialties B.
EFSA Panel on Food Enzymes (FEZ)   +18 more
europepmc   +2 more sources

Degradation of Resistant α-1,4-glucan by Vaginal Gardnerella Species is Associated with Bacterial Vaginosis. [PDF]

open access: yesCurr Microbiol
This study investigates the degradation of resistant α-1,4-glucan by vaginal bacterial species, with a focus on Gardnerella spp., to elucidate its role in bacterial vaginosis (BV).
Hertzberger R   +8 more
europepmc   +2 more sources

Safety evaluation of a food enzyme with glucan 1,4-alpha-glucosidase and alpha-amylase activities from the genetically modified Aspergillus niger strain NZYM-BX

open access: yes, 2021
[EN] The food enzyme with glucan 1,4-alpha-glucosidase (EC 3.2.1.3) and alpha-amylase (EC 3.2.1.1) activities is produced with the genetically modified strain of Aspergillus niger NZYM-BX by Novozymes A/S.
Gott, David Michael   +14 more
core   +1 more source

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