Bowman–Birk proteinase inhibitor from Clitoria fairchildiana seeds: Isolation, biochemical properties and insecticidal potential

Dantzger, Miriam; Vasconcelos, Ilka M.; Scorsato, Valéria; Aparício, Ricardo; Marangoni, Sérgio; Macedo, Maria Lígia Rodrigues

doi:10.1016/j.phytochem.2015.08.013

Cited by 46 publications

(29 citation statements)

References 58 publications

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“…This finding suggests the existence of more disulfide bonds near the anti‐trypsin reactive site than near the anti‐chymotrypsin reactive site. Similar findings have been reported for CFPI from C. fairchildiana and horsegram BBI from Dolichos biflorus …”

Section: Resultssupporting

confidence: 89%

“…This finding suggests the existence of more disulfide bonds near the anti-trypsin reactive site than near the anti-chymotrypsin reactive site. Similar findings have been reported for CFPI from C. fairchildiana 56 and horsegram BBI from Dolichos biflorus. 58 When exposed to treatment with a range of pHs, LsCTI was stable, with none of the pHs tested being able to reduce its inhibitory activity on chymotrypsin ( Figure 5C) and trypsin ( Figure 5D).…”

Section: Resultssupporting

confidence: 89%

“…Within serine protease inhibitors, there are two families that should be highlighted, Kunitz and Bowman–Birk. These families are abundant in various legumes . The characteristics of LsCTI, such as its low molecular mass (8.87 kDa), its inhibitory activity towards several serine enzymes and its remarkable stability in the presence of denaturing agents, suggest that the inhibitor is a novel BBI.…”

Section: Resultsmentioning

confidence: 63%

“…The lowest DTT concentration (1 x 10 ‐3 m ) did not affect the activity even after 120 min of incubation, whereas at 10 x 10 ‐3 m only 30 min of incubation was necessary to reduce the inhibitory activity almost totally for chymotrypsin (Figure A) and totally for trypsin (Figure B). Although the LsCTI reduction caused by higher DTT concentrations led to loss of activity for both enzymes assessed, the molecule was more resistant to reduction than the Clitoria fairchildiana protease inhibitor (CFPI), which was found to lose 77% of its inhibitory activity for trypsin and 44% for chymotrypsin after 120 min of incubation with DTT (1 x 10 ‐3 m ), and BgPI from Vigna mungo , which completely lost its activity after 15 min at the same DTT concentration . The incubation of LsCTI with DTT (10 x 10 ‐3 m ) for 30 min caused complete loss of its inhibitory activity on trypsin and a > 80% loss for chymotrypsin.…”

Section: Resultsmentioning

confidence: 99%

“…These families are abundant in various legumes. 56 The characteristics of LsCTI, such as its low molecular mass (8.87 kDa), its inhibitory activity towards several serine enzymes and its remarkable stability in the presence of denaturing agents, suggest that the inhibitor is a novel BBI. Furthermore, L. sericeus belongs to Papilionoideae, the most evolutionarily derived Fabaceae subfamily which typically expresses BBIs in contrast to other subfamilies expressing Kunitz-type inhibitors.…”

Section: Resultsmentioning

confidence: 99%

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First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin‐trypsin inhibitor purified from Lonchocarpus sericeus seeds

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show abstract

Section: Resultssupporting

confidence: 89%

Section: Resultssupporting

confidence: 89%

Section: Resultsmentioning

confidence: 63%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 3 more Smart Citations

First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin‐trypsin inhibitor purified from Lonchocarpus sericeus seeds

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et al. 2018

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Larval development and proteolytic activity of Anticarsia gemmatalis Hübner (Lepidoptera: Noctuidae) exposed to different soybean protease inhibitors

Mendonça

Barros

Cordeiro

et al. 2019

Arch Insect Biochem Physiol

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Anticarsia gemmatalis represents a relevant factor for lowering soybean and other legume crop productivities.Protease inhibitors affect protein degradation and reduce the availability of amino acids, impairing the development and survival of insect pests. To evaluate the possible use of proteinaceous protease inhibitors in the management of this pest, the activities of midgut proteases and the growth and development of A. gemmatalis larvae exposed to soybean Bowman-Birk trypsin-chymotrypsin inhibitor (SBBI) and soybean Kunitz trypsin inhibitor (SKTI) were determined. The survival curves obtained using Kaplan-Meier estimators indicated that SKTI and SBBI stimulated larval survival. However, the development of A.gemmatalis was delayed, and prepupal weight decreased in the presence of both inhibitors. The results showed that SKTI and SBBI inhibited the trypsin-like and total proteolytic activities of larvae on the 12th day after eclosion. On the 15th day after eclosion, larvae exposed to SKTI increased the activities of trypsin and total proteases.Although SKTI and SBBI did not affect the survival of the insect, they had effects on midgut proteases in a stage wherein A. gemmatalis fed voraciously, increased the larval cycle, and decreased prepupal weight. These findings provide baseline information about the potential of proteinaceous protease inhibitors to manage the velvetbean caterpillar, avoiding chemical pesticides.K E Y W O R D S biotic stress, insect attack, insect performance, protease inhibitory

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Faba bean nutrition: Macronutrients, antinutrients, and the effect of processing

Shi,

Stone,

Marinangeli

et al. 2024

Cereal Chem

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Background and ObjectivesFaba beans are emerging as highly nutritious ingredients that have the potential to contribute to the global demand for healthy and sustainable plant‐based proteins. The current review aims to provide a summarized overview of faba bean macronutrients, protein quality, and antinutritional factors (ANFs), as well as their reduction strategies through a variety of processing means.FindingsRelative to other pulses, faba beans are higher in protein content and similar in protein quality. However, without proper preparation and/or processing, the presence of minor amounts of ANFs can hinder their nutritional value. These nonnutritive, but biologically active, compounds can be diminished through mechanical, thermal, and nonthermal treatments.ConclusionsNonconventional processing techniques to retain or improve protein quality remain an area of future research for improving faba bean nutrition and expanding its utilization.Significance and NoveltyThis review will advance the science and utilization of faba bean ingredients while providing future research opportunities.

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Bowman–Birk proteinase inhibitor from Clitoria fairchildiana seeds: Isolation, biochemical properties and insecticidal potential

Cited by 46 publications

References 58 publications

First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin‐trypsin inhibitor purified from Lonchocarpus sericeus seeds

First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin‐trypsin inhibitor purified from Lonchocarpus sericeus seeds

Larval development and proteolytic activity of Anticarsia gemmatalis Hübner (Lepidoptera: Noctuidae) exposed to different soybean protease inhibitors

Faba bean nutrition: Macronutrients, antinutrients, and the effect of processing

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