Renneting is an enzymatic process that turns milk into curd which is then transformed into cheese. Rennet-induced coagulation of caseins (CNs) is the critical step during this process and the key is the primary hydrolysis of κ-CN's Phe-Met bond by chymosin. This article comprehensively reviews the existing data on the extent/degree of κ-CN hydrolysis during renneting of bovine milk and critically evaluates its determination methods. The data show that under normal cheese-making conditions, milk gelation occurs at a degree of κ-CN hydrolysis <80%, which varies due to several factors including analytical and estimation approaches. The common approach involves isolating the macropeptides released, by precipitating whey proteins and residual CN in 1%-12% trichloroacetic acid (TCA), then assuming that the maximum amount obtained is 100% κ-CN hydrolysis. The drawback is that the estimated degree of κ-CN hydrolysis may be higher than the actual value as TCA partially precipitates the macropeptide fractions. Moreover, macropeptide isolation seems unnecessary based on current advances in chromatographic and electrophoretic techniques. The present work proposes a simple mass balance-based approach that will provide accurate estimates in future studies. The accuracy of measuring the degree of κ-CN hydrolysis has implications on the precision of the data in relation to its partitioning (% distribution between the curd and whey) which is essential for improving whey quality.
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http://dx.doi.org/10.1002/fsn3.3868 | DOI Listing |
Foods
November 2024
Biological Research Institute, National Scientific and Technical Research Council (CONICET), University of Mar del Plata (UNMDP), Mar del Plata 7600, Argentina.
Food Sci Nutr
March 2024
Advanced Food Systems Research Unit, Institute for Sustainable Industries and Liveable Cities, College of Health and Biomedicine Victoria University Melbourne Victoria Australia.
Renneting is an enzymatic process that turns milk into curd which is then transformed into cheese. Rennet-induced coagulation of caseins (CNs) is the critical step during this process and the key is the primary hydrolysis of κ-CN's Phe-Met bond by chymosin. This article comprehensively reviews the existing data on the extent/degree of κ-CN hydrolysis during renneting of bovine milk and critically evaluates its determination methods.
View Article and Find Full Text PDFCell Mol Biol (Noisy-le-grand)
December 2023
Livestock and Wild Life Laboratory, Arid Lands Institute (IRA), University of Gabes, Medenine, 4119, Tunisia.
Camel milk transformation into cheese remains an objective to be improved today. This study aimed to improve camel milk clotting using a crude extract from green pods of carob as a substitute for commercial rennet. The composition of the crude carob extract was determined for dry matter and protein content.
View Article and Find Full Text PDFFood Technol Biotechnol
September 2023
Department of Basic and Experimental Sciences, National University of the Northwest of the Province of Buenos Aires (UNNOBA), Newbery 355, 6000 Junín, Buenos Aires, Argentina.
Research Background: A few studies have investigated enzymes as a substitute for calf rennet in cheese making. They used aqueous extracts prepared by maceration of plant material and stored by freezing. However, it was indicated that lyophilisation is a better alternative to preserve the coagulant properties of plant extracts over a longer period of time, as it is a more controllable, stable and hygienic alternative with a better shelf life that is easier to transport, store and standardise.
View Article and Find Full Text PDFFoods
June 2023
Department of Food Engineering and Machines, University of Life Sciences in Lublin, Głęboka 28, 20-612 Lublin, Poland.
The purpose of this study was to evaluate the caseinolytic and milk-clotting activities of aqueous crude extracts from leaves and latex of the , to determine their suitability as a rennet substitute. These extracts were subjected to a series of biochemical tests before being used in the production of cheese. The results showed that the enzymatic latex extract had a higher coagulant activity than the leaf extract.
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