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Purification of lectin and Kunitz trypsin inhibitor from soya seeds

Purification of lectin and Kunitz trypsin inhibitor from soya seeds

Roy, Uttam K., Lavignac, Nathalie, Rahman, Azizur M. and Nielsen, Birthe V. ORCID: 0000-0002-0849-4987 (2018) Purification of lectin and Kunitz trypsin inhibitor from soya seeds. Journal of Chromatographic Science, 56 (5). pp. 436-442. ISSN 0021-9665 (Print), 1945-239X (Online) (doi:

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The search for potent and selective therapeutic agents is progressing by the study of natural compounds in plants. Plant-derived macromolecules are considered emerging therapeutic agents and an alternative to synthetic and small molecule drugs. Where it has long been known that plants possess medicinal properties, the compounds responsible for their action are in many cases still unknown: often only whole crude plant extracts or fractionated extracts are tested for the ability to inhibit common pathogens. Here, we present a fast protein liquid chromatography method for the separation of crude plant proteins. Kunitz trypsin inhibitor (KTI; 24.2 kDa) and lectin (31 kDa) were purified from Glycine max by liquid extraction followed by ion exchange column chromatography. The need for serial chromatographic separation steps has been eliminated by introducing more complex elution profiles hence reducing cost, time and improving recovery. The identity of KTI-A and lectin was confirmed by MALDI-TOF/TOF Mass Spectrometry. Cell proliferation assays using B16F1 melanoma cells revealed that both KTI and the monomeric lectin retained some antiproliferative activity. This method could be useful for rapid and cost-effective purification of bioactive compounds from plant material.

Item Type: Article
Uncontrolled Keywords: Kunitz trypsin inhibitor, lectin, soya
Faculty / School / Research Centre / Research Group: Faculty of Engineering & Science
Faculty of Engineering & Science > School of Science (SCI)
Last Modified: 01 May 2020 09:30

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