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Literature summary for 3.4.22.7 extracted from

  • Torres, M.J.; Natalucci, C.; Lopez, L.M.I.; Trejo, S.A.
    Insights into the hydrolytic activity of Asclepias fruticosa L. protease (2019), Biotechnol. Lett., 41, 1043-1050 .
    View publication on PubMed
Search for more literature for 3.4.22.7

Application

Application Comment Organism
additional information asclepain f is revealed as a successful enzyme for biocatalysis of protein hydrolysis processes at alkaline pH. It has a broad substrate specificity and is capable of selectively degrading the fractions of soy proteins and improving its functional properties Gomphocarpus fruticosus subsp. fruticosus

Organism

Organism UniProt Comment Textmining
Gomphocarpus fruticosus subsp. fruticosus B5BLP0 pro-asclepain f
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Source Tissue

Source Tissue Comment Organism Textmining
latex
-
 Gomphocarpus fruticosus subsp. fruticosus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the cut specificity is governed by the presence of hydrophobic residues (F, L, V) in the P2 position Gomphocarpus fruticosus subsp. fruticosus ?
-
 ?
oxidized insulin B chain + H2O 12 cut-off points Gomphocarpus fruticosus subsp. fruticosus ?
-
 ?
pGlu-Phe-Leu 4-nitroanilide + H2O
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 Gomphocarpus fruticosus subsp. fruticosus pGlu-Phe-Leu + 4-nitroaniline
-
 ?
soybean protein + H2O the enzyme is able to selectively hydrolyze soybean proteins at pH 10, employing an enzyme/substrate ratio of 0.2% (w/w). The enzymatic hydrolysis allows a strong increase in the solubility, water and oil holding capacity Gomphocarpus fruticosus subsp. fruticosus ?
-
 ?

Synonyms

Synonyms Comment Organism
asclepain f
-
 Gomphocarpus fruticosus subsp. fruticosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7 substrate: pGlu-Phe-Leu 4-nitroanilide Gomphocarpus fruticosus subsp. fruticosus