Determination of chymosin and bovine pepsin A activity in combined rennets on the basis of immunochemical inhibition

1989 ◽  
Vol 56 (4) ◽  
pp. 631-637 ◽  
Author(s):  
Eva Beránková ◽  
Pavel Rauch ◽  
Jan Káš
Keyword(s):  
Residual Activity ◽  
Specific Inhibition ◽  
Milk Clotting ◽  
The Difference ◽  
Milk Clotting Activity

SummaryThe milk clotting activity of chymosin in combined rennets was determined as the difference between the total and residual activity after specific inhibition of chymosin with the purified immunoglobulin fraction of chymosin antiserum. The milk clotting activity of bovine pepsin A was assessed in a similar manner. In bovine rennets milk clotting activity of chymosin was measured directly after immunochemical inactivation of bovine pepsin A. Any method may be used for the determination of milk clotting activity. High correlation was found between the proposed method, which is simple and rapid to perform, and Chromatographic assay.

Indirect assay of milk clotting activity of Mucor miehei proteinase (Fromase) in combined rennets

1987 ◽  
Vol 54 (3) ◽  
pp. 407-412 ◽  
Author(s):  
Eva Beránková ◽  
Pavel Rauch ◽  
Jan Káš ◽  
Vladimír Hušek ◽  
Eduard Paluska
Keyword(s):  
Blood Serum ◽  
Proteinase Inhibitors ◽  
Residual Activity ◽  
Total Activity ◽  
Mucor Miehei ◽  
Milk Clotting ◽  
The Difference ◽  
Indirect Assay ◽  
Milk Clotting Activity

SummaryMilk clotting activity of Mucor miehei proteinase (commercial name Fromase) was determined in combined rennets as the difference between the total activity of combined rennet and the residual activity after inhibition of Fromase by the purified immunoglobulin fraction of a Fromase antiserum. The proposed method is simple, rapid, and makes possible the use of any arbitrary method for assaying milk clotting activity. The application of the immunoglobulin fraction, instead of the whole antiserum, is necessary owing to the presence of nonspecific proteinase inhibitors in blood serum.

A two-tube immunochemical method for determination of CK-MB isoenzyme in serum evaluated

1990 ◽  
Vol 36 (3) ◽  
pp. 550-553
Author(s):  
M Panteghini ◽  
R Bonora ◽  
F Pagani
Keyword(s):  
Adenylate Kinase ◽  
Residual Activity ◽  
Peak Activity ◽  
Linear Regression Equation ◽  
Immunochemical Method ◽  
Electrophoretic Method ◽  
Analytical Recovery ◽  
The Difference ◽  
Commercial Kit

Abstract A new commercial kit (Impres-MB; International Immunoassay Labs.) recently was introduced for measuring the MB isoenzyme of creatine kinase (CK-MB) based on the use of monoclonal antibodies. After antibodies to CK-MM isoenzyme are added to precipitate the CK-MM, antibodies to CK-M monomer are added to precipitate the M-subunit isoenzymes of CK. Subtracting the enzymatic activity of the second supernate from the residual activity in the first yields the activity of CK-MB. Results are not affected by CK-BB, mitochondrial CK, or adenylate kinase. However, the anti-CK-MM antibodies precipitated only about 98% of serum CK-MM and may have partly precipitated CK-MB isoenzyme (average analytical recovery of CK-MB, 86.6%). Comparison between Impres-MB (y) and electrophoresis (x) yielded the following linear-regression equation: y = 0.79x + 3 (r = 0.982, n = 97). Data for CK-MB temporal kinetics, obtained from patients with myocardial infarction, correlated significantly in both methods; however, peak activity values of CK-MB were significantly different, confirming that the difference between the new method and the electrophoretic method average 20%.

Measurement of milk clotting activity by rotational viscometry

2011 ◽  
Vol 78 (2) ◽  
pp. 191-195 ◽  
Author(s):  
Mandy Jacob ◽  
Martin Schmidt ◽  
Doris Jaros ◽  
Harald Rohm
Keyword(s):  
Standard Method ◽  
Small Amplitude ◽  
Clotting Time ◽  
Milk Clotting ◽  
Rotational Viscometry ◽  
Milk Gelation ◽  
Reconstituted Milk ◽  
Flocculation Time ◽  
Milk Clotting Activity

Standard method for the determination of the activity of milk coagulants is the rotating bottle method, where clotting time is defined as the time when visually observable flocculation starts. Aim of this study was to verify whether it is possible to determine milk clotting time by rotational viscometry. Using three different coagulants and reconstituted milk of different pH and temperature, flocculation time and viscosity in steady shear was determined, and milk gelation was monitored by small amplitude oscillating shear rheometry. The results show that, independent of pH and temperature, milk clotting time is related to an apparent viscosity of 7·24±0·45 mPa.s, indicating that rotational viscometry can be used for the screening of flocculation time with an accuracy of approximately 6%.

scholarly journals Characteristics of Curds With Milk Clotting Enzyme from Indonesian Local Isolate of Lactic Acid Bacteria

2020 ◽  
Vol 1 (2) ◽  
pp. 79-86
Author(s):  
Wendry Putranto ◽  
Apon Mustopa ◽  
Jendri Mamangkey ◽  
Netty Aritonang
Keyword(s):  
Enzyme Activity ◽  
Ammonium Sulfate ◽  
Observational Research ◽  
Ammonium Sulfate Precipitation ◽  
Fermentation Time ◽  
Milk Clotting ◽  
Milk Clotting Enzyme ◽  
Qualitative Observation ◽  
Milk Clotting Activity

To get the potential of lalcat acid bacteria isolate to produce Milk Clotting Enzyme (MCE), it is necessary to screen milk clotting activity both quantitatively and qualitatively. Through qualitative observation, the characteristics of the curd resulting from enzyme activity can be obtained. MCE is a protease that has the characteristics of milking. Based on the results of this observational research, the curd characteristic produced can be used as a benchmark to determine the length of time of fermentation and optimization of the determination of ammonium sulfate precipitation concentration. Isolate BAL shows the results of a compact curd at a fermentation time of 25 hours at 37 ℃ and the optimization results of the deposition of ammonium sulfate which shows the characteristics of a compact curd by 45% ammonium sulfate.

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