Effects of phosphorus and sulfur nutrition on soluble sugars and growth inClitoria ternatea L.

Zaroug, M. G.; Munns, D. N.

doi:10.1007/bf02181804

Cited by 2 publications

(1 citation statement)

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“…Nodulation was shown to be more favorably induced with a soil moisture content of around 25–45% with a light duration of 11–14 h and an intensity of 11–17 W/m 2 (Habish and Mahdi, 1983). Supplementing the soil with sulfur was also demonstrated as beneficial for nodule formation (Zaroug and Munns, 1980a). Several studies have reported the benefits of C. ternatea to soil health (De Souza et al, 1996; Dwivedi and Kumar, 2001; Kamh et al, 2002; Alderete-Chavez et al, 2011).…”

Section: Historical and Current Applicationsmentioning

confidence: 99%

Butterfly Pea (Clitoria ternatea), a Cyclotide-Bearing Plant With Applications in Agriculture and Medicine

et al. 2019

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The perennial leguminous herb Clitoria ternatea (butterfly pea) has attracted significant interest based on its agricultural and medical applications, which range from use as a fodder and nitrogen fixing crop, to applications in food coloring and cosmetics, traditional medicine and as a source of an eco-friendly insecticide. In this article we provide a broad multidisciplinary review that includes descriptions of the physical appearance, distribution, taxonomy, habitat, growth and propagation, phytochemical composition and applications of this plant. Notable amongst its repertoire of chemical components are anthocyanins which give C. ternatea flowers their characteristic blue color, and cyclotides, ultra-stable macrocyclic peptides that are present in all tissues of this plant. The latter are potent insecticidal molecules and are implicated as the bioactive agents in a plant extract used commercially as an insecticide. We include a description of the genetic origin of these peptides, which interestingly involve the co-option of an ancestral albumin gene to produce the cyclotide precursor protein. The biosynthesis step in which the cyclic peptide backbone is formed involves an asparaginyl endopeptidase, of which in C. ternatea is known as butelase-1. This enzyme is highly efficient in peptide ligation and has been the focus of many recent studies on peptide ligation and cyclization for biotechnological applications. The article concludes with some suggestions for future studies on this plant, including the need to explore possible synergies between the various peptidic and non-peptidic phytochemicals.

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