Lysinoalanine Determination in Proteins Using High‐pressure Liquid Chromatography

Wood-Rethwill, J. C.; Warthesen, J. J.

doi:10.1111/j.1365-2621.1980.tb07579.x

Cited by 12 publications

(2 citation statements)

References 28 publications

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“…Recently the technique of high-pressure liquid chromatography has been shown to function in the detection of LAL (Wood-Rethwill and Warthesen, 1980). Basically, the dansyl derivative of LAL is formed and measured.…”

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confidence: 99%

Lysinoalanine in foods

Maga¹

1984

J. Agric. Food Chem.

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The formation of lysinoalanine has been primarily associated with the alkaline treatment or heat processing of proteins. The chemistry, food occurrences, nutritional significance, and methods available for the analysis of this phenomenon, relative to the literature, are discussed.Lysinoalanine (LAL) [JV'-(DL-2-amino-2-carboxyethyl)-L-lysine] represents a unique amino acid that apparently has been present in our food supply for centuries, especially in products that undergo alkaline processing and/or heating of a protein-containing food. In addition, Gross et al. (1975) report that LAL is a natural constituent of cinnamycin and duramycin, which are two peptides present in certain species of Streptomyces.However, it was not until the mid 1960s that LAL was actually identified (Patchornik and Sokolovsky, 1964b;Bohak, 1964). Since that time numerous studies have been reported in an attempt to more completely understand its formation mechanism(s), ways of minimizing its formation, and levels present in foods and, most importantly, to identify its specific nutritional and potential toxicological significance relative to food processing and preparation. Several reviews have appeared that discuss certain aspects of the above (Sternberg and Kim, 1977;de Groot et al., 1977;Struthers, 1981), but no review has attempted to provide an inclusive overview of the entire subject. Thus, the primary objective of this review is to more extensively discuss the literature to date in an effort to summarize our knowledge of LAL in food and to point out areas that need further investigation or clarification.

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Lysinoalanine in foods

Maga¹

1984

J. Agric. Food Chem.

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“…It is well known that LAL reacts with dansyl chloride to form a fluorescent product which can be determined by liquid chromatography with fluorimetric detector [ 25 ]. Recently this method was also employed by Karami et al [ 26 ] to determine LAL in infant formula.…”

Section: Nonreference Methods Based On Single Thermal Treatment Inmentioning

confidence: 99%

New Trends for the Evaluation of Heat Treatments of Milk

Ritota¹,

Costanzo²,

Mattera³

et al. 2017

Journal of Analytical Methods in Chemistry

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Milk is generally very rich in nutrients and this may lead it to be an ideal growth environment for many microorganisms, including pathogens, so effective measurements aiming to ensure total microbiological safety of milk and minimize the risk to human health are needed. Milk heat treatments are the most common practices carried out to inhibit the microbial growth; therefore it is necessary to have analytical procedures that are more and more up-to-date and capable of detecting the effectiveness of the heat treatments. Most of the reference and official methods to assess heat treatment in milk are based on the evaluation of the modifications of some milk components following the thermal process, such as the determination of enzyme activities (alkaline phosphatase and lactoperoxidase), whey proteins, Maillard reaction compounds (generally furosine), and lactulose. Besides the most common techniques (liquid and gas chromatography, capillary electrophoresis, or spectroscopy) used for the detection of single thermal indicators, new approaches, such as chemometric studies or more recent techniques, including size-exclusion chromatography with online electrospray mass spectrometry or stable isotope ratio mass spectrometry, are discussed in this review in order to evaluate heat treatment in milk.

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Determination of lysinoalanine by high performance liquid chromatography

Moret

Cherubin

Rodríguez‐Estrada

et al. 1994

J. High Resol. Chromatogr.

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This work suggests an HPLC method for qualitative and quantitative determination of N-epsilon(2-amino-2-carboxyethyl)-L-lysine (LAL). LAL was released from total hydrolysates of various proteins of animal origin and derivatized with dansyl chloride, The performance of two different columns, Spherisorb 3S TG and mu-Bondapack C-18, was compared; better resolution and quantitative response were obtained with the former. The mobile phase was a mixture of 0.01 M phosphate buffer (pH 7) and acetonitrile. Linear response and quantitative repeatability were tested for both detectors used (UV-Vis set at 254 nm; fluorimetric set at lambda(ex(max))= 360 nm and lambda(em(max))= 525 nm). For LAL standard the minimum detectable amount was 0.05 ng, whereas for LAL in actual samples the amount was 0.5 ng (40 mu g/g of analyzed proteins). Good analytical repeatability was obtained, resulting in CV% of 4.7 and 3.8 for UV and fluorimetric detectors, respectively. LAL recovery was determined using both detectors; the values obtained were 94 % (fluorimetric) and 92 % (UV). Greater noise levels were observed with the fluorimetric detector and its higher sensitivity could not, therefore, be fully utilized, The highest amounts of LAL were found in the casein (2816 mu g/g) and cooked albumin (615 mu g/g) samples

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Lysinoalanine Determination in Proteins Using High‐pressure Liquid Chromatography

Cited by 12 publications

References 28 publications

Lysinoalanine in foods

Lysinoalanine in foods

New Trends for the Evaluation of Heat Treatments of Milk

Determination of lysinoalanine by high performance liquid chromatography

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