Results 1 to 10 of about 771 (98)

Regulating Pathways of Bacillus pumilus Adamalysin-like Metalloendopeptidase Expression [PDF]

open access: yesInternational Journal of Molecular Sciences, 2023
The minor secreted proteinase of B. pumilus 3-19 MprBp classified as the unique bacillary adamalysin-like enzyme of the metzincin clan. The functional role of this metalloproteinase in the bacilli cells is not clear. Analysis of the regulatory region of the mprBp gene showed the presence of potential binding sites to the transcription regulatory ...
Natalia L. Rudakova   +4 more
openaire   +3 more sources

Molecular Docking and In Vitro Studies of Ochratoxin A (OTA) Biodetoxification Testing Three Endopeptidases [PDF]

open access: yesMolecules, 2023
Ochratoxin A (OTA) is considered one of the main mycotoxins responsible for health problems and considerable economic losses in the feed industry.
Pablo César Orozco-Cortés   +4 more
doaj   +2 more sources

Genomic Characterization of a Halovirus Representing a Novel Siphoviral Cluster [PDF]

open access: yesViruses, 2023
Salt mines are a special type of hypersaline environment. Current research mainly focuses on prokaryotes, and the understanding of viruses in salt mines remains limited.
Kaixin Diao   +5 more
doaj   +2 more sources

Safety evaluation of the food enzyme bacillolysin from the non‐genetically modified Bacillus amyloliquefaciens strain GNP [PDF]

open access: yesEFSA Journal, 2023
The food enzyme bacillolysin (EC 3.4.24.28) is produced with the non‐genetically modified Bacillus amyloliquefaciens strain GNP by DSM Food Specialties B.V.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +23 more
doaj   +2 more sources

Safety evaluation of the food enzyme bacillolysin from the non‐genetically modified Bacillus amyloliquefaciens strain AGS 430 [PDF]

open access: yesEFSA Journal, 2023
The food enzyme bacillolysin (EC 3.4.24.28) is produced with the non‐genetically modified Bacillus amyloliquefaciens strain AGS 430 by Kerry Ingredients & Flavours Ltd.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +23 more
doaj   +2 more sources

Safety evaluation of the food enzyme bacillolysin from the non‐genetically modified Bacillus amyloliquefaciens strain HPN 131 [PDF]

open access: yesEFSA Journal, 2023
The food enzyme bacillolysin (EC 3.4.24.28) is produced with the non‐genetically modified Bacillus amyloliquefaciens strain HPN 131 by ENMEX SA de CV.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +23 more
doaj   +2 more sources

Safety evaluation of the food enzyme bacillolysin from the non‐genetically modified Bacillus amyloliquefaciens strain NZYM‐NB [PDF]

open access: yesEFSA Journal
The food enzyme bacillolysin (EC 3.4.24.28) is produced with the non‐genetically modified Bacillus amyloliquefaciens strain NZYM‐NB by Novozymes A/S.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +24 more
doaj   +2 more sources

Features of gene expression of Bacillus pumilus metalloendopeptidase [PDF]

open access: yesBiochemistry (Moscow), 2016
Features of gene expression of the secreted Bacillus pumilus metalloendopeptidase belonging to the adamalysin/reprolysin family were investigated. In the regulatory region of the gene, we identified hypothetical binding sites for transcription factors CcpA and TnrA.
Rudakova N.   +4 more
openaire   +6 more sources

Safety evaluation of the food enzyme bacillolysin from the non‐genetically modified Bacillus amyloliquefaciens strain AE‐NP [PDF]

open access: yesEFSA Journal
The food enzyme bacillolysin (EC 3.4.24.28) is produced with the non‐genetically modified Bacillus amyloliquefaciens strain AE‐NP by Amano Enzyme Inc. The production strain meets the requirements for the qualified presumption of safety (QPS) approach to ...
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +22 more
doaj   +2 more sources

Production and application of peptidyl-lys metalloendopeptidase: advances, challenges, and future perspectives. [PDF]

open access: yesAppl Microbiol Biotechnol
Peptidyl-lys metalloendopeptidases (PKMs) are enzymes that selectively cleave peptide bonds at the N-terminus of lysine residues present in the P1′ position, making them valuable tools in proteomics.
Ahmed U, Ochsenreither K, Eisele T.
europepmc   +3 more sources

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