Automated enzymatic determination of starch in meat products

1982 ◽  
Vol 174 (4) ◽  
pp. 274-277
Author(s):  
Nel Haagsma ◽  
Joost W. Melten ◽  
Betty G. M. Gortemaker
1991 ◽  
Vol 74 (6) ◽  
pp. 921-925 ◽  
Author(s):  
M Tapani Hattula ◽  
Harriet C Wallin ◽  
◽  
R Andersen ◽  
K Blomberg ◽  
...  

Abstract An enzymatic method for the determination of free glutamic acid in meat products and dried soups was collaboratively studied in 11 laboratories. In the presence of the enzyme glutamate dehydrogenase, L-giutamic acid is oxidatively deaminated by nicotinamide adenine dinucleotide (NAD) to 2-oxoglutarate. In a reaction catalyzed by diaphorase, the NADH thus formed converts 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride to a formazan, which is measured in the visible range at 492 nm. Fourteen samples (7 samples of minced sausage and 7 samples of dried cauliflower soup) with glutamate contents varying between 0.4 and 16 g/kg were included In the study. Materials were distributed to participants as blind duplicates and as split level pairs. The mean relative standard deviation (RSDR) for reproducibility for the dried soup material containing glutamate between 7 and 16 g/kg was 4.6%. RSDR values for samples of minced sausage containing glutamate at lower levels (0.4-1.3 g/kg) were between 12 and 16%.


1997 ◽  
Vol 80 (3) ◽  
pp. 584-590 ◽  
Author(s):  
Antti Mustranta ◽  
Carola Östman ◽  
I Aminoff ◽  
P Baardseth ◽  
E Eklund ◽  
...  

Abstract Enzymes are widely used in food chemistry as analytical tools. An enzymatic method for determining lactose and galactose in foods was evaluated in an interlaboratory methods performance study by 12 laboratories in 4 countries. The method is based on enzymatic hydrolysis of lactose and enzymatic oxidation of the hydrolysis products. The exchange of the coenzyme in the second reaction is the basis of quantitation. The method may be used for various types of foods, such as liquid and solid milk products, meat products, cereal products, fats, dressings, sweets, chocolate, and foods for special dietary uses. It is also applicable to lactose-free foods but not to products in which lactose has been partially hydrolyzed enzymatically to glucose and galactose. Six commonly used foodstuffs with lactose concentrations ranging from 0.4 g/100 g to 40 g/100 g and galactose concentrations up to 0.7 g/100 g were analyzed: crisp rye bread, milk chocolate, sausage, cheese, margarine, and baby food containing milk powder. They were distributed to the 12 participants as 12 randomly numbered test samples, representing blind duplicates of the 6 materials. The relative standard deviations for reproducibility (RSDR) were between 2.3-11% for lactose and 6.8-50% for galactose.


1963 ◽  
Vol 41 (5) ◽  
pp. 265-268 ◽  
Author(s):  
Thomas J Cook ◽  
Allan L Lorincz ◽  
Alan R Spector

1983 ◽  
Vol 29 (8) ◽  
pp. 1513-1517 ◽  
Author(s):  
M W McGowan ◽  
J D Artiss ◽  
B Zak

Abstract A procedure for the enzymatic determination of lecithin and sphingomyelin in aqueous solution is described. The phospholipids are first dissolved in chloroform:methanol (2:1 by vol), the solvent is evaporated, and the residue is redissolved in an aqueous zwitterionic detergent solution. The enzymatic reaction sequences of both assays involve hydrolysis of the phospholipids to produce choline, which is then oxidized to betaine, thus generating hydrogen peroxide. The hydrogen peroxide is subsequently utilized in the enzymatic coupling of 4-aminoantipyrine and sodium 2-hydroxy-3,5-dichlorobenzenesulfonate, an intensely red color being formed. The presence of a non-reacting phospholipid enhances the hydrolysis of the reacting phospholipid. Thus we added lecithin to the sphingomyelin standards and sphingomyelin to the lecithin standards. This precise procedure may be applicable to determination of lecithin and sphingomyelin in amniotic fluid.


2019 ◽  
Vol 11 (30) ◽  
pp. 3866-3873 ◽  
Author(s):  
R. Karthikeyan ◽  
D. James Nelson ◽  
S. Abraham John

Selective and sensitive determination of one of the purine nucleotides, inosine (INO) using a low cost carbon dot (CD) modified glassy carbon (GC) electrode in 0.2 M phosphate buffer solution (pH 7.2) was demonstrated in this paper.


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