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Influence of chymosin type and curd scalding temperature on proteolysis of hard cooked cheeses

Published online by Cambridge University Press:  16 April 2015

Luciana M. Costabel ,
Carina V. Bergamini ,
Leila Pozza ,
Facundo Cuffia ,
Mario C. Candioti  and
Erica Hynes
Luciana M. Costabel*
Affiliation:
Instituto Nacional de Tecnología Agropecuaria (INTA), Estación Experimental Agropecuaria Rafaela, Ruta 34 km 227, 2300, Rafaela. Santa Fe, Argentina
Carina V. Bergamini
Affiliation:
Instituto de Lactología Industrial, Universidad Nacional del Litoral – Consejo Nacional de Investigaciones Científicas y Técnicas, Santa Fe, Argentina
Leila Pozza
Affiliation:
Instituto de Lactología Industrial, Universidad Nacional del Litoral – Consejo Nacional de Investigaciones Científicas y Técnicas, Santa Fe, Argentina
Facundo Cuffia
Affiliation:
Instituto de Lactología Industrial, Universidad Nacional del Litoral – Consejo Nacional de Investigaciones Científicas y Técnicas, Santa Fe, Argentina
Mario C. Candioti
Affiliation:
Instituto de Lactología Industrial, Universidad Nacional del Litoral – Consejo Nacional de Investigaciones Científicas y Técnicas, Santa Fe, Argentina
Erica Hynes
Affiliation:
Instituto de Lactología Industrial, Universidad Nacional del Litoral – Consejo Nacional de Investigaciones Científicas y Técnicas, Santa Fe, Argentina Facultad de Ingeniería Química, Universidad Nacional del Litoral, Santa Fe, Argentina
*
*For correspondence; e-mail: costabel.luciana@inta.gob.ar
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Abstract

In this work, we studied the influence of the type of coagulant enzyme and the curd scalding temperature on the proteolysis and residual coagulant and plasmin activities of a cooked cheese, Reggianito, in the interest of reducing ripening time. A two-factor experimental design was applied in two levels: type of coagulant enzyme, bovine chymosin or camel chymosin, and curd scalding temperature, 50 or 56 °C. The experimental treatments were applied in Reggianito cheese making experiments, and the samples were ripened for 90 d at 12 °C. Scalding temperature influenced residual coagulant activity; the cheeses cooked at 50 °C had significantly higher activity than those treated at 56 °C. In contrast, scalding temperature did not modify plasmin activity. Proteolysis was primarily affected by curd cooking temperature because chymosin-mediated hydrolysis of αs1 casein was slower in cheeses treated at 56 °C. Additionally, the nitrogen content in the cheese soluble fractions was consistently lower in the cheeses scalded at 56 °C than those cooked at 50 °C. A significant influence of the type of coagulant enzyme was observed, especially in the nitrogen fractions and peptide profiles, which demonstrated that camel chymosin was slightly less proteolytic; however, these differences were lower than those caused by the scalding temperature.

Keywords

Camel chymosinbovine chymosinresidual coagulant activityscalding temperatureproteolysis

Information

Type
Research Article
Information
Journal of Dairy Research , Volume 82 , Issue 3 , August 2015 , pp. 375 - 384
Copyright
Copyright © Proprietors of Journal of Dairy Research 2015 

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