Trypsin inhibitor from Dimorphandra mollis seeds: purification and properties

Macedo, Maria Lígia Rodrigues; Matos, Daniela Gaspar G. de; Machado, Olga Lima Tavares; Marangoni, Sérgio; Novello, José Camillo

doi:10.1016/s0031-9422(00)00155-2

Cited by 79 publications

(57 citation statements)

References 21 publications

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“…These results indicate that, in its native state, CpaTI has high intrinsic stability due to the presence of disulfide bridges. Its high degree of thermal stability was also similar to other trypsin inhibitors [40,45,482]. For the same reasons, the inhibitory activity of CpaTI was not sensitive to pH over the range 2-12; a similar result was reported for ACTI [39], DMTI-II [33] and PDTI [45].…”

Section: Discussionsupporting

confidence: 75%

“…The CpaTI purified here is a protein with two polypeptide chains of molecular mass of 27.6 and 5.6 kDa, as observed by SDS-PAGE (reducing and non-reducing conditions) analysis, which is similar to the molecular mass of other trypsin inhibitors [38][39][40][41][42][43][44]. The specificity of the inhibitory activity of the Fabaceae family serine proteinase inhibitors varies.…”

Section: Discussionmentioning

confidence: 90%

“…Thermal stability of CpaTI (0.2 μg μl -1 ) was tested by incubating the protein at different temperatures (37,40,50,60,70,80,90, and 100°C) for 30 min. After cooling the samples at 4°C for 10 min, the inhibitory assays against trypsin were performed.…”

Section: Thermal and Ph Stability Of Cpatimentioning

confidence: 99%

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Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Gomes

Barbosa

Macedo

et al. 2005

Plant Physiology and Biochemistry

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Section: Discussionsupporting

confidence: 75%

Section: Discussionmentioning

confidence: 90%

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Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Gomes

Barbosa

Macedo

et al. 2005

Plant Physiology and Biochemistry

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“…MALDI-TOF was calibrated using a Saquazyme calibration mixture (Applied Biosystems) consisting of bovine insulin (5,734 Da), E. coli thioredoxin (11,674 Da) and horse apomyoglobin (16,952 Da).…”

Section: Advances In Engineering Research Volume 129mentioning

confidence: 99%

Purification and characterization of Kunitz trypsin inhibitor from soybean

Gu¹,

Li²,

Song³

2017

Proceedings of the 2017 6th International Conference on Energy, Environment and Sustainable Development (ICEESD 2017)

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Abstract. In this paper, a Kunitz trypsin inhibitor from soybean meal was isolated to apparent homogeneity by a combination of phosphoric acid extraction, heat treatment, ammonium sulfate precipitation, ion exchange chromatography, affinity chromatography and gel filtration. The results showed that the specific activity of 4733 U· mg -1 and purification fold of 72.39 were obtained. The purified Kunitz trypsin inhibitor appeared a single protein band in SDS-PAGE electrophoresis. The accurate molecular mass of this inhibitor was determined as 22907.51Da by MALDI-TOF. Partial amino acid sequence of the purified protein from Edman degration showed a high degree of homology with various members of the Kunitz-inhibitor family.

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“…The reaction was allowed to proceed at 37°C for 20 min and then stopped by adding 0.2 ml of 30% (v/v) acetic acid. The resulting absorbance was read at 410 nm (Macedo et al, 2000). To evaluate the anti-trypsin activity of both the aqueous seeds-extracts (T. esculenta and S. soponaria), samples of 50 µl were used (10 µg and 17 µg of proteins respectively) in assays of serial dilutions, containing 200 mM Tris-HCl buffer, pH 8.5 and added 50 µl of trypsin bovine enzyme (0.3 mg/ml).…”

Section: Twentymentioning

confidence: 99%