Characterization of Protease inhibitors from the seeds of <i>Senna alata</i>

Chandrashekharaiah, K. S.; Shweta, H P; Bharadwaj, Rajiv; Raju, Naga; Swamy, N. Ramachandra

doi:10.5958/0974-4150.2018.00063.9

Cited by 2 publications

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“…The isolated inhibitors were found to be stable at temperatures below 80°C and maximum activity was obtained at 40−50°C and also the inhibitors were stable in a wide pH range (2−12). The high temperature and pH stability of α-amylase inhibitors were confirmed by other authors on α-amylase inhibitor isolated from different sources (Gavit et al 2013;Puntambekar and Dake 2017;Chandrashekharaiah 2018). The high temperature tolerance and broad pH stability observed for Beni Suef-1 and Beni Suef-5 α-amylase inhibitors indicate their effectiveness in controlling a variety of phytophagous insects with different gut conditions.…”

Section: Discussionsupporting

confidence: 52%

“…Working on Vigna sublobata, Kokiladevi et al (2005) reported that the specific activity of a purified fraction using ammonium sulfate was 7.48 times that of the crude extract. On the other hand, high purification of 16 and 24.24 times were obtained in the purification of α-amylase inhibitor from A. paniculatus (Gavit et al 2013) and Sena alata (Chandrashekharaiah 2018), respectively. As suggested by Prabhu and Pattabiraman (1980) and Babu and Subrhamnyam (2010), the low level of purification achieved in this study may be due to the high concentration of the inhibitor in the seed.…”

Section: Discussionmentioning

confidence: 99%

“…Compared to other fractions, the F 60-90 (NH 4 ) 2 SO 4 proteins in both varieties showed strong inhibitory activity against α-amylase. F 80-100 (NH 4 ) 2 SO 4 was found to be suitable for the purification α-amylase inhibitor from Amaranthus paniculatus (Gavit et al 2013) and F 0−90 was suitable for Sena alata (Chandrashekharaiah 2018). The F 60-90 protein was applied to ion exchange chromatography, DEAE-Sephadex G-50 column and the retained The ion exchange purified α-amylase inhibitors from Beni Suef-1 and Beni Suef-5 showed a molecular weight of 16 and 24 kDa.…”

Section: Discussionmentioning

confidence: 99%

“…Gavit et al (2013) reported α-amylase inhibitor with a molecular weight of 14.3 kDa from rice. Chandrashekharaiah (2018) reported α-amylase inhibitor 14 kDa from rice. Similarly,15.488,18.62 and 26.302 kDa α-amylase inhibitors from bean cultivars were reported by Gupta et al (2014).…”

Section: Discussionmentioning

confidence: 99%

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Journal of Plant Protection Research

El-Latif,

Mohieldeen,

Salman

et al. 2020

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Plant derived α-amylase inhibitors are proteinaceous molecules that regulate the enzyme activity in plants and also protect plants from insect attack. In the current study, 28 accessions of 19 plant species were screened for their α-amylase inhibitory activity. The durum wheat varieties, Beni Suef-1 and Beni Suef-5, showed strong α-amylase inhibitory activity and were subjected to further purification studies using ammonium sulfate fractionation and DEAE-Sephadex G-25 column. The isolated inhibitors were found to be stable at temperatures below 80°C with maximum activity obtained at 40−50°C. Also, they were stable in a wide pH range (2−12). The ion exchange products of purified α-amylase inhibitors from Beni Suef-1 and Beni Suef-5 varieties showed a molecular weight of 16 and 24 kDa, respectively. The purified α-amylase inhibitors were tested against Tribo lium castaneum and Callosobruchus maculatus both in vitro and in vivo. There was linear inhibition of α-amylase activity with increasing inhibitor concentration until saturation was reached. Beni Suef-5 α-amylase inhibitor was more potent against α-amylase with lower IC 50 values than Beni Suef-1 α-amylase inhibitor except in the case of T. castaneum larva. Kinetics analysis revealed that Beni Suef-1 and Beni Suef-5 α-amylase inhibitors are non--competitive types of inhibitors with high affinity toward α-amylase of T. castaneum and C. maculatus. Results of the in vivo studies demonstrated that α-amylase inhibitors isolated from durum wheat, Beni Suef-1 and Beni Suef-5 varieties, were very effective in inhibiting the development of T. castaneum and C. maculatus and could be used for future studies in developing insect resistant transgenic plants approaching α-amylase inhibitor genes.

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Section: Discussionsupporting

confidence: 52%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Journal of Plant Protection Research

El-Latif,

Mohieldeen,

Salman

et al. 2020

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“…As the seeds of this plant are edible, the inhibitor is a dietary source for humans [23]. Senna alata is a medicinal plant, and from its seeds two potential inhibitors are isolated [24]. Previous research has identified trypsin inhibitors in many food plants like potatoes (Solanum tuberosum), sweet corn (Zea mays), sweet potato (Ipomea batatus), spinach (Spinacia oleracea), broccoli (Brassica oleracea var.botrytis), Brussels sprouts (Brassica oleracea var.…”

Section: Trypsin Inhibition By Plant Extractsmentioning

confidence: 99%

Assessment of Cytotoxic Effects of Plant Protease Inhibitors on Cancerous Cell Lines

Moosaripparambil,

Meethal

2024

UPJOZ

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Protease inhibitors, whether natural or synthetic, show promise in cancer treatment by targeting dysregulated proteolytic activity linked to tumor progression and metastasis. This study evaluated trypsin inhibitory activity and cytotoxic effects of selected plant extracts. Screening twenty-six plant extracts revealed twelve extracts contain trypsin inhibitors, and eighteen plant extracts showed cytotoxicity to the HT29 cell line, with the highest cytotoxicity shown by Senna alatta extract (98.45 ± 0.44 %). When plant extracts containing protease inhibitors were subjected to proteinase K digestion, the protease inhibitor activity as well as cytotoxicity was reduced. For example, extracts from Chassalia curviflora, Senna alata, and Grewia nervosa showed high trypsin inhibition as well as cytotoxicity, both of which were reduced by proteinase K treatment. This indicates that there is some correlation between cytotoxicity and trypsin inhibition (r = 0.52) and proteinaceous trypsin inhibitors or other proteins are involved in the cytotoxicity. These findings highlight the potential role of trypsin inhibitors in cytotoxicity against cancer cell lines.

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Characterization of Protease inhibitors from the seeds of Senna alata

Cited by 2 publications

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Journal of Plant Protection Research

Journal of Plant Protection Research

Assessment of Cytotoxic Effects of Plant Protease Inhibitors on Cancerous Cell Lines

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