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Literature summary extracted from

  • Wang, K.; Tian, Y.; Zhou, N.; Liu, D.; Zhang, D.
    Studies on fermentation optimization, stability and application of prolyl aminopeptidase from Bacillus subtilis (2018), Process Biochem., 74, 10-20 .
No PubMed abstract available

Application

EC Number Application Comment Organism
3.4.11.5 food industry Aspergillus oryzae enzyme PAP together with alkaline protease and leucine aminopeptidase is used to hydrolyze rice protein. The amount of hydrophobic amino acids is significantly increased, which contributes to a reduction in the bitterness Aspergillus oryzae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.5 gene pap, recombinant expression of His-tagged Pap in Bacillus subtilis strain WB600, for cell culture, batch fermentation conditions, including the agitation speed, pH and temperature, are systematically optimized based on a kinetic analysis, method optimization, overview. The yield of PAP reaches 174.8 U/ml under the optimized conditions, which is 1.66 times higher than that of the original production Aspergillus oryzae

Protein Variants

EC Number Protein Variants Comment Organism
3.4.11.5 additional information recombinant expression of enzyme Pap in Bacillus subtilis strain WB600. For cell culture, batch fermentation conditions, including the agitation speed, pH and temperature, are systematically optimized based on a kinetic analysis, fermentation kinetics, method optimization, overview. The yield of PAP reaches 174.8 U/ml under the optimized conditions, which is 1.66 times higher than that of the original production. The structure and storage stability of the lyophilized enzyme are significantly increased when protectants are added, and PAP together with alkaline protease and leucine aminopeptidase is used to hydrolyze rice protein. The amount of hydrophobic amino acids is significantly increased, which contributes to a reduction in the bitterness Aspergillus oryzae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.11.5 additional information Aspergillus oryzae hydrolysis of reice protein by wild-type and mutant enzymes ?
-
?
3.4.11.5 additional information Aspergillus oryzae JN-412 hydrolysis of reice protein by wild-type and mutant enzymes ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.5 Aspergillus oryzae W8GG09
-
-
3.4.11.5 Aspergillus oryzae JN-412 W8GG09
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.5 L-proline-4-nitroanilide + H2O
-
Aspergillus oryzae L-proline + 4-nitroaniline
-
?
3.4.11.5 L-proline-4-nitroanilide + H2O
-
Aspergillus oryzae JN-412 L-proline + 4-nitroaniline
-
?
3.4.11.5 additional information hydrolysis of reice protein by wild-type and mutant enzymes Aspergillus oryzae ?
-
?
3.4.11.5 additional information hydrolysis of reice protein by wild-type and mutant enzymes Aspergillus oryzae JN-412 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.11.5 More secondary structure analysis of PAP, overview Aspergillus oryzae

Synonyms

EC Number Synonyms Comment Organism
3.4.11.5 PAP
-
Aspergillus oryzae
3.4.11.5 Prolyl aminopeptidase
-
Aspergillus oryzae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.11.5 50
-
recombinant enzyme Aspergillus oryzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.5 7.5
-
recombinant enzyme Aspergillus oryzae