Dubiumin, a chymotrypsin-like serine protease from the seeds of Solanum dubium Fresen
Abstract
A serine protease was purified 6.7-fold and with 35% recovery from the seeds Solanum dubium Fresen by a simple purification procedure that combined ammonium sulfate fractionation, cation exchange and gel filtration chromatographies. The enzyme, named dubiumin, has a molecular mass of 66kDa as estimated by gel filtration and SDS-PAGE. Carbohydrate staining established the existence of a carbohydrate moiety attached to the enzyme. Inhibition of enzyme activity by serine protease inhibitors such as PMSF and chymostatin indicated that the enzyme belongs to the chymotrypsin-like serine protease class. Dubiumin is a basic protein with pI value of 9.3, acts optimally at pH 11.0, and is stable over a wide range of pH (3.0-12.0). The enzyme is also thermostable retaining complete activity at 60 degrees C after 1h and acts optimally at 70 degrees C for 30 min. Furthermore, it is highly stable in the presence of various denaturants (2.0% SDS, 7.0M urea and 3.0M guanidine hydrochloride) and organic solvents [CH(3)CN-H(2)O (1:1, v/v) and MeOH-H(2)O (1:1, v/v)] when incubated for 1h. The enzyme showed a high resistance to autodigestion even at low concentrations.
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Dubiumin was purified from the seeds of Solanum dubium, having a molecular mass of 66 kDa.
“Dubiumin was purified from the seeds of Solanum dubium, having a molecular mass of 66 kDa (Ahmed et al. 2009b).”
From Plant proteases as milk-clotting enzymes in cheesemaking: a review (2014) · cites this paper as Ahmed et al. 2009b
Dubiumin is a serine protease isolated from Solanum dubium seeds.
“A serine protease named dubiumin, isolated from Solanum dubium seeds, having pI value of 9.3 and optimum pH 11.0 worked efficiently under different salts concentration and at different pH levels.”
From Plant proteases as milk-clotting enzymes in cheesemaking: a review (2014) · cites this paper as Ahmed et al. 2009b
Dubiumin is highly stable in the presence of various denaturants and organic solvents.
“Furthermore, it is highly stable in the presence of various denaturants and organic solvents (Ahmed et al. 2009b).”
From Plant proteases as milk-clotting enzymes in cheesemaking: a review (2014) · cites this paper as Ahmed et al. 2009b
Dubiumin acts optimally at 70 °C for 30 min.
“It is also thermostable retaining complete activity at 60 °C after 1 h and acts optimally at 70 °C for 30 min.”
From Plant proteases as milk-clotting enzymes in cheesemaking: a review (2014) · cites this paper as Ahmed et al. 2009b
Dubiumin hydrolyzes casein fractions in separate forms or in whole casein form very efficiently at different conditions.
“It hydrolyzes casein fractions in separate forms or in a whole casein form very efficiently at different conditions.”
From Plant proteases as milk-clotting enzymes in cheesemaking: a review (2014) · cites this paper as Ahmed et al. 2009b
Dubiumin has an optimum pH of 11.0.
“A serine protease named dubiumin, isolated from Solanum dubium seeds, having pI value of 9.3 and optimum pH 11.0 worked efficiently under different salts concentration and at different pH levels.”
From Plant proteases as milk-clotting enzymes in cheesemaking: a review (2014) · cites this paper as Ahmed et al. 2009b
Dubiumin works efficiently under different salt concentrations and at different pH levels.
“A serine protease named dubiumin, isolated from Solanum dubium seeds, having pI value of 9.3 and optimum pH 11.0 worked efficiently under different salts concentration and at different pH levels.”
From Plant proteases as milk-clotting enzymes in cheesemaking: a review (2014) · cites this paper as Ahmed et al. 2009b
Dubiumin is thermostable, retaining complete activity at 60 °C after 1 h.
“It is also thermostable retaining complete activity at 60 °C after 1 h and acts optimally at 70 °C for 30 min.”
From Plant proteases as milk-clotting enzymes in cheesemaking: a review (2014) · cites this paper as Ahmed et al. 2009b
Dubiumin has a pI of 9.3.
“A serine protease named dubiumin, isolated from Solanum dubium seeds, having pI value of 9.3 and optimum pH 11.0 worked efficiently under different salts concentration and at different pH levels.”
From Plant proteases as milk-clotting enzymes in cheesemaking: a review (2014) · cites this paper as Ahmed et al. 2009b
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References 47 · Cited by 71
- Authors
- Mohamed Ahmed, I. A., Morishima, I., Babiker, E. E., & Mori, N.
- Affiliations
- Tottori University (JP)
- Corresponding author
- Mori, Nobuhiro
- Venue
- Phytochemistry
- Publisher
- Elsevier BV
- Published
- 2009-03
- Volume
- 70
- Issue
- 4
- Pages
- 483-491
- ISSN
- 0031-9422 (ISSN-L)
- OpenAlex
- W1977184427
- Cited by
- 71
- References
- 47
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 4 · 2023: 2 · 2022: 5 · 2021: 1 · 2019: 6 · 2018: 9 · 2017: 5 · 2016: 2 · 2015: 2 · 2014: 4 · 2013: 2 · 2012: 6
- FWCI
- 5.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Phytochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Pineapple and bromelain studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- chymotrypsin-like serine protease, seed proteins, enzyme purification, thermal stability, carbohydrate moiety, basic proteins
- MeSH terms
- Animals, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Enzyme Stability, Chemical Fractionation, Hydrogen-Ion Concentration, Milk, Plant Proteins, Protease Inhibitors, Protein Denaturation, Seeds, Solvents, Temperature, Sequence Analysis, Protein, Solanum, Chymases
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