Two legume defense proteins suppress the mobility of nasopharyngeal carcinoma cells

Dan, Xiuli; Ng, Tzi Bun

doi:10.3109/14756366.2015.1132709

Cited by 2 publications

(2 citation statements)

References 30 publications

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“…Lectins are widespread in nature, and most of them have been isolated and characterized from Fabaceae, Gramineae, and Lamiaceae families, among others [47,48]. Those lectins have been related to insect defense mechanisms, storage proteins, carbohydrate transport, mechanisms of physiological regulation, and mitogenic stimulation processes [49][50][51][52][53][54][55]. The ability of the nitrogen-fixing bacteria rhizobia to form a symbiotic relationship with legumes, in which plant root lectins are involved, is well known.…”

Section: Fabaceae (Legume) and Lamiaceae (Mint) Lectinsmentioning

confidence: 99%

Plant Lectins with Insecticidal and Insectistatic Activities

Reyes-Montaño¹,

Castro²

2018

Insecticides - Agriculture and Toxicology

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Lectins are an important group of proteins which are spread in all kingdoms of life. Their most lighted characteristic is associated to their specific carbohydrate binding, although function has been not even identified. According to their carbohydrate specificity, several biological activities have been assessed, finding that lectins can be used as mitogenic agents, biomarkers, and cytotoxic and insecticide proteins. Lectins have been classified according to several features such as structure, source, and carbohydrate recognition. The Protein Research Group (PRG) has worked on Colombian seeds from the family of Fabaceae and Lamiaceae plants, isolating and characterizing their lectins, and found more than one lectin in some plants, indicating that according to its specificity, different lectins can have different biological activities. In the case of legume domain lectins, they have shown the biggest potential as insecticide or insectistatic agents due to the glycosylation pattern in insect midgut cells. This review attempts to identify the characteristics of plant legume lectin domains that determine their insecticidal and insectistatic activities.

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Section: Fabaceae (Legume) and Lamiaceae (Mint) Lectinsmentioning

confidence: 99%

Plant Lectins with Insecticidal and Insectistatic Activities

Reyes-Montaño¹,

Castro²

2018

Insecticides - Agriculture and Toxicology

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“…This is due to intestinal proteolysis inhibition, meaning relevant endogenous sulfur amino acid losses, affecting the biological value and bioavailability of nutrients (Coscueta et al, ). However, positive physiological effects such as carcinogenesis suppression and anti‐inflammatory activity in several in vitro and animal studies were associated with soy products found in the diet, Bowman‐Birk‐Inhibitor (BBI) PI type being the main one involved (Dan & Ng, ; Gemede & Ratta, ).…”

Section: Introductionmentioning

confidence: 99%

Thermal treatment for soybean flour processing with high‐quality color and reduced Kunitz trypsin inhibitor

Dahmer

Rigó

Steffens

et al. 2018

J Food Process Engineering

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In this work thermal treatment was applied in whole soybean flour and bleached whole soybean flour production aimed at Kunitz trypsin inhibitor (KTI) reduction and color. A 22 Central Composite Rotational Design was developed to evaluate the effects of temperature (91.80–148.20 °C) and time (15.9–44.10 min). In general, the bleached whole soybean flour presented higher KTI reduction and better color than whole soybean flour in the evaluated temperature and time ranges. It was observed that at 148.2 °C for 30 min the whole soybean flour presented a lower KTI value (1.56 mg/g) than bleached whole soybean flour (1.48 mg/g) and good luminosity. As the bleached presents an extra step in the treatment process, new experiments were made with whole soybean flour without bleached to evaluate KTI and color reduction as a time function (10–30 min) at 148.2 °C. The time was evaluated the verify the behavior of KTI and color of whole soybean flour. The treatment at 148.2 °C for 20 and 30 min presented the lowest KTI values, however, the L* color value at 20 min was higher and soybean flour was whiter, hence 20 min was considered the best condition for whole soybean flour production. Practical applications In order to increase the nutritional quality of soybeans and use them as food, the inactivation of protease inhibitors is required. As soybean nutritional value is adversely affected by protease inhibitors presence that are considered anti‐nutritional factors, these need to be eliminated. Thermal treatment has been used as a physical method to inactivate these factors. However, it must be controlled to avoid essential amino acids destruction. Thermal treatment prior to soybean processing for flour production is common. However, recommendation for the best time and temperature for the grains is nonexistent in order to inactivate and/or reduce their phytochemicals with anti‐nutritional action, to the detriment of those with functional effect, preserving their nutrients. Usually, commercial soybean products are thermally treated with less than 20% of in natura soybean trypsin inhibitory activity.

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Two legume defense proteins suppress the mobility of nasopharyngeal carcinoma cells

Cited by 2 publications

References 30 publications

Plant Lectins with Insecticidal and Insectistatic Activities

Plant Lectins with Insecticidal and Insectistatic Activities

Thermal treatment for soybean flour processing with high‐quality color and reduced Kunitz trypsin inhibitor

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