A Bowman–Birk protease inhibitor with antifeedant and antifungal activity from Dolichos biflorus

Kuhar, Kalika; Kansal, Rekha; Subrahmanyam, B.; Koundal, K. R.; Miglani, Kanika; Gupta, Vijay

doi:10.1007/s11738-013-1227-8

Cited by 32 publications

(18 citation statements)

References 55 publications

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“…The results are similar to our previous report, which also observed that the chymotrypsin pea protein hydrolysate inhibited α-amylase in a competitive manner; in contrast, inhibition of α-glucosidase was non-competitive [37]. Trypsin inhibition by a horse gram protease inhibitor was also shown to be competitive [49], which is consistent with the results obtained for the pea protein hydrolysates and peptide fractions. The inhibition constant (Ki) provides an indication of the binding affinity of inhibitors to an enzyme target; lower values suggest stronger binding affinity than higher values.…”

Section: Discussionsupporting

confidence: 92%

Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors

Awosika

Aluko

2019

Foods

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In this work, we report the potency of enzymatic hydrolysates of pea proteins against trypsin and chymotrypsin. Pea protein concentrate was digested with each of alcalase, chymotrypsin, pepsin, and trypsin, followed by membrane separation of the protein hydrolysates into peptide fractions (<1, 1–3, 3–5, and 5–10 kDa). Peptide size profiling with size-exclusion gel chromatography indicated the narrowest size range (0.85–4.98 kDa) for alcalase. Trypsin activity was strongly (p < 0.05) inhibited by the ultrafiltration fractions (mean IC50 = 2.2 mg/mL) obtained from the trypsin hydrolysate when compared to the unfractionated hydrolysate (IC50 = 6.8 mg/mL). Similarly, ultrafiltration also enhanced trypsin inhibition by the alcalase-digested peptides with an IC50 of 21.4 mg/mL for the unfractionated hydrolysate in comparison to 3.1–4.7 mg/mL for the fractions. However, ultrafiltration did not enhance trypsin inhibitory activity of chymotrypsin-digested peptides, while the peptide separation reduced efficacy of pepsin-digested peptides. In contrast, chymotrypsin inhibition by all the enzymatic digests was significantly (p < 0.05) enhanced by ultrafiltration, especially peptide sizes >3 kDa. Kinetics of enzyme inhibition indicate peptides were bound to the enzyme active site in a competitive mode that led to reduced catalysis. We conclude that the pea peptides could function as useful tools to promote human health and as a preservative during food processing and storage.

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Section: Discussionsupporting

confidence: 92%

Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors

Awosika

Aluko

2019

Foods

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“…Increase in POX activity in response to fungal infection has been reported in several studies (Seevers and Daly 1970; Thorpe and Hall 1984; Southerton and Deverall 1990). Bowman–Birk type trypsin inhibitor is a serine protease inhibitor that is known to exhibit antifungal activity (Wissenschafts et al 2000; Qu et al 2003; Kuhar et al 2013). Hydroxyproline-rich glycoproteins are integral components of the primary cell wall of plants that accumulate in defense response to various pathogens (Showalter et al 1985; Shailasree et al 2004).…”

Section: Discussionmentioning

confidence: 99%

Genome-wide association mapping for resistance to leaf rust, stripe rust and tan spot in wheat reveals potential candidate genes

