Gas Chromatography-Mass Spectrometry of Lysinoalanine and the Related Crosslinked Amino Acids in Alkali-treated Food Proteins

Hasegawa, Kiyozo; Iwata, Shoko

doi:10.1080/00021369.1982.10865465

Cited by 8 publications

(10 citation statements)

References 12 publications

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“…The fragmentation pattern for the N-TFA-IPE of LMeAL is shown in Figure 4. The fragmentation characteristics are nearly identical with those of the corresponding LAL derivative (Hasegawa and Iwata, 1982). Thé base peak of LMeAL arises from the same decomposition reactions (M -212 -42) as reported for LAL and shows a difference of m/e 14 to the base peak of LAL.…”

Section: Resultssupporting

confidence: 65%

Evidence for lysinomethylalanine formation in model systems

Kruse¹,

Steinhart²

1989

J. Agric. Food Chem.

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Threonine (Thr) gives rise to the formation of a dehydro amino acid, methyldehydroalanine (MDHA) (2-aminobut-2-enoic acid), by p-elimination in alkaline medium. MDHA can react with functional groups within protein chains, for example with the €-amino group of lysine to form lysinomethylalanine (LMeAL), a cross-link not clearly demonstrated before now. To be able to show the presence of LMeAL in peptides, the intermediate product MDHA was prepared first in the form of a stable derivative of the (tert-butyloxycarbony1)methyldehydroalanine isopropyl ester (BOC-MDHA-IPE). This was followed by the synthesis of LMeAL by the reaction of BOC-MDHA-IPE with N-a-acetyl-L-lysine. The formation of LMeAL in threonine-containing di-and tripeptides with added N-a-acetyl-L-lysine was studied at different pH values within the alkaline range.

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Section: Resultssupporting

confidence: 65%

Evidence for lysinomethylalanine formation in model systems

Kruse¹,

Steinhart²

1989

J. Agric. Food Chem.

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“…Various techniques such as ion-exchange chromatography with colorimetric and fluorescence detection have been applied to analyse the isopeptides (Friedman & Cuq, 1988;Fritsch & Klostermeyer, 1981;Henle, Walter, & Klostermeyer, 1993;Wilkinson & Hewavitharana, 1997). GC analysis of n-butyl esters of N(O)-trifluoroacetyl derivatives (Buser & Erbersdobler, 1984;Hasegawa &Iwata, 1982;Hasegawa, Mukai, Gotoh, Honjo, & Matoba, 1987), GC-MS analysis of diasteriomeric N(O,S)-perfluoropropionyl isopropyl esters (Liardon, 1991), and 2-D thin layer chromatography (Fujimoto, 1984) have been used. HPLC based on derivatisation with 9-flouroenylmethylchloroformate (FMOC) or dansyl chloride (D'Agostina, Boschin, Rinaldi, & Arnoldi, 2003;Faist, Drusch, Kiesner, Elmadfa, & Erbersdobler, 2000), or selective ion monitoring by LC-ESI-MS on FMOC-LAL are the most recent methods used (Calabrese, Mamone, Caira, Ferranti, & Addeo, 2009).…”

Section: Protein Cross-linkingmentioning

confidence: 99%

Proteomics of major bovine milk proteins: Novel insights

Deeth

Larsen

2017

International Dairy Journal

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Milk proteomics covers the identification, characterisation and quantification of milk proteins. Its applications vary from the basic composition of milk proteins to their post-translational modifications (PTMs), occurring naturally or via processing and storage. Through the combination of liquid chromatography or two-dimensional gel electrophoresis with advanced mass spectrometry, milk proteomics has revealed PTMs that affect milk protein structural and functional properties. This review discusses detection by proteomics-based methods with special emphasis on natural and process induced PTMs in the major bovine milk proteins. The review covers the importance of milk proteomics in determining PTMs, especially those formed by heat treatment and during storage, and highlights some breakthroughs in PTM studies. Furthermore, aspects and applications of quantitative proteomics on milk proteins and bioinformatics are covered. ___________________________________________________________________________________ 1998). Milk from other species have been included in other reviews (Cunsolo, Muccilli, Saletti & Foti, 2011; El-Salam, 2014) and will not be included here. Overall, bovine milk proteins and related peptides can be classified into four different groups: caseins (α S1-, α S2-, βand κ-caseins), serum proteins [αlactalbumin (α-La), β-lactoglobulin (β-Lg), bovine serum albumin (BSA), immunoglobulins (Igs) and a range of other minor whey proteins], proteose peptones (low molecular weight peptides derived from caseins and well as proteose peptone component 3, called PP3) and membrane [mostly milk fat globule membrane (MFGM)] proteins (Table 1).

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“…In the steaming method moisture conditions are not optimum for LAL formation. Hasegawa and Okamoto (1980) also looked at longtime heating at 80 °C using 0.1 N NaOH on LAL formation in soy protein but found little difference between 1 and 5 h. This is not surprising in view of data generated by de Rham et al (1977) as discussed below.…”

mentioning

confidence: 89%

“…Food Occurrences. Due to the fact that alkaline exposure to proteins has been shown to result in significant LAL formation (de Groot and Slump, 1969;Provansal et al, 1975; Chu et al, 1976; de Groot et al, 1977;Karayiannis et al, 1979a;Hasegawa and Okamoto, 1980;Hasegawa et al, 1981; Dworschak et al, 1981;Hayashi and Kameda, 1980a,c;Meyer et al, 1981), one would suspect that foods that are traditionally exposed to alkaline conditions during processing or preparation would probably contain LAL. This in fact is the case.…”

mentioning

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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Gas Chromatography-Mass Spectrometry of Lysinoalanine and the Related Crosslinked Amino Acids in Alkali-treated Food Proteins

Cited by 8 publications

References 12 publications

Evidence for lysinomethylalanine formation in model systems

Evidence for lysinomethylalanine formation in model systems

Proteomics of major bovine milk proteins: Novel insights

Lysinoalanine in foods

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