Results 1 to 10 of about 25,546 (199)

New insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina [PDF]

open access: yesBMC Evolutionary Biology, 2010
Background Subtilisin-like serine proteases play an important role in pathogenic fungi during the penetration and colonization of their hosts. In this study, we perform an evolutionary analysis of the subtilisin-like serine protease genes of subphylum ...
Zhang Ying   +9 more
doaj   +3 more sources

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

open access: yesEFSA Journal
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 safety of this food enzyme was evaluated previously and it did not give rise to safety concerns when used ...
EFSA Panel on Food Enzymes (FEZ)   +15 more
doaj   +2 more sources

Comprehensive Assessment of the Virulence Factors sub 3, sub 6 and mcpA in the Zoonotic Dermatophyte Trichophyton benhamiae Using FISH and qPCR

open access: yesJournal of Fungi, 2021
Skin infections by keratinophilic fungi are commonly referred to as dermatophytosis and represent a major health burden worldwide. Although patient numbers are on the rise, data on virulence factors, their function and kinetics are scarce. We employed an
Christina-Marie Baumbach   +5 more
doaj   +1 more source

Relevance of Nutrient-Sensing in the Pathogenesis of Trichophyton rubrum and Trichophyton interdigitale

open access: yesFrontiers in Fungal Biology, 2022
The growth and development of organisms depend on nutrient availability. Dermatophytes must sense nutrient levels and adapt to the host environment to colonize human and animal keratinized tissues.
Aline H. S. Cruz   +9 more
doaj   +1 more source

Diazoacetyl Subtilisin [PDF]

open access: yesProceedings 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

Nattokinase historical sketch on experimental and clinical evidence

open access: yesItalian Journal of Medicine, 2023
Nattokinase (NK) is a protease derived from food used mainly in the Japanese diet that has several properties. The main activity is related to improving fibrinolytic activities. Other activities have been demonstrated in the regulation of blood pressure
Pierpaolo Di Micco   +7 more
doaj   +1 more source

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

open access: yesEFSA 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)   +23 more
doaj   +1 more source

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

open access: yesFrontiers 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   +10 more
doaj   +1 more source

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

open access: yesFEBS 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   +4 more
doaj   +1 more source

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

open access: yesHepatology, 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   +30 more
wiley   +1 more source

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