et al. 2018

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Key messageGenome-wide association mapping in conjunction with population sequencing map and Ensembl plants was used to identify markers/candidate genes linked to leaf rust, stripe rust and tan spot resistance in wheat.AbstractLeaf rust (LR), stripe rust (YR) and tan spot (TS) are some of the important foliar diseases in wheat (Triticum aestivum L.). To identify candidate resistance genes for these diseases in CIMMYT’s (International Maize and Wheat Improvement Center) International bread wheat screening nurseries, we used genome-wide association studies (GWAS) in conjunction with information from the population sequencing map and Ensembl plants. Wheat entries were genotyped using genotyping-by-sequencing and phenotyped in replicated trials. Using a mixed linear model, we observed that seedling resistance to LR was associated with 12 markers on chromosomes 1DS, 2AS, 2BL, 3B, 4AL, 6AS and 6AL, and seedling resistance to TS was associated with 14 markers on chromosomes 1AS, 2AL, 2BL, 3AS, 3AL, 3B, 6AS and 6AL. Seedling and adult plant resistance (APR) to YR were associated with several markers at the distal end of chromosome 2AS. In addition, YR APR was also associated with markers on chromosomes 2DL, 3B and 7DS. The potential candidate genes for these diseases included several resistance genes, receptor-like serine/threonine-protein kinases and defense-related enzymes. However, extensive LD in wheat that decays at about 5 × 107 bps, poses a huge challenge for delineating candidate gene intervals and candidates should be further mapped, functionally characterized and validated. We also explored a segment on chromosome 2AS associated with multiple disease resistance and identified seventeen disease resistance linked genes. We conclude that identifying candidate genes linked to significant markers in GWAS is feasible in wheat, thus creating opportunities for accelerating molecular breeding.Electronic supplementary materialThe online version of this article (10.1007/s00122-018-3086-6) contains supplementary material, which is available to authorized users.

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“…In this study, the effect of PI alone on CBB adults was not tested. However, prior research has found that PI derived from plant sources induce low or modest mortality effects (6-28 %) to larvae or adult target pests (Fabrick et al, 2002;Franco et al, 2004;Gujar et al, 2004;Kuhar et al, 2013;Shamsi et al, 2018;Zhao et al, 2019). Further, PI from plant sources cause a restricted digestion process and nutritional deficiencies over susceptible insects (Zhu-Salzman and Zeng, 2015;Singh et al, 2018), affecting proper insect development, fecundity and survival of different pests (Ruan et al, 2015;Vasudev and Sohal, 2016).…”

Section: Discussionmentioning

confidence: 99%

Soybean protease inhibitors increase Bacillus thuringiensis subs. israelensis toxicity against Hypothenemus hampei

et al. 2020

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Introduction. The coffee berry borer (Hypothenemus hampei Ferrari, CBB) is one of the most devastating pests on coffee plantations around the world. Although CBB is susceptible to the effect of δ–endotoxins of Bacillus thuringiensis subs. israelensis (Bti) at laboratory level, the efficacy of this control method is poor in the field, presumably due to the inactivation by digestive proteases different to those required for protoxin activation. Objective. To study whether the addition of a soybean flour extract enriched with protease inhibitors (PI), mixed with Bti crystals and spores (Bti-sc) in an artificial diet, could improve the toxicity of Bti against CBB. Materials and methods. This study was performed in San José, Costa Rica, between 2012 and 2013. A set of adult female CBB insects was exposed to a mixture containing different concentrations of a partially purified soybean meal extract with active PI and lyophilized Bti-sc, and were tested through a bioassay in artificial diet to estimate the sub-lethal concentration (LC50). The mortality results were validated by observing the dissected midgut, whose ultrastructure was analyzed by transmission electron microscopy. Results. The soybean extracts partially degraded the Bti-sc complex, it reduced its LC50 by almost four times (from 1.135 to 0.315 µg µl-1) and enhanced CBB mortality in a concentration-dependent manner. Histological analyses of the midgut confirmed this synergistic effect, since severe epithelial damage to the intestinal epithelium of CBB exposed to Bti-sc + PI was visualized compared to Bti-sc alone. Conclusions. The combination of a soybean extract enriched in PI and Bti-sc enhanced the mortality effect over CBB, which was confirmed by the midgut collapse. Soybean flour is a cost-effective supplement that could increase Bti effectiveness against CBB and delay the appearance of biological resistance.

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A Bowman–Birk protease inhibitor with antifeedant and antifungal activity from Dolichos biflorus

Cited by 32 publications

References 55 publications

Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors

Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors

Genome-wide association mapping for resistance to leaf rust, stripe rust and tan spot in wheat reveals potential candidate genes

Soybean protease inhibitors increase Bacillus thuringiensis subs. israelensis toxicity against Hypothenemus hampei

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