Plant Protease Inhibitors as Food Processing Aids

2020 ◽  
pp. 213-224
Author(s):  
Norman F. Haard
Keyword(s):  
Protease Inhibitors ◽  
Food Processing ◽  
Plant Protease ◽  
Processing Aids

Adaptive Mechanisms of Insect Pests Against Plant Protease Inhibitors and Future Prospects Related to Crop Protection: A Review

2015 ◽  
Vol 22 (2) ◽  
pp. 149-163 ◽  
Author(s):  
Maria Macedo ◽  
Caio de Oliveira ◽  
Poliene Costa ◽  
Elaine Castelhano ◽  
Marcio Silva-Filho
Keyword(s):  
Protease Inhibitors ◽  
Insect Pests ◽  
Crop Protection ◽  
Future Prospects ◽  
Adaptive Mechanisms ◽  
Plant Protease

scholarly journals The complex world of plant protease inhibitors: Insights into a Kunitz-type cysteine protease inhibitor of Arabidopsis thaliana

2017 ◽  
Vol 11 (1) ◽  
pp. e1368599 ◽  
Author(s):  
Sachin Rustgi ◽  
Edouard Boex-Fontvieille ◽  
Christiane Reinbothe ◽  
Diter von Wettstein ◽  
Steffen Reinbothe
Keyword(s):  
Arabidopsis Thaliana ◽  
Protease Inhibitor ◽  
Protease Inhibitors ◽  
Cysteine Protease ◽  
Cysteine Protease Inhibitor ◽  
Complex World ◽  
Plant Protease ◽  
Kunitz Type

Exclusive rewards in mutualisms: ant proteases and plant protease inhibitors create a lock-key system to protectAcaciafood bodies from exploitation

2013 ◽  
Vol 22 (15) ◽  
pp. 4087-4100 ◽  
Author(s):  
Domancar Orona-Tamayo ◽  
Natalie Wielsch ◽  
Alejandro Blanco-Labra ◽  
Ales Svatos ◽  
Rodolfo Farías-Rodríguez ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Plant Protease

The adaptation of insects to plant protease inhibitors

1997 ◽  
Vol 43 (10) ◽  
pp. 885-895 ◽  
Author(s):  
Maarten A Jongsma ◽  
Caroline Bolter
Keyword(s):  
Protease Inhibitors ◽  
Plant Protease

scholarly journals Peanut Seed Cultivars with Contrasting Resistance to Aspergillus parasiticus Colonization Display Differential Temporal Response of Protease Inhibitors

2017 ◽  
Vol 107 (4) ◽  
pp. 474-482 ◽  
Author(s):  
Virginia Müller ◽  
Gustavo Bonacci ◽  
Carlos Batthyany ◽  
María V. Amé ◽  
Fernando Carrari ◽  
...  
Keyword(s):  
Fungal Infection ◽  
Protease Inhibitors ◽  
Aspergillus Parasiticus ◽  
Biological Significance ◽  
Aflatoxin Contamination ◽  
Resistant Cultivar ◽  
2D Electrophoresis ◽  
Susceptible Cultivar ◽  
Plant Protease ◽  
Trypsin Inhibitory Activity

Significant efforts are being made to minimize aflatoxin contamination in peanut seeds and one possible strategy is to understand and exploit the mechanisms of plant defense against fungal infection. In this study we have identified and characterized, at biochemical and molecular levels, plant protease inhibitors (PPIs) produced in peanut seeds of the resistant PI 337394 and the susceptible Forman cultivar during Aspergillus parasiticus colonization. With chromatographic methods and 2D-electrophoresis-mass spectrometry we have isolated and identified four variants of Bowman-Birk trypsin inhibitor (BBTI) and a novel Kunitz-type protease inhibitor (KPI) produced in response to A. parasiticus colonization. KPI was detected only in the resistant cultivar, while BBTI was produced in the resistant cultivar in a higher concentration than susceptible cultivar and with different isoforms. The kinetic expression of KPI and BBTI genes along with trypsin inhibitory activity was analyzed in both cultivars during infection. In the susceptible cultivar an early PPI activity response was associated with BBTI occurrence. Meanwhile, in the resistant cultivar a later response with a larger increase in PPI activity was associated with BBTI and KPI occurrence. The biological significance of PPI in seed defense against fungal infection was analyzed and linked to inhibitory properties on enzymes released by the fungus during infection, and to the antifungal effect of KPI.

