Results 201 to 210 of about 63,644 (328)

Characterisation of a cold‐adapted, thermostable glucokinase from psychrophilic Pseudoalteromonas sp. AS‐131 reveals how the enzyme achieves high thermal stability without loss of cold adaptation

open access: yesThe FEBS Journal, EarlyView.
We investigated glucokinase from the psychrophilic Pseudoalteromonas sp. AS‐131 (PsGK), which was isolated from the Antarctic Ocean. Biochemical studies revealed that PsGK is a cold‐adapted enzyme with high thermal stability, in contrast to general cold‐adapted enzymes, which have low thermal stability.
Akane Yato   +10 more
wiley   +1 more source

Investigation of Non-<i>Saccharomyces</i> Yeasts for Developing Unique Flavor Profiles in Nonalcoholic Mulberry Fermented Beverage. [PDF]

open access: yesInt J Food Sci
Kerdkhong C   +8 more
europepmc   +1 more source

Biocontrol of Non-Saccharomyces Yeasts in Vineyard against the Gray Mold Disease Agent Botrytis cinerea. [PDF]

open access: yesMicroorganisms, 2022
Agarbati A   +5 more
europepmc   +1 more source

Selection of Native Non-Saccharomyces Yeasts with Biocontrol Activity against Spoilage Yeasts in Order to Produce Healthy Regional Wines [PDF]

open access: gold, 2019
B. Kuchen   +5 more
openalex   +1 more source

Shikimate pathway disruption in yeast induces metabolite self‐assembly into toxic aggregates

open access: yesThe FEBS Journal, EarlyView.
In Saccharomyces cerevisiae, shikimate pathway disruption induces toxic metabolite assemblies. Deleting ARO4 plus phenylalanine (Phe) feeding causes Phenylalanine accumulation, lowers ARO3 activity, and triggers amyloid‐like fibril formation. Deleting ARO3 plus tyrosine (Tyr) feeding leads to Tyrosine buildup and similar fibril assembly.
Hanaa Adsi   +6 more
wiley   +1 more source

Selection of Non-<i>Saccharomyces</i> Yeasts from Extreme Oenological Environments for Potential Use in Winemaking. [PDF]

open access: yesMicroorganisms
Alcalá-Jiménez MT   +5 more
europepmc   +1 more source

Intrinsic specificity of a ‘core’ TIP60 acetyltransferase complex in Drosophila

open access: yesThe FEBS Journal, EarlyView.
The intrinsic substrate selectivity of the Drosophila TIP60‐core acetyltransferase was determined using synthetic nucleosome arrays. Targeted mass spectrometry revealed site‐specific acetylation of histones H2A, H2A.V, and H4, uncovering distinct acetylation rates and patterns across individual lysines.
Silke Krause   +5 more
wiley   +1 more source

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