ArticleJournal of protein chemistry2003
Hieronymain I, a new cysteine peptidase isolated from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae).
Article in Journal of protein chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 32 citations in OpenAlex.
- Asclepain cI, a proteolytic enzyme fromFrontiers in microbiology · 2022Article
- Antimicrobial Effect of a Proteolytic Enzyme From the Fruits ofFrontiers in nutrition · 2021Article
- Proteolytic extracts of three Bromeliaceae species as eco-compatible tools for leather industry.Environmental science and pollution research international · 2018Article
- Article
- Recombinant bromelain production in Escherichia coli: process optimization in shake flask culture by response surface methodology.AMB Express · 2012Article
- Penduliflorain I: A cysteine protease isolated from Hohenbergia penduliflora (A.Rich.) Mez (Bromeliaceae).The protein journal · 2010Article
- Purification and characterization of hieronymain III. Comparison with other proteases previously isolated from Bromelia hieronymi Mez.The protein journal · 2008Article
- Granulosain I, a cysteine protease isolated from ripe fruits of Solanum granuloso-leprosum (Solanaceae).The protein journal · 2008Article
- Purification and characterization of four new cysteine endopeptidases from fruits of Bromelia pinguin L. grown in Cuba.The protein journal · 2008Article
- Isolation and characterization of hieronymain II, another peptidase isolated from fruits of Bromelia hieronymi Mez (Bromeliaceae).The protein journal · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
A new peptidase, named hieronymain I, was purified to homogeneity from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae) by acetone fractionation followed by cation exchange chromatography (FPLC) on CM-Sepharose FF. Homogeneity of the enzyme was confirmed by mass spectroscopy (MALDI-TOF), isoelectric focusing, and SDS-PAGE. Hieronymain is a basic peptidase (pI > 9.3) and its molecular mass was 24,066 Da. Maximum proteolytic activity on casein (>90% of maximum activity) was achieved at pH 8.5-9.5. The enzyme was completely inhibited by E-64 and iodoacetic acid and activated by the addition of cysteine; these results strongly suggest that the isolated protease should be included within the cysteine group. The N-terminal sequence of hieronymain (ALPESIDWRAKGAVTEVKRQDG) was compared with 25 plant cysteine proteases that showed more than 50% of identity.
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