Determination of Soy in Meat

1987 ◽  
Vol 70 (1) ◽  
pp. 85-90
Author(s):  
David B Berkowitz ◽  
Donald W Webert

Abstract A number of methods may be used for determining soy flour in meat products. Highly purified soy products are more difficult to determine because the nonprotein components used to quantify the flour are reduced. Immunoassays have been used to directly measure protein content of soy products. Immunological methods for determination of soy proteins in meat are complicated by changes in the structure of the soy proteins during processing. These changes alter the available epitopes, changing the immunoreactivity of soy proteins. The epitopes available are dictated by the details of the processing. Other workers circumvented this problem by denaturing the soy protein with urea and mercaptoethanol, and then removing these agents by dialysis; whatever the initial protein conformation, all soy samples came to the same final conformation after the denaturing agents were removed. The assay used antibody made against the "renatured protein." These steps made the assay long and laborious. Attempts to develop a rapid assay were complicated by the same protein denaturation problems. Sodium dodecylsulfate gel electrophoresis coupled with immunoblotting may be the best quantitative approach.

1987 ◽  
Vol 70 (3) ◽  
pp. 582-587
Author(s):  
James H Rittenburg ◽  
Alexandra Adams ◽  
John Palmer ◽  
John C Allen

Abstract An Indirect, Competitive Enzyme-Linked Immunosorbent Assay (Elisa) Has Been Developed For Quantitation Of Soy Protein In Meat Products. The Methodology Allows Rapid Aqueous Extraction Of Meat Samples Into A Liquid Form Suitable For Assay. The Assay Is Highly Specific For Soy Protein And Is Designed To Measure Soy Protein Levels Between 1 And 10% Of The Wet Weight Of The Sample. Standardized, Stabilized Reagents For Carrying Out The Procedure Are Commercially Available In A Kit. The Analysis, Including Sample Preparation, Can Be Completed Within A Workday, And The Actual Immunoassay In Less Than 60 Min.


Holzforschung ◽  
2012 ◽  
Vol 66 (7) ◽  
pp. 857-862 ◽  
Author(s):  
Guangbo He ◽  
Martin Feng ◽  
Chunping Dai

Abstract Soy-based resins have recently attracted great attention as adhesives in the wood composite industry. This article is focusing on hydrolysis and modification of soy protein concentrates to formulate soy-based resins for wood composites. The soy-based resins have been evaluated in terms of bondability on wood substrates and bonding performance in plywood products. The performance of plywood was found to meet the relevant CSA standard (Canadian Standard Association) requirements under both of dry and wet conditions, if the soy-based resins were obtained from low hydrolyzed soy flour. Hydrolysis is an effective and efficient tool for reducing the viscosity of soy resins. However, hydrolysis also reduces the bond strength of soy-based resins as hydrolysis cleaves the macromolecules of soy proteins into smaller molecules. Modified soy-based resins have a certain potential for production of interior- and exterior-used plywood.


2009 ◽  
Vol 27 (No. 4) ◽  
pp. 234-239 ◽  
Author(s):  
J. Vaňha ◽  
A. Hinková ◽  
M. Sluková ◽  
F. Kvasnička

The Czech legislation (Decrees No. 326/2001, 202/2003 and 651/2004 of the law No. 110/1997 as amended) regulates the requirements for the selected meat products with regard to the contents of individual ingredients. However, the methods of the determination of compliance with these regulations are not closely specified. The study presented here deals with the development and verification of analytical methods suitable for the detection of the material of plant origin. Due to the high variability in the contents in meat products of these ingredients, various markers were observed (isoflavones, phytic acid, galactooligosaccharides). For the purpose of detection, substances commonly used in food processing industries were taken into account such as soy flour, wheat flour, soy isolate, HAM 60 preparation. The values gained by measuring the given markers were subsequently converted to reflect the amount of the plant based substance added. Out of 18 products commonly available in shops, only 7 filfilled the legal criteria.


1995 ◽  
Vol 41 (5) ◽  
pp. 731-738 ◽  
Author(s):  
M Nauck ◽  
K Winkler ◽  
C Wittmann ◽  
H Mayer ◽  
C Luley ◽  
...  

Abstract Lipoprotein(a) [(Lp(a)], a low-density lipoprotein (LDL)-like particle, contains in addition to LDL a specific protein component, apolipoprotein(a) [apo(a)]. Conventionally, Lp(a) has been measured by immunological methods that distinguish between Lp(a) and LDL by dealing with apo(a) as an antigen. We describe a new method to determine Lp(a) on the basis of its cholesterol content. Very-low-density lipoproteins were removed from serum by preparative ultracentrifugation at a density of 1.006 kg/L. The infranate was subjected to agarose gel electrophoresis to separate Lp(a) and LDL. Lp(a) cholesterol was then determined by direct enzymatic staining for cholesterol. On electrophoresis of the > 1.006 kg/L (bottom) fraction, Lp(a) migrates to the pre-beta position, regardless of the genetic apo(a) isoform. The interassay CVs of Lp(a) cholesterol determinations ranged from 6.9% to 11.5%, and the results correlated well with the Lp(a) concentrations measured by immunonephelometry (r = 0.937). There was an inverse relation between the molecular mass of the genetically determined apo(a) isoforms and Lp(a) cholesterol concentrations. Patients with angiographically proven coronary artery disease (CAD) had significantly more Lp(a) cholesterol than healthy controls did. The ratio of Lp(a) cholesterol to immunologically determined Lp(a) tended to be lower in CAD patients, suggesting that Lp(a) particles contained less cholesterol than apo(a). In addition, the new method allows determination of LDL cholesterol without contamination by Lp(a).


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