Effect of a Bowman-Birk Proteinase Inhibitor from Phaseolus coccineus on Hypothenemus hampei Gut Proteinases In Vitro

Pereira, Ricardo; Valencia-Jiménez, Arnubio; Magalhães, Cláudio Picanço; Prates, Maura V.; Melo, Jorge Alex Taquita; Lima, Liziane Maria de; Sales, Maurı́cio P.; Nakasu, Erich Yukio Tempel; Silva, Maria Cristina Mattar da; Grossi-de-Sá, Maria Fátima

doi:10.1021/jf072155x

Cited by 22 publications

(15 citation statements)

References 38 publications

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“…In agreement, MALDI-TOF mass spectrum of BBI also showed the presence of a peak at 7837.46 Da. These observations corroborated with the previous reports on BBI type PIs isolated from Glycine soja [27] and Phaseolus coccineus [28].…”

Section: Electrophoretic and Maldi-tof Analysis Of Bbisupporting

confidence: 93%

Purification and Characterization of Bowman-Birk Trypsin Inhibitor from Soybean

Gu¹,

Song²,

Zhao³

et al. 2014

JFNR

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In this paper, crude extract of a Bowman-Birk trypsin inhibitor from soybean meal was firstly isolated by a combination of alcohol precipitation, thermal denaturation, isoelectric precipitation and acetone precipitation. Then this extract was purified by DE-52 ion exchange and affinity chromatography. The results showed that soybean Bowman-Birk trypsin inhibitor (SBBI) was purified to 50.07-fold with trypsin activity of 822.31 U·mg-1. The purified SBBI gave a single protein band in SDS-PAGE electrophoresis. The accurate molecular mass of this inhibitor was determined to be 8837.46Da by MALDI-TOF. N-terminal sequence showed high homology with other serine proteinase inhibitors belonging to the Leguminosae family.

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Section: Electrophoretic and Maldi-tof Analysis Of Bbisupporting

confidence: 93%

Purification and Characterization of Bowman-Birk Trypsin Inhibitor from Soybean

Gu¹,

Song²,

Zhao³

et al. 2014

JFNR

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“…ClustalW2 alignment of internal peptide sequences: (B) 'SFPPQCR' obtained from tryptic digested C11PI for m/z 970.386 and (C) 'MELMNKKVMMK' obtained from PMF after Lys-C digestion of C11PI, which showed similarity with several BBIs from NCBI database. (D) N-terminal sequence of C11PI obtained after Edman's degradation exhibiting similarity with several BBIs: RgPI, Cajanus cajan (ICP 14770) (Prasad et al, 2010b); DE-3, DE-4, Macrotyloma axillare BBI (Joubert et al, 1979); PcBBI1, Phaseolus coccineus BBI (Pereira et al, 2007); TBPI, Phaseolus acutifolius BBI (Campos et al, 2004); CLTI-I, Canavalia lineata BBI (Terada et al, 1994); HGI-3, Dolichos biflorus BBI (Sreerama et al, 1997); MBTI-F, Vigna radiata BBI (Wilson and Chen, 1983); AB-I, Vigna angularis BBI (Ishikawa et al, 1985); CMTI2, Cratylia mollis BBI (Paiva et al, 2006). The lift spectrum and PMF shown here is a representative of C11PI purified from at least three to four different batches of seeds.…”

Section: Determination Of Partial Amino Acid Sequencesmentioning

confidence: 99%

Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan (cv. ICP 7118)

Swathi

Lokya

Swaroop

et al. 2014

Plant Physiology and Biochemistry

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Proteinase inhibitors (C11PI) from mature dry seeds of Cajanus cajan (cv. ICP 7118) were purified by chromatography which resulted in 87-fold purification and 7.9% yield. SDS-PAGE, matrix assisted laser desorption ionization time-of-flight (MALDI-TOF/TOF) mass spectrum and two-dimensional (2-D) gel electrophoresis together resolved that C11PI possessed molecular mass of 8385.682 Da and existed as isoinhibitors. However, several of these isoinhibitors exhibited self association tendency to form small oligomers. All the isoinhibitors resolved in Native-PAGE and 2-D gel electrophoresis showed inhibitory activity against bovine pancreatic trypsin and chymotrypsin as well as Achaea janata midgut trypsin-like proteases (AjPs), a devastating pest of castor plant. Partial sequences of isoinhibitor (pI 6.0) obtained from MALDI-TOF/TOF analysis and N-terminal sequencing showed 100% homology to Bowman-Birk Inhibitors (BBIs) of leguminous plants. C11PI showed non-competitive inhibition against trypsin and chymotrypsin. A marginal loss (<15%) in C11PI activity against trypsin at 80 (°)C and basic pH (12.0) was associated with concurrent changes in its far-UV CD spectra. Further, in vitro assays demonstrated that C11PI possessed significant inhibitory potential (IC50 of 78 ng) against AjPs. On the other hand, in vivo leaf coating assays demonstrated that C11PI caused significant mortality rate with concomitant reduction in body weight of both larvae and pupae, prolonged the duration of transition from larva to pupa along with formation of abnormal larval-pupal and pupal-adult intermediates. Being smaller peptides, it is possible to express C11PI in castor to protect them against its devastating pest A. janata.

