Extraction, purification and properties of trypsin inhibitor from Thai mung bean (Vigna radiata (L.) R. Wilczek)

Klomklao, Sappasith; Benjakul, Soottawat; Kishimura, Hideki; Chaijan, Manat

doi:10.1016/j.foodchem.2011.05.029

Cited by 54 publications

(53 citation statements)

References 22 publications

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“…Such families differ from each other in mass, cysteine content and number of reative sites. The Bowman-Birk type inhibitor has a lower molecular weight (6 to 9 kDa), whereas the Kunitz type are proteins of a molecular weight above 20 kDa (Klomklao et al 2011, Kumar & Gowda 2013.…”

Section: Discussionmentioning

confidence: 99%

“…Studies have indicated that there is a relationship between the families of proteolytic inhibitors found in legume seeds and the development degree of these plants, where tropical species, for example, Kunitz-type inhibitors are mainly found in basal subfamilies, Caesalpinioideae and Mimosoideae, while the Bowman-Birk inhibitors are more frequent in the derived subfamily, the Faboideae (Norioka et al 1988, Oliveira et al 2007, Bhattacharyya & Babu 2009, Klomklao et al 2011.…”

Section: Discussionmentioning

confidence: 99%

“…Furthemore, those molecules as a source of sulfur amino acids, and/or have been associated with defense against insect and pathogen attack (Klomklao et al 2011, Martínez et al 2012, Praxedes-Garcia et al 2012.…”

Section: Introductionmentioning

confidence: 99%

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Partial purification of trypsin inhibitors from Parkia seeds (Fabaceae)

Chevreuil

Gonçalves

Calderon³

et al. 2014

Hoehnea

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-(Partial purification of trypsin inhibitors from Parkia seeds (Fabaceae)). Leguminous seeds (Fabaceae) have a high content of inhibitors of which serine protease inhibitors are the most widely studied. However, there are only a few studies related to the investigation of these proteins in tree species belonging to the Amazon flora. The protein content presented in seeds of four Amazonian Leguminosae species, Parkia pendula, P. discolor, P. multijuga and P. Nitida, was extracted by using NaCl 0.15 mol L -1 and then partially fractionated by using affinity chromatography performed on a trypsinSepharose 4B. These inhibitors presented different affinities between trypsin and chymotrypsin serine proteases, showing a higher inhibition to trypsin compared to chymotrypsin, except for P. nitida, which showed high inhibition against both enzymes. The SDS-PAGE analysis showed that the species from Parkia genus have a main band corresponding to partially purified trypsin inhibitors. The apparent molecular mass inhibitors (approximately 13-18 kDa) and the high specificity for trypsin suggest the occurrence of Bowman-Birk and Kunitz type inhibitors. Keywords: Amazonia, Bowman-Birk inhibitor, Kunitz inhibitor, leguminous seeds, serine protease RESUMO -(Purificação parcial de inibidores de tripsina de sementes de Parkia (Fabaceae)). Sementes de leguminosas (Fabaceae) apresentam alto conteúdo de inibidores, incluindo os inibidores de serinoproteinases que têm sido extensivamente estudados. Todavia, poucos estudos foram realizados quanto à investigação dessas proteínas em espécies arbóreas pertencentes à flora amazônica. As proteínas presentes nas sementes de quatro espécies de leguminosas da Amazônia, Parkia pendula, P. discolor, P. multijuga e P. nitida, foram obtidas pela extração usando NaCl 0.15 mol L -1 e, parcialmente purificadas usando a cromatografia de afinidade em tripsina-Sepharose 4B. Os inibidores exibiram afinidades diferentes entre a tripsina e a quimotripsina, exceto para P. nitida, a qual apresentou alta inibição contra as duas enzimas. A análise em SDS-PAGE mostrou que as espécies do gênero Parkia contém uma banda principal correspondendo aos inibidores de tripsina parcialmente purificados. As massas moleculares aparentes determinadas para os inibidores (aproximadamente, 13 a 18 kDa) e a alta especificidade pela tripsina sugerem a ocorrência de inibidores do tipo Bowman-Birk e Kunitz. Palavras-chave: Amazônia, Inibidor Bowman-Birk, Inibidor Kunitz, sementes de leguminosas, serinoproteinase 1.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Partial purification of trypsin inhibitors from Parkia seeds (Fabaceae)

