Results 11 to 20 of about 1,424 (153)

Updated safety evaluation of the food enzyme AMP deaminase from the non‐genetically modified Streptomyces murinus strain AE‐DNTS

open access: yesEFSA Journal, Volume 23, Issue 11, November 2025.
The food enzyme AMP deaminase (AMP aminohydrolase; EC 3.5.4.6) is produced with the non‐genetically modified Streptomyces murinus strain AE‐DNTS by Amano Enzyme Inc. In a previous evaluation, the Panel could not conclude on the safety of this food enzyme
Holger Zorn   +13 more
semanticscholar   +2 more sources

Safety evaluation of an extension of use of the food enzyme leucyl aminopeptidase from the non‐genetically modified Lichtheimia ramosa strain AE‐PER

open access: yesEFSA Journal, Volume 23, Issue 12, December 2025.
The food enzyme leucyl aminopeptidase (AMP aminohydrolase; EC 3.4.11.1) is produced with the non‐genetically modified Lichtheimia ramosa strain AE‐PER by Amano Enzyme Inc.
Holger Zorn   +13 more
semanticscholar   +2 more sources

Safety evaluation of the food enzyme AMP deaminase from the non‐genetically modified Aspergillus pallidofulvus strain AE‐DN

open access: yesEFSA Journal, Volume 23, Issue 7, July 2025.
The food enzyme AMP deaminase (AMP aminohydrolase; EC 3.5.4.6) is produced with the non‐genetically modified Aspergillus pallidofulvus strain AE‐DN by Amano Enzyme Inc. The food enzyme was free from viable cells of the production organism. It is intended
Holger Zorn   +16 more
semanticscholar   +2 more sources

Safety evaluation of the food enzyme AMP deaminase from non‐genetically modified Aspergillus sp. strain DEA 56‐111

open access: yesEFSA Journal, Volume 22, Issue 4, April 2024.
The food enzyme AMP deaminase (AMP aminohydrolase; EC 3.5.4.6) is produced with the non‐genetically modified microorganism Aspergillus sp. strain DEA 56‐111 by Shin Nihon Chemical Co., Ltd.
C. Lambré   +23 more
semanticscholar   +2 more sources

Physiology of trans‐translation deficiency in Bacillus subtilis – a comparative proteomics study

open access: yesPROTEOMICS, Volume 23, Issue 18, September 2023., 2023
Abstract trans‐Translation is the most effective ribosome rescue system known in bacteria. While it is essential in some bacteria, Bacillus subtilis possesses two additional alternative ribosome rescue mechanisms that require the proteins BrfA or RqcH. To investigate the physiology of trans‐translation deficiency in the model organism B.
Melissa Vázquez‐Hernández   +3 more
wiley   +1 more source

The Arabidopsis thaliana Isogene NIT4 and Its Orthologs in Tobacco Encode β-Cyano-l-alanine Hydratase/Nitrilase*

open access: yesJournal of Biological Chemistry, 2001
Nitrilases (nitrile aminohydrolases, EC 3.5.5.1) are enzymes that catalyze the hydrolysis of nitriles to the corresponding carbon acids. Among the four known nitrilases ofArabidopsis thaliana, the isoform NIT4 is the most divergent one, and homologs of ...
M. Piotrowski   +2 more
semanticscholar   +1 more source

Streptococcus pyogenes Ser/Thr Kinase-regulated Cell Wall Hydrolase Is a Cell Division Plane-recognizing and Chain-forming Virulence Factor*

open access: yesJournal of Biological Chemistry, 2010
Cell division and cell wall synthesis are closely linked complex phenomena and play a crucial role in the maintenance and regulation of bacterial virulence. Eukaryotic-type Ser/Thr kinases reported in prokaryotes, including that in group A Streptococcus (
V. Pancholi, G. Boël, Hong Jin
semanticscholar   +1 more source

Safety evaluation of the food enzyme AMP deaminase from the non‐genetically modified Streptomyces murinus strain AE‐DNTS

open access: yesEFSA journal. European Food Safety Authority, 2023
The food enzyme AMP deaminase (AMP aminohydrolase; EC 3.5.4.6) is produced with the non‐genetically modified Streptomyces murinus strain AE‐DNTS by Amano Enzyme Inc. The food enzyme is free from viable cells. It is intended to be used in yeast processing
C. Lambré   +22 more
semanticscholar   +1 more source

Immobilization and Characterization of L-Asparaginase over Carbon Xerogels

open access: yesBioTech, 2022
L-asparaginase (ASNase) is an aminohydrolase currently used in the pharmaceutical and food industries. Enzyme immobilization is an exciting option for both applications, allowing for a more straightforward recovery and increased stability.
Rita A. M. Barros   +8 more
semanticscholar   +1 more source

Substrate promiscuity of the Escherichia coli xanthine oxidase

open access: yesbioRxiv, 2023
PpnN is a cytosolic nucleosidase that cleaves nucleotide monophosphates to nucleobases and ribose-5-phosphate and plays a crucial role in regulating bacterial competitive fitness and persistence. To quantify the PpnN reaction, here we developed an enzyme-
Kristina Kronborg, Y. E. Zhang
semanticscholar   +1 more source

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