Rennet
Rennet structure
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Common Name | Rennet | ||
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| CAS Number | 9042-08-4 | Molecular Weight | 181.028 | |
| Density | 1.4±0.1 g/cm3 | Boiling Point | 179.0±0.0 °C at 760 mmHg | |
| Molecular Formula | C5H9BrO2 | Melting Point | N/A | |
| MSDS | USA | Flash Point | 79.4±0.0 °C | |
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Starch addition in renneted milk gels: Partitioning between curd and whey and effect on curd syneresis and gel microstructure
J. Dairy Sci. 95(12) , 6871-81, (2012) Milk gels were made by renneting and acidifying skim milk containing 5 different starches, and then compressed by centrifugation to express whey and simulate curd syneresis during the manufacture of low-fat cheese. A series of 17 starches were examined, with ... |
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Effect of soluble calcium on the renneting properties of casein micelles as measured by rheology and diffusing wave spectroscopy.
J. Dairy Sci. 95(1) , 75-82, (2012) Addition of calcium chloride to milk has positive effects on cheese-making because it decreases coagulation time, creates firmer gels, and increases curd yield. Although addition of calcium chloride is a widely used industrial practice, the effect of soluble ... |
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Modeling rennet coagulation time and curd firmness of milk
J. Dairy Sci. 94(12) , 5821-32, (2011) Milk coagulation properties (MCP) are traditionally expressed using rennet coagulation time (RCT), time to curd firmness (CF) of 20mm (k20), and CF 30min after enzyme addition (a30) values, all of which are single-point measures taken from the output of compu... |
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Effect of fat content and homogenization under conventional or ultra-high-pressure conditions on interactions between proteins in rennet curds.
J. Dairy Sci. 95(9) , 4796-803, (2012) The objective of this study was to investigate the influence of conventional and ultra-high-pressure homogenization on interactions between proteins within drained rennet curds. The effect of fat content of milk (0.0, 1.8, or 3.6%) and homogenization treatmen... |
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Encapsulation of probiotic bacteria in lamb rennet paste: Effects on the quality of Pecorino cheese
J. Dairy Sci. 95(7) , 3489-500, (2012) Lamb rennet pastes containing encapsulated Lactobacillus acidophilus and a mix of Bifidobacterium longum and Bifidobacterium lactis were produced for Pecorino cheese manufacture from Gentile di Puglia ewe milk. Cheeses were denoted as RP cheese when made with... |
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Real-time visual/near-infrared analysis of milk-clotting parameters for industrial applications.
Animal 6(7) , 1170-7, (2012) The economical profitability of the dairy industry is based on the quality of the bulk milk collected in the farms, therefore it was based on the herd level rather than on the individual animals at real time. Udder infection and stage of lactation are directl... |
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Formation of early and advanced Maillard reaction products correlates to the ripening of cheese.
J. Agric. Food Chem. 60(2) , 600-7, (2012) The present study deals with the characterization of the ripening of cheese. A traditional German acid curd cheese was ripened under defined conditions at elevated temperature, and protein and amino acid modifications were investigated. Degree of proteolysis ... |
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Free amino acid content of goat's milk cheese made with animal rennet and plant coagulant.
J. Sci. Food Agric. 92(8) , 1657-64, (2012) Enzymes present in the flowers of Cynara cardunculus (cyprosins) are used in the production of some traditional Spanish and Portuguese cheeses, replacing animal rennet. The aim of this work was to study the changes that take place in free amino acids during t... |
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Kappa-casein based electrochemical and surface plasmon resonance biosensors for the assessment of the clotting activity of rennet.
Anal. Chim. Acta 712 , 132-7, (2012) We report for the first time the development of kappa-casein (κ-CN)-based electrochemical and surface plasmon resonance (SPR) biosensors for the assessment of the clotting activity of rennet. Electrochemical biosensors were developed over gold electrodes modi... |
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Effect of heat treatment of rennet skim milk induced coagulation on the rheological properties and molecular structure determined by synchronous fluorescence spectroscopy and turbiscan.
Food Chem. 135 , 1809-17, (2012) Heat treatment applied to milk induces denaturation of whey proteins, leading to a complex mixture of whey protein and whey protein coated casein micelles. The present paper investigates the effects of heat treatment (60 and 80°C during 20min) and rennet-indu... |