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3.4.22.2: papain

This is an abbreviated version!
For detailed information about papain, go to the full flat file.

Word Map on EC 3.4.22.2

Reaction

Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1' =

Synonyms

Adolph's Meat Tenderizer, arbuz, CpXCP5, EC 3.4.4.10, enzeco papain, papain, papain-like cysteine protease, papain-like protease, papaine, papaya peptidase I, papaya proteinase 1, Papaya proteinase I, papayotin, PLCP, PLpro, PPI, summetrin, velardon

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.2 papain

Organic Solvent Stability

Organic Solvent Stability on EC 3.4.22.2 - papain

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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetonitrile
-
papain retains almost all its catalytic activity after 24 h of incubation in the presence of 99% (v/v) acetonitrile with a more compact conformation
dimethyl formamide
-
papain shows a complete inactivation after 24 h when exposed to those media containing 90% (v/v) dimethyl formamide because of an irreversible conformational change
Ethanol
12% (v/v), 4°C, pH 3.2, 530 h, about 90% loss of activity
Glycerol
-
in the presence of 20% (v/v) glycerol the enzyme retains nearly 80% of its activity even after heating at 75°C for 40 min and it retains almost 70% of its activity even after heating for 80 min, at 30% (v/v) glycerol the enzyme retains nearly 80 and 65% of its activity after heating for 40 and 80 min, respectively at 75°C
hexadecyltrimethyl ammonium bromide
-
the presence of hexadecyltrimethyl ammonium bromide allows 41% recovery of enzymatic activity of acid-unfolded papain in the presence of hexadecyltrimethyl ammonium bromide the enzyme exists as a compact intermediate with regain of native-like secondary and partial tertiary structure as well as high 8-anilino-1-naphthalene-sulfonic acid binding with the partially recovered enzymatic activity
Methanol
-
papain shows 80% loss of activity after 24 h incubation in 90% (v/v) methanol although no global conformational change and minor secondary structure rearrangements are detected
SDS
-
the presence of SDS allows 43% recovery of enzymatic activity of acid-unfolded papain, addition of 8 mM SDS results in the loss of 8-anilino-1-naphthalene-sulfonic acid binding sites exhibited by a decrease in 8-anilino-1-naphthalene-sulfonic acid fluorescence intensity, suggesting the burial of hydrophobic patches, papain at low pH and in the presence of SDS exists in a partially folded state characterized by native-like secondary structure and tertiary folds
tetrahydrofuran
-
30%, inactivation within 30 min. Sugars protect papain from tetrahydrofuran-induced inactivation in the decreasing order D-ribose, D-fructose, D-glucose, D-saccharose, D-raffinose. D-ribose at 1.6 mol per l is the most effective stabiliser. In 60% tetrahydrofuran in the presence of ribose, papain preserves about 55% of its initial activity after 2 h
Tween
-
the presence of Tween-20 allows 39% recovery of enzymatic activity of acid-unfolded papain in the presence of Tween-20, acid-unfolded papain exists as a compact intermediate with molten-globule-like characteristics