Safety evaluation of an extension of use of the food enzyme leucyl aminopeptidase from the genetically modified Aspergillus oryzae strain NZYM‐BU [PDF]
EFSA JournalThe food enzyme leucyl aminopeptidase (EC 3.4.11.1) is produced with the genetically modified Aspergillus oryzae strain NZYM‐BU by Novozymes A/S. The safety of this food enzyme was evaluated previously, and it did not give rise to safety concerns when ...
EFSA Panel on Food Enzymes (FEZ) +15 more
doaj +3 more sources
Safety evaluation of a food enzyme containing carboxypeptidase C, oryzin and leucyl aminopeptidase activities from the non‐genetically modified Aspergillus sp. strain FP 12‐385 [PDF]
EFSA JournalThe food enzyme containing carboxypeptidase C (EC 3.4.16.5), oryzin (EC 3.4.21.63) and leucyl aminopeptidase (EC 3.4.11.1) activities is produced with the non‐genetically modified Aspergillus sp. strain FP 12‐385 by Shin Nihon Chemical Co., Ltd. The food
EFSA Panel on Food Enzymes (FEZ) +21 more
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Safety evaluation of a food enzyme containing leucyl aminopeptidase and Xaa‐Pro dipeptidyl‐peptidase activities from the non‐genetically modified Aspergillus sp. strain DAP 19‐109 [PDF]
EFSA JournalThe food enzyme containing leucyl aminopeptidase (EC 3.4.11.1) and Xaa‐Pro dipeptidyl‐peptidase (EC 3.4.14.11) activities is produced with the non‐genetically modified Aspergillus sp. strain DAP 19‐109 by Shin Nihon Chemical Co., Ltd. The food enzyme was
EFSA Panel on Food Enzymes (FEZ) +20 more
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Safety evaluation of the food enzyme containing metalloendopeptidase and leucyl aminopeptidase activities from the non‐genetically modified Aspergillus oryzae strain HBI‐POP01 [PDF]
EFSA JournalThe food enzyme containing metalloendopeptidase (EC 3.4.24) and leucyl aminopeptidase (EC 3.4.11.1) activities is produced with the non‐genetically modified Aspergillus oryzae strain HBI‐POP01 by HBI Enzymes Inc.
EFSA Panel on Food Enzymes (FEZ) +19 more
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Safety evaluation of a food enzyme containing leucyl aminopeptidase, oryzin and aspergillopepsin I from the non‐genetically modified Aspergillus sp. strain AE‐PR [PDF]
EFSA JournalThe food enzyme containing leucyl aminopeptidase (EC 3.4.11.1), oryzin (EC 3.4.21.63) and aspergillopepsin I (EC 3.4.23.18) activities is produced with the non‐genetically modified Aspergillus sp. strain AE‐PR by Amano Enzyme Inc.
EFSA Panel on Food Enzymes (FEZ) +17 more
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Cloning, Purification and Preliminary Crystallographic Analysis of the Helicobacter pylori Leucyl Aminopeptidase–Bestatin Complex [PDF]
Acta Crystallographica Section F: Structural Biology Communications, 2013 Cloning, purification and preliminary crystallographic analysis of the Helicobacter pylori leucyl aminopeptidase-bestatin ...
Anna Roujeinikova, Joyanta K Modak
exaly +3 more sources
New role for leucyl aminopeptidase in glutathione turnover. [PDF]
Biochem J, 2004 A manganese-dependent cysteinyl-glycine hydrolysing activity has been purified to electrophoretic homogeneity from bovine lens. The characterization of the purified enzyme (molecular mass of the native protein, molecular mass of the subunit and extensive primary structure analysis) allowed the unequivocal attribution of the cysteinyl-glycine ...
Cappiello M +9 more
europepmc +8 more sources
Overexpression of Leucyl Aminopeptidase in Plasmodium falciparum Parasites [PDF]
Journal of Biological Chemistry, 2006 Malaria aminopeptidases are important in the generation and regulation of free amino acids that are used in protein anabolism and for maintaining osmotic stability within the infected erythrocyte. The intraerythrocytic development of malaria parasites is
Donald L. Gardiner +4 more
openaire +3 more sources
, 2004 This chapter examines the structural chemistry and the biological aspects of Leucyl aminopeptidase PepA. A heat-stable aminopeptidase with similar biochemical properties to eukaryotic leucine aminopeptidase was purified to homogeneity from Escherichia ...
Colloms, Sean D., Sean D. Colloms
openaire +2 more sources
Purification and partial characterization of Phaseolus vulgaris seed aminopeptidase [PDF]
Brazilian Journal of Medical and Biological Research, 1999 The aminopeptidase activity of Phaseolus vulgaris seeds was measured using L-Leu-p-nitroanilide and the L-aminoacyl-ß-naphthylamides of Leu, Ala, Arg and Met.
A.P. Abdala +3 more
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