Results 111 to 120 of about 63,430 (242)

DPPH‐based Antioxidant Screening and Cellulase‐assisted Hydrodistillation of Matourea azurea: Improved Essential Oil Yield and Density Functional Theory Insights Into a Rare Terpene

open access: yesChemistry &Biodiversity, EarlyView.
ABSTRACT Essential oils are rich in bioactive molecules like terpenes and phenolic compounds, but have low yields, making process efficiency crucial. Enzyme‐assisted hydrodistillation is a sustainable alternative, enhancing oil release by degrading the cell wall.
Júlio César Gonçalves de Souza   +7 more
wiley   +1 more source

Allosteric regulation of L-lactate dehydrogenase: Beyond effector-mediated tetramerization. [PDF]

open access: yesProtein Sci
Cai H   +5 more
europepmc   +1 more source

ADPglucose pyrophosphorylase’s N-terminus: Structural role in allosteric regulation [PDF]

open access: green, 2006
Clarisa Maria Bejar   +3 more
openalex   +1 more source

Hazelnut: Explorations toward the Biocatalytic Synthesis of its Aroma Precursor

open access: yesChemBioChem, EarlyView.
This article proposes a biosynthetic route for synthesizing filbertone, the principal flavor compound of hazelnut, through a multienzyme cascade. The pathway uses D‐amino acid oxidase, threonine deaminase, and a regioselective transketolase from Geobacillus stearothermophilus to produce a sustainable, natural hazelnut aroma precursor, addressing ...
Mireia Salvadó‐Pau   +3 more
wiley   +1 more source

Dynamic and structural insights into allosteric regulation on MKP5 a dual-specificity phosphatase. [PDF]

open access: yesNat Commun
Skeens E   +8 more
europepmc   +1 more source

Allosteric Regulation of Glycogen Phosphorylase by Order/Disorder Transition of the 250' and 280s Loops. [PDF]

open access: yesBiochemistry, 2023
Kish M   +7 more
europepmc   +1 more source

Activity‐Enhancing Mutations in an LmrR‐Based Artificial Metalloenzyme Destabilize the Protein Scaffold and Alter its Conformational Plasticity

open access: yesChemBioChem, EarlyView.
The protein LmrR is a versatile scaffold to design artificial metalloenzymes. Here, we show that the M8D/A92E (DE) mutations that result in a much more efficient catalyst, destabilize the protein dimerization interface and alter the conformation landscape when binding metal cofactor and substrates are shown.
Adil A. Safeer   +5 more
wiley   +1 more source

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