Novel assay for the determination of residual coagulant activity in cheese

Hurley, Michael J.; O'driscoll, B.; Kelly, Alan L.; McSweeney, P.L.H.

doi:10.1016/s0958-6946(99)00118-1

Cited by 50 publications

(53 citation statements)

References 10 publications

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“…As discussed in Sect. 12.2.2.5, the Formograph gives a measure of the gel strength but the data cannot be readily converted to rheological 12 Principle of a method used to measure chymosin activity using a synthetic sevenresidue peptide substrate containing a chymosin-susceptible Phe-Phe bond (Hurley et al 1999).…”

Section: Gel Strength (Curd Tension)mentioning

confidence: 99%

Chemistry and Biochemistry of Cheese

Fox

Uniacke‐Lowe

McSweeney

et al. 2015

Dairy Chemistry and Biochemistry

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Section: Gel Strength (Curd Tension)mentioning

confidence: 99%

Chemistry and Biochemistry of Cheese

Fox

Uniacke‐Lowe

McSweeney

et al. 2015

Dairy Chemistry and Biochemistry

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“…The method used was based on the method of Hurley et al (1999) used also by Bansal et al (2007Bansal et al ( , 2009. Briefly, 500 mg of grated cheese were dispersed in 1 mL of 0.2 mmol.L −1 trisodium citrate buffer pH 7.0 and then incubated at 37°C for 30 min under periodical stirring.…”

Section: Measurement Of Residual Coagulant Activitymentioning

confidence: 99%

“…After incubation at 37°C for 6 h the enzymatic reaction was terminated by heat treatment at 70°C for 10 min. The assay mixture was centrifuged at 16,000×g for 10 min and 100 μL of the supernatant filtered through 0.45 μm filter paper was analyzed using a C8 RPcolumn 4.6×250 mm, 5 μm particle size, 300Å pore size (Macherey-Nagel, Düren, Germany) by the elution method reported by Hurley et al (1999). For the determination of the retention time of the substrate, assays including substrate without cheese extract or substrate incubated with rennet were carried out.…”

Section: Measurement Of Residual Coagulant Activitymentioning

confidence: 99%

“…The first studies about residual chymosin activity in cheese were mainly about the partition of the enzymes between curd and whey and showed that the most important factors are the type of rennet, thermal treatment of the curd, and pH during drainage (Guinee and Wilkinson 1992). During the last years, an enzymatic method specific for aspartic proteinases (Hurley et al 1999) has been added to the methods used for the determination of residual chymosin in cheese (Baer and Collin 1993). Using this method, recent studies have been published about the factors that affect the retention of rennet in cheese curd and the residual coagulant activity in different cheese varieties in relation to cheesemaking technology (Bansal et al 2007(Bansal et al , 2009.…”

Section: Introductionmentioning

confidence: 99%

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Proteolysis and related enzymatic activities in ten Greek cheese varieties

Nega

Moatsou

2011

Dairy Science & Technol.

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The objective of this study was to assess indices of proteolysis and related enzymatic activities of various cheese varieties produced in Greece. Physicochemical composition, extent of proteolysis (nitrogen fraction and reversed-phase high-performance liquid chromatography (RP-HPLC) profiles of cheese soluble fraction) and residual chymosin and plasmin activities were analyzed in 57 commercial samples, grouped according to cheesemaking technologies. The mean values of soluble nitrogen fraction on total nitrogen and trichloroacetic acid-soluble nitrogen fraction on total nitrogen did not differ significantly between the different cheese varieties, with mean values of 16.03% and 9.97%, respectively. Brined cheeses had the highest mean residual chymosin activity 0.166 International Milk Clotting units (IMCU).g −1 of cheese dry matter and the lowest mean plasmin plus plasminogen-derived activity 3.88 U.g −1 of cheese. The respective values for Gruyère and hard type cheeses were 0.029 and 0.047 IMCU.g −1 of cheese dry matter for chymosin and 6.22 and 6.94 U.g −1 of cheese for plasmin. It was interesting that both enzymatic activities were high in pasta filata type cheeses, i.e., respective mean values of 0.086 IMCU. g −1 of cheese dry matter and 7.42 U.g −1 of cheese. Intermediate regions on the RP-HPLC profiles were positively correlated with residual chymosin activity and negatively correlated with plasmin activity. It was concluded that cooking at pH close to cheesemilk pH and pressing are the most important technological factors both for proteolysis and activity of major proteolytic enzymes in various cheese varieties.

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“…An aqueous phase extract of each cheese sample was prepared (Hurley et al 1999). The heptapeptide (30 μL, 1 mg.mL −1 ) Pro-Thr-Glu-Phe-[NO 2 -Phe]-Arg-Leu (Bachem, Bubendorf, Switzerland) was mixed with sodium formate buffer (200 μL, 0.1 mol.L −1 , pH 3.2, 0.05% sodium azide (Chem-Supply, Gillman, Australia)) and the aqueous cheese extract (70 μL).…”

Section: Residual Rennet In the Fresh Cheesementioning

confidence: 99%

Effect of rennet on the composition, proteolysis and microstructure of reduced-fat Cheddar cheese during ripening

Soodam

Ong

Powell

et al. 2015

Dairy Sci. & Technol.

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Rennet is an important ingredient in Cheddar cheese manufacturing and both the type used and the concentration applied can affect the ripening process. In this work, reduced-fat Cheddar cheese was produced using different concentrations of microbial rennet (Hannilase; 0.026, 0.052 and 0.150 international milk clotting units (IMCU).g −1 of milk) as well as recombinant camel chymosin (0.052 IMCU.g −1 of milk). The composition of the resulting cheeses was not statistically different, but the ratio of pH 4.6 soluble nitrogen/total nitrogen (pH 4.6-SN/TN) increased significantly with increasing Hannilase rennet concentration. This ratio was also significantly lower in the cheese made with recombinant camel chymosin at a similar rennet concentration. Microstructural, biochemical and textural changes in the cheese were also monitored during ripening. The gel made with a high rennet concentration was qualitatively more porous but these changes in porosity were not reflected in the freshly pressed cheese. After 31 weeks of ripening, the cheese made with recombinant camel chymosin had a thicker protein network compared to the cheese made with microbial rennet (Hannilase), possibly due to lower proteolysis. Most of the Hannilase rennet was lost to the whey when the rennet was increased above the concentration of 0.052 IMCU.g as the texture was not significantly affected at the end of the observed ripening period. Recombinant camel chymosin may potentially be used as a substitute for products requiring lower proteolysis during ripening. However, the texture of this cheese was harder than the cheese made with Hannilase rennet at the end of the ripening period.

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Novel assay for the determination of residual coagulant activity in cheese

Cited by 50 publications

References 10 publications

Chemistry and Biochemistry of Cheese

Chemistry and Biochemistry of Cheese

Proteolysis and related enzymatic activities in ten Greek cheese varieties

Effect of rennet on the composition, proteolysis and microstructure of reduced-fat Cheddar cheese during ripening

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