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“…Proteínas de defesa têm sido reportadas na literatura, entre elas os inibidores proteicos (IPs), quitinases, proteínas inativadoras de ribossomo (RIPs), arcelinas, vicilinas, leguminas, lectinas, defensinas, tioninas e proteínas de transferências de lipídeos (LTPs) (Habib & Fazili, 2007;Pereira et al, 2007;Hartl et al, 2011;Lima & Morais, 2013). Esses inibidores formam um complexo inibindo, parcial ou totalmente, suas enzimas cognatas (Habib & Fazili, 2007) e exercem papel preponderante no melhoramento de plantas para resistência a insetos, tanto por meio convencional quanto biotecnológico, em razão da sua capacidade de inibir enzimas hidrolíticas (Pereira et al, 2007;Oliveira et al, 2009;De Paola et al, 2012 Vários autores reportam que os IPs (proteases e α-amilases) atuam como defensivos naturais contra insetos, principalmente das Ordens Lepidoptera e Coleoptera, em razão dos efeitos deletérios provocados, incluindo redução de fecundidade, perda de peso, aumento da mortalidade e algumas deformações, em virtude da redução da atividade proteolítica do trato digestivo, limitando a assimilação de nutrientes (Haq et al, 2004;Macedo et al, 2010).…”

Section: Introductionunclassified

“…Esses inibidores formam um complexo inibindo, parcial ou totalmente, suas enzimas cognatas (Habib & Fazili, 2007) e exercem papel preponderante no melhoramento de plantas para resistência a insetos, tanto por meio convencional quanto biotecnológico, em razão da sua capacidade de inibir enzimas hidrolíticas (Pereira et al, 2007;Oliveira et al, 2009;De Paola et al, 2012 Vários autores reportam que os IPs (proteases e α-amilases) atuam como defensivos naturais contra insetos, principalmente das Ordens Lepidoptera e Coleoptera, em razão dos efeitos deletérios provocados, incluindo redução de fecundidade, perda de peso, aumento da mortalidade e algumas deformações, em virtude da redução da atividade proteolítica do trato digestivo, limitando a assimilação de nutrientes (Haq et al, 2004;Macedo et al, 2010). Isto demonstra o potencial do uso desses metabólitos como ferramenta para seleção de plantas resistentes a pragas (Chye et al, 2006;Mosolov & Valueva, 2008).…”

Section: Introductionunclassified

Prospecção de descritores para seleção de genótipos de amendoim tolerantes a pragas de grãos armazenados

Santos

Luz

Pinheiro

et al. 2014

Rev. bras. eng. agríc. ambient.

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5 R E S U M OAs inter-relações entre descritores bioquímicos e agronômicos foram investigadas em genótipos de amendoim visando identificar indicadores de seleção para tolerância a pragas de grãos armazenados, com base na capacidade inibitória para tripsina e quimotripsina. Dez genótipos foram cultivados em campo, em 2011/2012, e suas sementes utilizadas para os ensaios bioquímicos. Quatro descritores agronômicos foram utilizados para compor as análises de correlação. Sete genótipos revelaram alta capacidade inibitória para tripsina, com mais de 80% de inibição; contudo, para quimotripsina, observou-se baixa inibição em todos os genótipos, variando entre 4 e 12%. Nas análises de correlação não foram observadas inter-relações significativas entre os inibidores e as demais variáveis, com exceção de inibidor de tripsina x proteínas nas folhas, que revelou correlação negativa de alta magnitude indicando que alto teor de proteínas nas folhas pode reduzir o nível de inibidor de tripsina nas sementes. Este descritor poderia ser utilizado como indicador de seleção para tolerância a pragas de grãos armazenados, com o benefício de não destruir a semente. Prospecting of descriptors for selection of peanut genotypes tolerant to stored grain pests A B S T R A C TThe interrelations between biochemical and agronomic descriptors were investigated in peanut genotypes in order to identify selection indicators for tolerance to stored grain pests, based on the inhibitory capacity for trypsin and chymotrypsin. Ten genotypes were grown in field, in 2011/2012, and their seeds were further used for biochemical assays. Four agronomic traits were used in order to compose the correlation analysis. Seven genotypes showed high inhibitory capacity for trypsin with more than 80% inhibition; however, chymotrypsin inhibition was low in all genotypes, varying between 4 and 12%. No significant interrelationships between inhibitors and the other variables were seen in correlation analysis, except trypsin inhibitor x leaves protein, which revealed a negative correlation with high magnitude, indicating that a high protein content in the leaves can reduce the level of trypsin inhibitor in the seeds. This descriptor could be used as a selection indicator for tolerance to stored grain pests, adding the benefit of saving the seed.

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Effect of a Bowman-Birk Proteinase Inhibitor from Phaseolus coccineus on Hypothenemus hampei Gut Proteinases In Vitro

Cited by 22 publications

References 38 publications

Purification and Characterization of Bowman-Birk Trypsin Inhibitor from Soybean

Purification and Characterization of Bowman-Birk Trypsin Inhibitor from Soybean

Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan (cv. ICP 7118)

Prospecção de descritores para seleção de genótipos de amendoim tolerantes a pragas de grãos armazenados

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