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dc.date.accessioned 2023-05-18T15:09:48Z
dc.date.available 2023-05-18T15:09:48Z
dc.date.issued 2005
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/153187
dc.description.abstract An outstanding parameter in cheese making is the type of coagulant, which greatly influences the characteristics of the final products. Proteolysis is the most important set of biochemical changes during ripening of most cheeses, and is carried out, in different magnitude, by proteolytic agents originated in milk, rennet (or rennet substitute), and starter and non-starter micro-organisms (Silva & Malcata, 2000). The demand for alternative sources of milk coagulants, to replace the expensive and limited natural rennet supplies, has increased (Esteves et al. 2001). All commercial enzymes employed as milk coagulant are aspartic proteinases, which are most active at acidic pH and preferentially cleave peptide bonds between residues with hydrophobic side-chains (Silva & Malcata, 1999). Because of the presence of aspartic proteinases, aqueous crude extracts from flowers of Cynara cardunculus (Verı´ssimo et al. 1995, 1996), Cynara humilis, and/or Cynara scolymus are traditionally employed in the Iberian Peninsula as vegetable rennet for cheesemaking (Reis et al. 2000). Milk clotting activity was also proved in flowers of Centaurea calcitrapa and Onopordum turcicum (Tamer, 1993; Domingos et al. 1998). All these species are included within the Asteraceae family and furthermore in the same tribe : Cardueae Cass.=Cynareae Less. (Ariza Espinar & Delucchi, 1998). When a potential rennet substitute is studied, it is particularly important to evaluate adequately the degradation patterns of the caseins because of their effects on yield, consistency, and flavour of the final cheese (Fox, 1989). It is important to guarantee a well-balanced breakdown of curd proteins (caseins) in order to avoid formation of undesired attributes in cheese such as low viscosity and high bitterness (Visser, 1993). One of the most frequently used methods to monitor proteolytic processes on caseins is urea-polyacrylamide gel electrophoresis. On the other hand, tricine-SDS polyacrylamide gel electrophoresis improves the separation, identification and quantification of casein hydrolysates because it allows the visualization of large and small peptides (Pardo & Natalucci, 2001), with the additional advantage of allowing the estimation of molecular masses. Both methods are then suitable to characterize the performance of vegetable rennet in different ways. This preliminary study had the following objectives: the partial characterization of (i) the aspartic proteolytic activity present in flowers of Silybum marianum (L.) Gaertn. (Asteraceae); and (ii) the hydrolytic profile of bovine caseins. en
dc.format.extent 271-275 es
dc.language en es
dc.subject Aspartic proteolytic activity es
dc.subject Casein hydrolysis es
dc.subject Milk clotting es
dc.subject Rennet substitute es
dc.subject Sylibum marianum es
dc.title Extraction and partial characterization of a coagulant preparation from Silybum marianum flowers: its action on bovine caseinate en
dc.type Articulo es
sedici.identifier.other https://doi.org/10.1017/S0022029905000749 es
sedici.identifier.issn 1469-7629 es
sedici.creator.person Vairo Cavalli, Sandra Elizabeth es
sedici.creator.person Claver, Santiago Pablo es
sedici.creator.person Priolo de Lufrano, Nora Silvia es
sedici.creator.person Natalucci, Claudia Luisa es
sedici.subject.materias Biología es
sedici.description.fulltext true es
mods.originInfo.place Centro de Investigación de Proteínas Vegetales es
sedici.subtype Articulo es
sedici.rights.license Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by-nc-sa/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle Journal of Dairy Research es
sedici.relation.journalVolumeAndIssue vol. 72, no. 3 es


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Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) Except where otherwise noted, this item's license is described as Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)