Results 1 to 10 of about 576 (111)

Enzymatic Upgrading of Biomass-Derived Aldoses to Rare Deoxy Ketoses Catalyzed by Transketolase Variants. [PDF]

open access: yesChemSusChem
A sustainable, convenient, scalable, one‐step method for the two‐carbon chain elongation of cheap, biomass‐derived pentoses (l‐arabinose, and 2‐deoxy‐d‐ribose) and a hexose (l‐rhamnose) was developed to produce Cn+2 deoxy ketoses (C‐7 and C‐8) using transketolase, an enzyme catalyzing the irreversible transfer of a ketol group from an α‐ketoacid to an ...
Arbia G   +6 more
europepmc   +2 more sources

Merging Biocatalysis and Chemocatalysis in Flow: State-of-the-Art and Future Directions for Sustainable Synthesis. [PDF]

open access: yesAngew Chem Int Ed Engl
This review highlights recent advances in integrating biocatalysis and chemocatalysis in continuous flow to create streamlined, sustainable processes. It examines chemo‐enzymatic cascades combining at least one enzymatic and one chemical step, discusses challenges such as enzyme immobilization, leaching, and reactor clogging, and presents solutions ...
Siasiaridis P, Damian M, Mutti FG.
europepmc   +2 more sources

Substrate Induced Movement of the Metal Cofactor between Active and Resting State

open access: yesAngewandte Chemie, Volume 134, Issue 49, December 5, 2022., 2022
Pyruvate dependent Class II aldolases require a ketoacid to induce a metal shift from resting state to active enzyme. This occurs without alterations in the protein structure and might be a common, but to date overlooked, feature in many metalloproteins. Abstract Regulation of enzyme activity is vital for living organisms.
Stefan R. Marsden   +11 more
wiley   +2 more sources

Observations of reaction intermediates and the mechanism of aldose-ketose interconversion by D-xylose isomerase. [PDF]

open access: yesProceedings of the National Academy of Sciences, 1990
Crystallographic studies of D-xylose isomerase (D-xylose ketol-isomerase, EC 5.3.1.5) incubated to equilibrium with substrate/product mixtures of xylose and xylulose show electron density for a bound intermediate. The accumulation of this bound intermediate shows that the mechanism is a non-Michaelis type. Carrell et al. [Carrell, H. L., Glusker, J. P.,
C A, Collyer, D M, Blow
openaire   +2 more sources

Aroma and color development during the production of specialty malts: A review

open access: yesComprehensive Reviews in Food Science and Food Safety, Volume 20, Issue 5, Page 4816-4840, September 2021., 2021
Abstract Specialty malts comprise a promising field for innovative approaches concerning their potential in terms of color, aroma, and taste influence on the composition of beer and other beverages. Nevertheless, poor reproducibility of aroma and taste is a recurrent struggle between maltsters, leaving color as a practical parameter for quality control.
Raphael Prado   +2 more
wiley   +1 more source

The anoxic electrode‐driven fructose catabolism of Pseudomonas putida KT2440

open access: yesMicrobial Biotechnology, Volume 14, Issue 4, Page 1784-1796, July 2021., 2021
A new pathway was uncovered for the fructose metabolism in Pseudomonas putida KT2440 cultivated anaerobically in a bioelectrochemical system. In addition to the typical PTS transporter‐based pathway observed under aerobic condition, fructose was firstly converted to mannose by isomerization and then oxidized to mannonate by the glucose dehydrogenase ...
Anh Vu Nguyen   +3 more
wiley   +1 more source

Crystal structure of a novel homodimeric l‐ribulose 3‐epimerase from Methylomonus sp.

open access: yesFEBS Open Bio, Volume 11, Issue 6, Page 1621-1637, June 2021., 2021
d‐Allulose has potential as a low‐calorie sweetener which can suppress fat accumulation. The enzymes capable of d‐allulose production have attracted attention. Here, we report the X‐ray structure of a novel l‐ribulose 3‐epimerase from Methylomonas sp.
Hiromi Yoshida   +6 more
wiley   +1 more source

Safety evaluation of the food enzyme xylose isomerase from the genetically modified Streptomyces rubiginosus strain DP‐Pzn37

open access: yesEFSA Journal, Volume 18, Issue 1, January 2020., 2020
Abstract The food enzyme is a d‐xylose aldose‐ketose‐isomerase (EC 5.3.1.5) produced with the genetically modified Streptomyces rubiginosus strain DP‐Pzn37 by Danisco US Inc. Although the production strain contains antibiotic resistance genes, the food enzyme was shown to be free from viable cells of the production organism and its DNA. The food enzyme
EFSA Panel on Food Contact Materials   +28 more
wiley   +1 more source

ITRAQ‐Based Quantitative Proteomics Reveals the Proteome Profiles of Primary Duck Embryo Fibroblast Cells Infected with Duck Tembusu Virus

open access: yesBioMed Research International, Volume 2019, Issue 1, 2019., 2019
Outbreaks of duck Tembusu virus (DTMUV) have caused substantial economic losses in the major duck‐producing regions of China since 2010. To improve our understanding of the host cellular responses to virus infection and the pathogenesis of DTMUV infection, we applied isobaric tags for relative and absolute quantification (iTRAQ) labeling coupled with ...
Feng Hu   +9 more
wiley   +1 more source

Safety evaluation of the food enzyme glucose isomerase from Streptomyces murinus (strain NZYM‐GA)

open access: yesEFSA Journal, Volume 17, Issue 1, January 2019., 2019
Abstract The food enzyme is a glucose isomerase (d‐xylose aldose‐ketose‐isomerase; EC 5.3.1.5) produced with a non‐genetically modified Streptomyces murinus strain NZYM‐GA by Novozymes A/S. The glucose isomerase is intended only to be used in an immobilised form in glucose isomerisation for the production of high fructose syrups.
EFSA Panel on Food Contact Materials   +28 more
wiley   +1 more source

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