Identification of proteins from wild cardoon flowers (Cynara cardunculus L.) by a proteomic approach

Amira, Amal Ben; Bauwens, Julien; Pauw, Edwin De; Besbes, Souhail; Attia, Hamadi; Francis, Frédéric; Blecker, Christophe

doi:10.1007/s12154-016-0161-9

Cited by 17 publications

(9 citation statements)

References 43 publications

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“…After electrophoresis, visible protein bands were excised from preparative 1D gels destained, reduced, alkylated, and trypsin‐digested as described by Ben Amira et al . Generated peptides were analyzed by LC‐MS/MS on a Q Exactive Mass Spectrometer (Thermo Fisher Scientific, UK).…”

Section: Comparative Analysis Of Chinese Gall Aphid Salivary Proteinsmentioning

confidence: 99%

Proteins Identified from Saliva and Salivary Glands of the Chinese Gall Aphid Schlechtendalia chinensis

Yang

Francis

et al. 2018

Proteomics

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Aphid saliva plays an essential role in the interaction between aphids and their host plants. Several aphid salivary proteins have been identified but none from galling aphids. Here the salivary proteins from the Chinese gall aphid are analyzed, Schlechtendalia chinensis, via an LC-MS/MS analysis. A total of 31 proteins are identified directly from saliva collected via an artificial diet, and 141 proteins are identified from extracts derived from dissected salivary glands. Among these identified proteins, 17 are found in both collected saliva and dissected salivary glands. In comparison with salivary proteins from ten other free-living Hemipterans, the most striking feature of the salivary protein from S. chinensis is the existence of high proportion of proteins with binding activity, including DNA-, protein-, ATP-, and iron-binding proteins. These proteins maybe involved in gall formation. These results provide a framework for future research to elucidate the molecular basis for gall induction by galling aphids.

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Section: Comparative Analysis Of Chinese Gall Aphid Salivary Proteinsmentioning

confidence: 99%

Proteins Identified from Saliva and Salivary Glands of the Chinese Gall Aphid Schlechtendalia chinensis

Yang

Francis

et al. 2018

Proteomics

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“…[52,65] Besides, the enzyme composition and the collecting region of C. cardunculus flowers could play a considerable role in promoting the specific activity of coagulant extract. [66] In fact, only four cardosins were identified in Tunisian cardoon flowers, among them the cardosin A can replace successfully calf chymosin. As concluded by the authors, the absence of the other cardosins (B, C, D, and F) could be an advantage, as it reduces the excessive non-specific PA during cheese making.…”

Section: Evaluation Of Enzymatic Activities Of Plant Rennetsmentioning

confidence: 99%

“…As concluded by the authors, the absence of the other cardosins (B, C, D, and F) could be an advantage, as it reduces the excessive non-specific PA during cheese making. [66] Some studies have also revealed high MCAs of plant rennets as compared with chymosin. Ahmed et al [34] concluded that the extract of Solanum dubium is an appropriate calf rennet substitute, as its MCA exceeds significantly that of calf rennet (880 and 249.6 CAU/mL at 37°C, respectively).…”

Section: Evaluation Of Enzymatic Activities Of Plant Rennetsmentioning

confidence: 99%

Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

Amira

Besbes

Attia

et al. 2017

International Journal of Food Properties

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Plant rennets hold an important position among various coagulants used in cheese technology. The selection of a suitable plant coagulant is important due to the increasing global demands of cheese alongside reduced supply of calf rennet. Thus, a literature synthesis is presented to investigate recent achievements on their functional properties and enzymatic role in cheese making. Efforts have also been done to compare certain rheological and sensory properties of final products, arising from some plant-and animalbased rennets. In fact, some coagulants such as actinidin or dubiumin produce cheeses with sensory qualities similar to those produced by animal rennet. Others, like ginger, cucumisin, or hieronymain proteases contribute to develop very different textures and flavours, due to excessive proteolytic activity and production of bitter peptides. For milk-clotting enzymes with high non-specific action, several improved strategies have been developed to produce cheeses with sensory properties close to those of animal rennet. For example, the mixture of coagulants (cardosins/chymosin), the selection of appropriate milk or its ultrafiltration, as well as the increase of salting time of cheese during ripening could be efficient ways to improve texture and reduce bitterness. Concerning cheeses with high yield loss, the whey could be used for a traditional production of whey cheese. To conclude, the selection of appropriate plant rennet with high milk-clotting activity/proteolytic activity ratio and the optimisation of all coagulation parameters play a central role in manufacturing cheese with superior rheological and sensory properties.

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“…Cardosin B has a higher specific proteolytic activity despite the fact that it is in less quantity than cardosin A. In addition to cardosins A and B, four new aspartic proteases from flowers of C. cardunculus were isolated, purified, separated by the method of 2D gel electrophoresis and identified by the MALDI-TOF-TOF method: cardasins E, F, G and H. The authors note a similarity in the biochemical parameters of cardosins A, E, F, G and H [32]. Plant aspartic proteases from the Asteraceae family mostly used in the production of cheese in the countries of the Mediterranean basin.…”

Section: Plant Proteases In Cheese Makingmentioning

confidence: 96%

Proteolytic Enzymes in Cheese Making

Aktayeva¹,

Akishev²,

Khassenov³

2018

Eurasian Journal of Applied Biotechnology

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There has been an increasing consumer demand for cheese along with a search for products with new organoleptic parameters, which has resulted in extensive research on alternative milk coagulants. The ratio of proteolytic activity to milk-clotting activity determines the requirements for proteases used in the cheese making process. To date, plant enzymes have largely been used for this purpose, along with traditional enzymes of animal origin, chymosin and pepsin. The most popular types of proteases used in the food industry, especially in cheese making, are plant proteases belonging to the cysteine (papain, bromelain, ficin), aspartate (cinarase, cardosin), and serine (kukumizin, leucine) group of proteases. The aspartate proteases of microbial origin mucorpepsin and endotyapepsin have found wide application in cheese production due to low production costs and high organoleptic characteristics of the final product. The use of plant and microbial milk-clotting enzymes as an alternative to animal-derived enzymes allows not only to diversify the assortment of cheeses on the market but also to solve ethical and economic issues. In addition, vegetable and microbial preparations meet the requirements of vegetarianism, halal, and kosher food, thus further opening the market.

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Identification of proteins from wild cardoon flowers (Cynara cardunculus L.) by a proteomic approach

Cited by 17 publications

References 43 publications

Proteins Identified from Saliva and Salivary Glands of the Chinese Gall Aphid Schlechtendalia chinensis

Proteins Identified from Saliva and Salivary Glands of the Chinese Gall Aphid Schlechtendalia chinensis

Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

Proteolytic Enzymes in Cheese Making

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