Chevreuil

Gonçalves

Calderon³

et al. 2014

Hoehnea

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“…Different extracting solvent including distilled water, 0.1M NaCl, 0.15M NaCl, 0.30M NaCl, 0.01M NaOH and 0.02M NaOH were used to extract protease inhibitor according Klomklao et al (2011). The seed flour was added to the medium at a ratio of solvent mass to feed mass of 5:1 (S/F) and shaken for 1h at 150rpm at room temperature.…”

Section: Effect Of Extraction Media On Trypsin Inhibitor Extractionmentioning

confidence: 99%

Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds

Pesoti

Oliveira

et al. 2015

Food Sci. Technol

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A novel trypsin inhibitor of protease (CqTI) was purified from Chenopodium quinoa seeds. The optimal extracting solvent was 0.1M NaCl pH 6.8 (p < 0.05). The extraction time of 5h and 90 °C was optimum for the recovery of the trypsin inhibitor from C. quinoa seeds. The purification occurred in gel-filtration and reverse phase chromatography. CqTI presented active against commercial bovine trypsin and chymotrypsin and had a specific activity of 5,033.00 (TIU/mg), which was purified to 333.5-fold. The extent of purification was determined by SDS-PAGE. CqTI had an apparent molecular weight of approximately 12KDa and two bands in reduced conditions as determined by Tricine-SDS-PAGE. MALDI-TOF showed two peaks in 4,246.5 and 7,908.18m/z. CqTI presented high levels of essential amino acids. N-terminal amino acid sequence of this protein did not show similarity to any known protease inhibitor. Its activity was stable over a pH range (2-12), temperatures range (20-100 °C) and reducing agents.Keywords: purification; characterization; inhibitor of trypsin; Chenopodium quinoa; seeds. Practical Application:The purification and characterization of this novel trypsin inhibitor allow its study for a diversity of applications such as antibacterial, anticancer, anti-inflammatory and biotechnology and its further use as drugs for human diseases.

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“…Many factors are involved in the protein solubility and isolation of target protease inhibitors. Those include particle size and nature of tissue, ionic strength, type and concentration of extracting medium and hydration characteristics of protein (Benjakul et al 2000;Klomklao et al 2011). Therefore, extraction time of 1 h was selected for the recovery of SOSPI from squid ovary powder.…”

Section: Resultsmentioning

confidence: 99%

Serine protease inhibitors from squid ovary: extraction and its effect on proteolysis and gel properties of surimi

Singh

Benjakul

2016

J Food Sci Technol

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Serine protease inhibitors from squid ovary (SOSPI) were extracted using different extraction media and conditions. Optimal condition included 0.45 M NaCl for 1 h. After heat treatment at 70°C for 10 min, the highest specific activity was obtained. Based on Sephadex G-75 gel filtration and activity staining, the major SOSPIs were present as monomer with molecular weight of 9.10 and 10.27 kDa. Impact of SOSPI on autolysis of bigeye snapper surimi was studied. Myosin heavy chain was more retained with coincidentally lower trichloroacetic acidsoluble peptide content as the level of SOSPI increased. When SOSPI at various levels (0.5-3%) was added into surimi, the highest breaking force of both kamaboko and modori gels containing 1% SOSPI was obtained. However, SOSPI had no effect on deformation of kamaboko gel but slightly increased the deformation of modori gel. SOSPI increased water holding capacity of both kamaboko and modori gels in a dose dependent manner, as indicated by the lowered expressible moisture content. SOSPI had no effect on the whiteness of both gels. Thus SOSPI can be used as the protein additive in surimi for increasing breaking force.

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Extraction, purification and properties of trypsin inhibitor from Thai mung bean (Vigna radiata (L.) R. Wilczek)

Cited by 54 publications

References 22 publications

Partial purification of trypsin inhibitors from Parkia seeds (Fabaceae)

Partial purification of trypsin inhibitors from Parkia seeds (Fabaceae)

Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds

Serine protease inhibitors from squid ovary: extraction and its effect on proteolysis and gel properties of surimi

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