Bowman-Birk Inhibitors from Legumes: Utilisation in Disease Prevention and Therapy

Clemente, Alfonso; Marín-Manzano, M. Carmen; Arques, Maria del Carmen; Domoney, Claire

doi:10.5772/51262

Cited by 14 publications

(12 citation statements)

References 100 publications

(108 reference statements)

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“…Sequence variation and polymorphism at active site domains of these double-headed inhibitors have been reviewed extensively (Clemente et al, 2006;and references therein). The recent demonstration of the capacity of legume seed protease inhibitors of the Bowman-Birk class to inhibit the growth of cancer cell lines in vitro has led to renewed interest in the properties of this class of protein (Clemente and Domoney, 2013). In seeds of pea, quantitative variation in protease inhibitor activity was mapped to a locus on linkage group V, where the structural genes encoding the trypsin/chymotrypsin inhibitors are located; molecular markers were developed later to facilitate the selection of alleles associated with quantitative variants in breeding programs (Page et al, 2002).…”

Section: E the Anti-nutritional Factor Riddle In Legumesmentioning

confidence: 99%

Achievements and Challenges in Improving the Nutritional Quality of Food Legumes

Patto

Amarowicz

Aryee

et al. 2014

Critical Reviews in Plant Sciences

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Section: E the Anti-nutritional Factor Riddle In Legumesmentioning

confidence: 99%

Achievements and Challenges in Improving the Nutritional Quality of Food Legumes

Patto

Amarowicz

Aryee

et al. 2014

Critical Reviews in Plant Sciences

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220

170

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“…Previous studies have shown the capability of BBI to protect lunasin from hydrolysis brought up by pepsin and pancreatin (Cruz-Huerta et al, 2015;Hsieh et al, 2010). In addition, BBI has possible health benefits such as being a chemopreventative (Clemente, Marín-manzano, Arques & Domoney, 2013) and anticarcinogenic agent (Kennedy, 1998). KTI is another protease inhibitor that is larger than BBI with molecular weight of approximately 20 kDa and contains less disulfide bridges.…”

Section: Introductionmentioning

confidence: 99%

Kunitz trypsin inhibitor in addition to Bowman-Birk inhibitor influence stability of lunasin against pepsin-pancreatin hydrolysis

Price

Pangloli

Krishnan

et al. 2016

Food Research International

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Soybean contains several biologically active components and one of this belongs to the bioactive peptide group. The objectives of this study were to produce different lunasin-enriched preparations (LEP) and determine the effect of Bowman-Birk inhibitor (BBI) and Kunitz trypsin inhibitor (KTI) concentrations on the stability of lunasin against pepsin-pancreatin hydrolysis (PPH). In addition, the effect of KTI mutation on lunasin stability against PPH was determined. LEP were produced by calcium and pH precipitation methods of 30% aqueous ethanol extract from defatted soybean flour. LEP, lunasin-enriched commercially available products and KTI control and mutant flours underwent PPH and samples were taken after pepsin and pepsin-pancreatin hydrolysis. The concentrations of BBI, KTI, and lunasin all decreased after hydrolysis, but they had varying results. BBI concentration ranged from 167.5 to 655.8μg/g pre-hydrolysis and 171.5 to 250.1μg/g after hydrolysis. KTI concentrations ranged from 0.3 to 122.3μg/g pre-hydrolysis and 9.0 to 18.7μg/g after hydrolysis. Lunasin concentrations ranged from 8.5 to 71.0μg/g pre-hydrolysis and 4.0 to 13.2μg/g after hydrolysis. In all products tested, lunasin concentration after PPH significantly correlated with BBI and KTI concentrations. Mutation in two KTI isoforms led to a lower concentration of lunasin after PPH. This is the first report on the potential role of KTI in lunasin stability against PPH and must be considered in designing lunasin-enriched products that could potentially survive digestion after oral ingestion.

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“…BBIs appear to exert a protective effect against inflammatory disorders and cancer development; such beneficial effect has been specifically attributed to their intrinsic ability to inhibit serine proteases (Safavi & Rostami, 2012;Clemente et al, 2013). Inactive BBI forms render these dietary proteins unable to inhibit cell proliferation of colon cancer cells (Clemente et al, 2010;.…”

Section: Discussionmentioning

confidence: 99%

“…The therapeutic value of protease inhibitors, both natural and synthetic, as modulators of such proteolytic activities in disease is well-recognized (Turk, 2006;Drag & Salvensen, 2010;Deu, Verdoes, & Bogyo, 2012). Within this framework, there is a growing interest in naturally-occurring serine protease inhibitors of the Bowman-Birk family due to their potential chemopreventive and/or therapeutic properties which can impact on several human diseases, including cancer, neurodegenerative disorders and inflammatory processes (Clemente, Marín-Manzano, Arques & Domoney, 2013). Bowman-Birk inhibitors (BBIs) from soybean (Glycine max) are the most extensively studied members of this protein family.…”

Section: Introductionmentioning

confidence: 99%

Quantitative determination of active Bowman-Birk isoinhibitors, IBB1 and IBBD2, in commercial soymilks

et al. 2014

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Naturally-occurring serine protease inhibitors of the Bowman-Birk family exert their potential chemopreventive and/or therapeutic properties via protease inhibition. In this study, we have quantified the amounts of active BBI isoinhibitors, IBB1 and IBBD2, in six commercial soymilks. By using cation exchange chromatography, the BBI isoinhibitors were isolated and their specific trypsin inhibitory activity was used to estimate their amounts in soymilk samples. IBB1 and IBBD2 concentrations ranged from 0.44 to 5.20 and 0.27 to 4.60 mg/100ml of soymilk, respectively; total BBI, considered as the sum of both isoinhibitors, ranged from 0.60 to 9.07 mg/100ml of soymilk. These data show that physiologically relevant amounts of active BBI are present in commercial soymilk and may exert potential health-promoting effects.

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Bowman-Birk Inhibitors from Legumes: Utilisation in Disease Prevention and Therapy

Cited by 14 publications

References 100 publications

Achievements and Challenges in Improving the Nutritional Quality of Food Legumes

Achievements and Challenges in Improving the Nutritional Quality of Food Legumes

Kunitz trypsin inhibitor in addition to Bowman-Birk inhibitor influence stability of lunasin against pepsin-pancreatin hydrolysis

Quantitative determination of active Bowman-Birk isoinhibitors, IBB1 and IBBD2, in commercial soymilks

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