Results 11 to 20 of about 54,156 (279)

Diazoacetyl Subtilisin [PDF]

Proceedings of the National Academy of Sciences, 1973
Subtilisin reacts at pH 6.8-7.8 with p -nitrophenyl diazoacetate to release p -nitrophenol and form diazoacetyl subtilisin. Although at pH 7.8 this derivative rapidly undergoes hydrolytic cleavage to regenerate active enzyme, the derivative can be trapped by rapidly lowering the pH to 5 ...
Y, Stefanovsky, F H, Westheimer
openaire   +2 more sources

PF-429242, a Subtilisin Inhibitor, Is Effective in vitro Against Leishmania infantum

Frontiers in Microbiology, 2021
PF-429242 is an inhibitor of subtilisin, an important protease found in Leishmania. However, studies regarding the effect of PF-429242 on Leishmania are scarce. In this work we evaluated the antileishmanial effect of PF-429242 against Leishmania infantum
Patrícia de Almeida Machado, Patrícia de Almeida Machado, Patrícia de Almeida Machado, Pollyanna Stephanie Gomes, Pollyanna Stephanie Gomes, Victor Midlej, Elaine Soares Coimbra, Herbert Leonel de Matos Guedes, Herbert Leonel de Matos Guedes, Herbert Leonel de Matos Guedes, Herbert Leonel de Matos Guedes   +10 more
doaj   +1 more source

Biochemical characterisation of a novel broad pH spectrum subtilisin from Fictibacillus arsenicus DSM 15822T

FEBS Open Bio, 2023
Subtilisins from microbial sources, especially from the Bacillaceae family, are of particular interest for biotechnological applications and serve the currently growing enzyme market as efficient and novel biocatalysts.
Fabian Falkenberg, Sophie Kohn, Michael Bott, Johannes Bongaerts, Petra Siegert   +4 more
doaj   +1 more source

Subtilisin of Leishmania amazonensis as Potential Druggable Target: Subcellular Localization, In Vitro Leishmanicidal Activity and Molecular Docking of PF-429242, a Subtilisin Inhibitor

Current Issues in Molecular Biology, 2022
Subtilisin proteases, found in all organisms, are enzymes important in the post-translational steps of protein processing. In Leishmania major and L. donovani, this enzyme has been described as essential to their survival; however, few compounds that ...
Pollyanna Stephanie Gomes, Monique Pacheco Duarte Carneiro, Patrícia de Almeida Machado, Valter Viana de Andrade-Neto, Alessandra Marcia da Fonseca-Martins, Amy Goundry, João Vitor Marques Pereira da Silva, Daniel Claudio Oliveira Gomes, Ana Paula Cabral de Araujo Lima, Vítor Ennes-Vidal, Ana Carolina Rennó Sodero, Salvatore Giovanni De-Simone, Herbert L. de Matos Guedes   +12 more
doaj   +1 more source

Soil Microbial Communities Involved in Proteolysis and Sulfate-Ester Hydrolysis Are More Influenced by Interannual Variability than by Crop Sequence

Agronomy, 2023
Proteases, catalysing protein hydrolysis, and arylsulfatases, catalysing sulfate-ester hydrolysis, are key microbial enzymes for N and S mineralization in soil.
Nicolas Romillac, Sophie Slezack-Deschaumes, Bernard Amiaud, Séverine Piutti   +3 more
doaj   +1 more source

Apolipoprotein F is reduced in humans with steatosis and controls plasma triglyceride‐rich lipoprotein metabolism

Hepatology, EarlyView., 2022
Hepatic APOF transcript levels correlate inversely with plasma TG and hepatic steatosis in humans. ApoF expression in mice promotes VLDL‐TG production and lipoprotein remnant clearance in mice. Abstract Background NAFLD affects nearly 25% of the global population. Cardiovascular disease (CVD) is the most common cause of death among patients with NAFLD,
Audrey Deprince, Nathalie Hennuyer, Sander Kooijman, Amanda C. M. Pronk, Eric Baugé, Viktor Lienard, An Verrijken, Eveline Dirinck, Luisa Vonghia, Eloïse Woitrain, Niels J. Kloosterhuis, Eléonore Marez, Pauline Jacquemain, Justina C. Wolters, Fanny Lalloyer, Delphine Eberlé, Sandrine Quemener, Emmanuelle Vallez, Anne Tailleux, Mostafa Kouach, Jean‐Francois Goossens, Violeta Raverdy, Bruno Derudas, Jan Albert Kuivenhoven, Mikaël Croyal, Bart van de Sluis, Sven Francque, François Pattou, Patrick C. N. Rensen, Bart Staels, Joel T. Haas   +30 more
wiley   +1 more source

Safety evaluation of the food enzyme subtilisin from the non‐genetically modified Bacillus paralicheniformis strain LMG S‐30155

EFSA Journal, 2023
The food enzyme subtilisin (serine endopeptidase, EC 3.4.21.62) is produced with the non‐genetically modified microorganism Bacillus paralicheniformis strain LMG S‐30155 by ENMEX SA de CV, now part of Kerry Food Ingredients (Cork) Ltd. The food enzyme is
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Lieve Herman, Yrjö Roos, Magdalena Andryszkiewicz, Cristina Fernàndez‐Fraguas, Yi Liu, Silvia Peluso, Andrew Chesson   +23 more
doaj   +1 more source

Safety evaluation of the food enzyme subtilisin from the non‐genetically modified Bacillus licheniformis strain NZYM‐CX

EFSA Journal, 2023
The food enzyme subtilisin (EC 3.4.21.62) is produced with the non‐genetically modified Bacillus licheniformis strain NZYM‐CX by Novozymes A/S. The production strain met the requirements for the qualified presumption of safety (QPS) approach.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Yrjö Roos, Jaime Aguilera, Magdalena Andryszkiewicz, Daniele Cavanna, Silvia Peluso, Giulio diPiazza, Francesco Pesce, Yi Liu, Andrew Chesson   +25 more
doaj   +1 more source

Production of subtilisin proteases in bacteria and yeast

Вавиловский журнал генетики и селекции, 2021
In this review, we discuss the progress in the study and modif ication of subtilisin proteases. Despite longstanding applications of microbial proteases and a large number of research papers, the search for new protease genes, the construction of ...
A. S. Rozanov, S. V. Shekhovtsov, N. V. Bogacheva, E. G. Pershina, A. V. Ryapolova, D. S. Bytyak, S. E. Peltek   +6 more
doaj   +1 more source

Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis

Frontiers in Bioengineering and Biotechnology, 2020
The cell envelope proteinase (CEP) of Lactococcus lactis is a large extracellular protease covalently linked to the peptidoglycan of the cell wall. Strains of L.
Egon Bech Hansen, Paolo Marcatili
doaj   +1 more source