Phytepsin

Kervinen, Jukka

doi:10.1016/b978-0-12-382219-2.00023-5

Cited by 2 publications

(3 citation statements)

References 78 publications

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“…In contrast, pepstatin A produced a 75% inhibition of the purified AP under those same assay conditions. This last result is consistent with the well documented characteristic inhibition of phytepsins by pepstatin A (Kervinen & Wlodawer, 2013).…”

Section: Proteolytic Specificity Catalytic Mechanism and Kinetic Para...supporting

confidence: 91%

Miniature cheeses made with blends of chymosin and a vegetable rennet from flowers of Silybum marianum: Enzymatic characterization of the flower-coagulant peptidase

Colombo

Fernández

Cimino³

et al. 2018

Food Chemistry

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Section: Proteolytic Specificity Catalytic Mechanism and Kinetic Para...supporting

confidence: 91%

Miniature cheeses made with blends of chymosin and a vegetable rennet from flowers of Silybum marianum: Enzymatic characterization of the flower-coagulant peptidase

Colombo

Fernández

Cimino³

et al. 2018

Food Chemistry

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“…After the purification step, the AP was purified 13.4-fold with a recovery of 32.1% and a specific activity of 3203.3 Ucas mg -1 from the starting material using casein as protein substrate (Table 1). This protease previously named SoAP was renamed salpichroin according to Kervinen [45].…”

Section: Purification and Characterization Of The Aspartic Protease (...mentioning

confidence: 99%

“…Both autocatalytic and heterocatalytic steps are needed to activate the enzyme. This mechanism presumably depends both on the prevailing pH and on the presence of processing proteases within the particular intracellular compartment traversed by the enzyme precursor [45]. Thus, the activation process in vitro is not always complete under this condition [65].…”

Section: Sequence Analysis Of Salpichroinmentioning

confidence: 99%

Isolation and characterization of an Aspartic Protease from Salpichroa origanifolia Fruits

Rocha¹,

Obregón²,

Muñoz³

et al. 2015

PPL

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This report describes the purification of an aspartic protease (salpichroin) from ripe fruits of Salpichroa origanifolia (Solanaceae) starting with precipitation using organic solvents and anionexchange chromatography with 32.1% recovery and 13.4-fold purification. SDS-PAGE and zymograms of this enzyme showed a single band corresponding to an apparent molecular mass of approximately 32 kDa. The biochemical and kinetic characterization of the pure enzyme showed an acidic behavior with an optimal pH value around 3.0-4.5 with hemoglobin and 5.5-6.0 with casein. Salpichroin activity was inhibited by pepstatin but not by phenylmethylsulfonyl fluoride, E-64, EDTA or 1,10-phenanthroline, thus suggesting an aspartic protease behavior. Salpichroin hydrolyzed natural substrates, such as casein and hemoglobin, with high specific activity. Kinetic studies conducted with the synthetic peptide H-Pro- Thr-Glu-Phe-p-(NO2)-Phe-Arg-Leu-OH showed lower affinity (Km 494 µM) than other representative aspartic proteases. By investigating the cleavage of oxidized insulin β-chain to establish the hydrolytic specificity of salpichroin, we found six cleavage sites on the substrate of peptide bonds similar to those of chymosin. MALDI-TOF/TOF-MS of the tryptic ingel digest of salpichroin showed that the isolated protease shared homologous sequences with other plant proteases of the A1 aspartic protease family. This is the first report concerning the isolation and biochemical characterization of an aspartic protease isolated from Salpichroa origanifolia fruits.

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Phytepsin

Cited by 2 publications

References 78 publications

Miniature cheeses made with blends of chymosin and a vegetable rennet from flowers of Silybum marianum: Enzymatic characterization of the flower-coagulant peptidase

Miniature cheeses made with blends of chymosin and a vegetable rennet from flowers of Silybum marianum: Enzymatic characterization of the flower-coagulant peptidase

Isolation and characterization of an Aspartic Protease from Salpichroa origanifolia Fruits

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