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3.4.22.67: zingipain

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

Word Map on EC 3.4.22.67

Reaction

preferential cleavage of peptides with a proline residue at the P2 position =

Synonyms

Bgp, C01.017, cysteine proteinase GP-II, F50, ginger protease, ginger protease II, GP-II, zingibain

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.67 zingipain

Purification

Purification on EC 3.4.22.67 - zingipain

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 14.91fold from rhizomes by ammonium sulfate fractionation, tert-butanol precipitation at 25°C and pH 7.0 using the interfacial precipitateand the aqueous phase, and ultrafiltration, method optimization
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native enzyme from rhizomes by ammonium sulfate fractionation and dialysis
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native enzyme from rhizomes by ammonium sulfate fractionation, anion exchange chromatography, SDS-PAGE, and gel filtration
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native enzyme from rhizomes by saturation ammonium sulfate fractionation and anion exchange chromatography to homogeneity
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partially purified 252fold with a recovery of 61%, ion exchange chromatography
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purification via a three-phase partitioning system
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ultrasonic-assisted liquid-liquid microextraction of the proteases from ginger and sodom apple using natural deep eutectic solvents, NADES. Selective partitioning of NADES-assisted microextraction yields more protease in NADES-enriched top phase. Maximum yield is achieved with 25% (v/v) of NADES, 15% (w/v) of source concentration and ultrasound temperature and time as 35°C and 10 min, respectively
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