Purification and characterization of a novel trypsin inhibitor from Solanum tuberosum subsp. andigenum var. overa: Study of the expression levels and preliminary evaluation of its antimicrobial activity

Cisneros, José Sebastián; Cotabarren, Juliana; Parisi, Mónica Graciela; Vasconcelos, Marta W.; Obregón, Walter David

doi:10.1016/j.ijbiomac.2020.04.217

Cited by 3 publications

(3 citation statements)

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“…It represents one of the most important food crops in the world along with wheat, rice, and corn 32 . Potato proteins present several functional and nutritional properties, as emulsifiers, foaming agents, gelation, and antioxidant activity 33 . This study reported the milk‐clotting activity of two potato aspartic proteases, St AP1 and St AP3 20 .…”

Section: Discussionmentioning

confidence: 91%

“…32 Potato proteins present several functional and nutritional properties, as emulsifiers, foaming agents, gelation, and antioxidant activity. 33 This study reported the milk-clotting activity of two potato aspartic proteases, StAP1 and StAP3. 20 The characterization of StAPs' MCA showed that these enzymes could be used as vrennets in artisanal cheese production.…”

Section: Discussionmentioning

confidence: 99%

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Optimization of caseinolytic and coagulating activities of Solanum tuberosum rennets for cheese making

et al. 2023

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BACKGROUNDIn recent years, the rising global demand for cheese, the high cost and limited supply of calf rennet, and consumer choices have increased research into new alternatives to animal or recombinant chymosins for cheese making. Plant proteases with caseinolytic activity (CA) and milk‐clotting activity (MCA) have been proposed as alternatives for milk clotting to obtain artisanal cheeses with new organoleptic properties. They have been named vegetable rennets (vrennets). The aim of this study was to evaluate the performance of two Solanum tuberosum aspartic proteases (StAP1 and StAP3) as vrennets for cheese making and to obtain a statistical model that could predict and optimize their enzymatic activity.RESULTSTo optimize the CA and MCA activities, a response surface methodology was used. Maximum values of CA and MCA for both enzymes were found at pH 5.0 and 30–35 °C. Analysis of the degradation of casein subunits showed that it is possible to tune the specificity of both enzymes by changing the pH. At pH 6.5, the αS‐ and β‐ subunit degradation is reduced while conserving a significant MCA.CONCLUSIONThe statistical models obtained in this work showed that StAP1 and StAP3 exert CA and MCA under pH and temperature conditions compatible with those used for cheese making. The casein subunit degradation percentages obtained also allowed us to select the best conditions for the degradation of the κ‐casein subunit by StAPs. These results suggest that StAP1 and StAP3 are good candidates as vrennets for artisan cheese making. © 2023 Society of Chemical Industry.

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Section: Discussionmentioning

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Optimization of caseinolytic and coagulating activities of Solanum tuberosum rennets for cheese making

et al. 2023

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“…Higher plants possess the ability to produce a wide variety of secondary metabolites with high chemical diversity, including proteins, peptides, sugars, and nucleosides. Many of these compounds, such as plant-derived proteins and peptides, are PIs with demonstrated antibacterial [ 6 , 7 ] and antifungal properties [ 8 ]. Plants are rich in small proteinaceous PIs as these molecules are involved in plant defense mechanisms against pathogens and predators [ 5 , 9 , 10 ].…”

Section: Introductionmentioning

confidence: 99%

A Multifunctional Trypsin Protease Inhibitor from Yellow Bell Pepper Seeds: Uncovering Its Dual Antifungal and Hypoglycemic Properties

et al. 2023

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Fungal infections are a growing public health concern worldwide and the emergence of antifungal resistance has limited the number of therapeutic options. Therefore, developing novel strategies for identifying and developing new antifungal compounds is an active area of research in the pharmaceutical industry. In this study, we purified and characterized a trypsin protease inhibitor obtained from Yellow Bell Pepper (Capsicum annuum L.) seeds. The inhibitor not only showed potent and specific activity against the pathogenic fungus Candida albicans, but was also found to be non-toxic against human cells. Furthermore, this inhibitor is unique in that it also inhibits α-1,4-glucosidase, positioning it as one of the first plant-derived protease inhibitors with dual biological activity. This exciting discovery opens new avenues for the development of this inhibitor as a promising antifungal agent and highlights the potential of plant-derived protease inhibitors as a rich source for the discovery of novel multifunctional bioactive molecules.

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Purification and characterization of a new protease inhibitor from Spatholobus parviflorus seeds which inhibits the larval gut proteases of Spodoptera mauritia (Boisduval) (Lepidoptera: Noctuidae)

Parambil

Meethal

2021

J. Plant Biochem. Biotechnol.

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Purification and characterization of a novel trypsin inhibitor from Solanum tuberosum subsp. andigenum var. overa: Study of the expression levels and preliminary evaluation of its antimicrobial activity

Cited by 3 publications

References 81 publications

Optimization of caseinolytic and coagulating activities of Solanum tuberosum rennets for cheese making

Optimization of caseinolytic and coagulating activities of Solanum tuberosum rennets for cheese making

A Multifunctional Trypsin Protease Inhibitor from Yellow Bell Pepper Seeds: Uncovering Its Dual Antifungal and Hypoglycemic Properties

Purification and characterization of a new protease inhibitor from Spatholobus parviflorus seeds which inhibits the larval gut proteases of Spodoptera mauritia (Boisduval) (Lepidoptera: Noctuidae)

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