Extraction and partial characterization of a coagulant preparation from Silybum marianum flowers: its action on bovine caseinate

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 orig...

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Autores principales: Vairo Cavalli, Sandra Elizabeth, Claver, Santiago Pablo, Priolo de Lufrano, Nora Silvia, Natalucci, Claudia Luisa
Formato: Articulo
Lenguaje:Inglés
Publicado: 2005
Materias:
Biología
Aspartic proteolytic activity
Casein hydrolysis
Milk clotting
Rennet substitute
Sylibum marianum
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/153187
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-153187
record_format dspace
spelling I19-R120-10915-1531872023-10-09T14:58:23Z http://sedici.unlp.edu.ar/handle/10915/153187 Extraction and partial characterization of a coagulant preparation from Silybum marianum flowers: its action on bovine caseinate Vairo Cavalli, Sandra Elizabeth Claver, Santiago Pablo Priolo de Lufrano, Nora Silvia Natalucci, Claudia Luisa 2005 2023-05-18T15:09:48Z en Biología Aspartic proteolytic activity Casein hydrolysis Milk clotting Rennet substitute Sylibum marianum 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. Centro de Investigación de Proteínas Vegetales Articulo Articulo http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf 271-275
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Aspartic proteolytic activity
Casein hydrolysis
Milk clotting
Rennet substitute
Sylibum marianum
spellingShingle Biología
Aspartic proteolytic activity
Casein hydrolysis
Milk clotting
Rennet substitute
Sylibum marianum
Vairo Cavalli, Sandra Elizabeth
Claver, Santiago Pablo
Priolo de Lufrano, Nora Silvia
Natalucci, Claudia Luisa
Extraction and partial characterization of a coagulant preparation from Silybum marianum flowers: its action on bovine caseinate
topic_facet Biología
Aspartic proteolytic activity
Casein hydrolysis
Milk clotting
Rennet substitute
Sylibum marianum
description 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.
format Articulo
Articulo
author Vairo Cavalli, Sandra Elizabeth
Claver, Santiago Pablo
Priolo de Lufrano, Nora Silvia
Natalucci, Claudia Luisa
author_facet Vairo Cavalli, Sandra Elizabeth
Claver, Santiago Pablo
Priolo de Lufrano, Nora Silvia
Natalucci, Claudia Luisa
author_sort Vairo Cavalli, Sandra Elizabeth
title Extraction and partial characterization of a coagulant preparation from Silybum marianum flowers: its action on bovine caseinate
title_short Extraction and partial characterization of a coagulant preparation from Silybum marianum flowers: its action on bovine caseinate
title_full Extraction and partial characterization of a coagulant preparation from Silybum marianum flowers: its action on bovine caseinate
title_fullStr Extraction and partial characterization of a coagulant preparation from Silybum marianum flowers: its action on bovine caseinate
title_full_unstemmed Extraction and partial characterization of a coagulant preparation from Silybum marianum flowers: its action on bovine caseinate
title_sort extraction and partial characterization of a coagulant preparation from silybum marianum flowers: its action on bovine caseinate
publishDate 2005
url http://sedici.unlp.edu.ar/handle/10915/153187
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AT priolodelufranonorasilvia extractionandpartialcharacterizationofacoagulantpreparationfromsilybummarianumflowersitsactiononbovinecaseinate
AT natalucciclaudialuisa extractionandpartialcharacterizationofacoagulantpreparationfromsilybummarianumflowersitsactiononbovinecaseinate
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