scholarly journals Purification, characterization, and bioassay of putative protease inhibitors from Hevea brasiliensis latex

2017 ◽  
Vol 84 (2) ◽  
Author(s):  
Riza Arief PUTRANTO ◽  
. SISWANTO ◽  
Agustin Sri MULYATNI ◽  
Asmini BUDIANI ◽  
Radite TISTAMA
Keyword(s):  
Protease Inhibitor ◽  
Protease Inhibitors ◽  
Inhibitory Activity ◽  
Hevea Brasiliensis ◽  
Rubber Tree ◽  
Exchange Chromatography ◽  
Mycelium Growth ◽  
Plant Protease ◽  
Putative Protease

Latex, a milky white liquid, is the main product from rubber tree (Hevea brasiliensis). Latex is the cytoplasm of complex cellular networks named laticifers in which it contains many different components, including important proteins. Various types of enzymes carrying functions associated with plant defense against pathogen and wounding have been detected in latex in which one of these enzymes is protease inhibitor (PI). Plant protease inhibitor has tremendous potential as an antifungal agent which can be developed as biofungicide. In this work, protease inhibitors from B-serum (lutoid) of rubber tree latex were isolated and purified using Ion Exchange Chromatography (IEC) technique. Of the total 70 fractions of proteins extracted from the columns, only 26 fractions showed measurable levels of protein. The concentration of obtained putative protease inhibitors (three fractions of IEC) ranged from 0.007 to 0.022 mL/g B-serum. Inhibitory activity against four protease enzymes (subtilisin A, trypsin, α-chymotrypsin, and papain) showed the characteristics of Hevea putative protease inhibitors from B-serum as serine and/or cysteine protease inhibitors with more than 15% inhibitory activity of target protease. Based on SDS-PAGE visualization, the molecular weight of dominant protein considered as Hevea putative protease inhibitors was 21.5 kDa. In vitro bioassay test of antifungal activity for Hevea putative protease inhibitors showed reduced mycelium growth of Ganoderma boninense, Sclerotium sp., and Rigidosporus lignosus.

scholarly journals A Review on Therapeutic Potential of Protease Inhibitors from Medicinal Plants

2019 ◽  
pp. 1-11
Author(s):  
R. N. N. Gamage ◽  
K. D. K. P. Kumari
Keyword(s):  
Protease Inhibitor ◽  
Protease Inhibitors ◽  
Blood Clotting ◽  
Therapeutic Potential ◽  
Biological Activities ◽  
Geographical Location ◽  
Therapeutic Agents ◽  
Human Diseases ◽  
Plant Protease ◽  
Protease Specificity

Most of the currently available therapeutic agents, particularly for cardiovascular disorders and cancers are very expensive and induce some serious side effects. Some of these drugs have also become less effective due to the emergence of antibiotic resistance. There is a necessity and great demand for the development of novel efficacious plant-based agents that are of pharmacologically effective. In this connection, this review focuses on therapeutic potential of plant protease inhibitors. Protease inhibitors are of a particular concern at present due to their potent ability to inhibit protease enzymes that are involved in pathogenesis of various human diseases. In addition to their function as protein-degrading enzymes, protease inhibitors are now well-known for their capability to involve in many biological activities as signaling molecules. Plant protease inhibitors are also engaged in several physiological and pathological processes, such as blood clotting, inflammation, immune regulation, apoptosis and carcinogenesis. Therefore, isolation of plant protease inhibitors and evaluation of their therapeutic capacity against chronic human diseases have become a major research interest. Nevertheless, protease inhibitor content and protease specificity vary significantly even in the same plant species depending on the geographical location and environmental factors. Consequently, it is important to identify potent therapeutic potential of each plant protease inhibitor on human health individually.

Co-Evolution of Insect Proteases and Plant Protease Inhibitors

2011 ◽  
Vol 12 (5) ◽  
pp. 437-447 ◽  
Author(s):  
Maarten A. Jongsma ◽  
Jules Beekwilder
Keyword(s):  
Protease Inhibitors ◽  
Plant Protease
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