1991
DOI: 10.1021/jf00003a020
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Racemization kinetics of free and protein-bound lysinoalanine (LAL) in strong acid media. Isomeric composition of bound LAL in processed proteins

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Cited by 31 publications
(30 citation statements)
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“…During this reaction, the hydrogen bound to the a-carbon atom is removed and another proton is added from the reverse side (Carey and Sundberg 1995). Performing hydrolysis in a deuterated medium therefore leads to a direct labeling of the inverted molecules (Liardon et al 1991;Goodlett et al 1995;Amelung and Brodowski 2002). We exploited this effect for the in vitro determination of the hydrolysis-induced racemization (HIR) of amino acids in each of pooled bulk soil and clay samples from the three agro-ecosystems' savanna sites and their !90 years old arable field plots, respectively.…”
Section: Method-induced Racemizationmentioning
confidence: 99%
“…During this reaction, the hydrogen bound to the a-carbon atom is removed and another proton is added from the reverse side (Carey and Sundberg 1995). Performing hydrolysis in a deuterated medium therefore leads to a direct labeling of the inverted molecules (Liardon et al 1991;Goodlett et al 1995;Amelung and Brodowski 2002). We exploited this effect for the in vitro determination of the hydrolysis-induced racemization (HIR) of amino acids in each of pooled bulk soil and clay samples from the three agro-ecosystems' savanna sites and their !90 years old arable field plots, respectively.…”
Section: Method-induced Racemizationmentioning
confidence: 99%
“…Various analytical procedures have been evaluated for determining LAL in protein and protein-containing foods and feeds. Because LAL survives the acidic conditions of protein hydrolysis commonly used for the analysis of amino acids [1], its determination can be performed by ionexchange chromatography (amino acid analyzer) with colorimetric and fluorometry detections after an acid protein digestion [18,19], GC analysis of n-butyl esters of N(O)-trifluoroacetyl derivatives [6,20,21], GC-MS analysis of diasteromeric N(O,S)-perfluoropropionyl isopropyl esters [22] or TLC and HPLC analysis [14, 23 -26]. Most of the data recently published related to LAL analysis in foods have been acquired by the HPLC method proposed by Pellegrino et al [9], based on derivatization with FMOC-Cl, SPE, RP chromatography, and fluorescence detection.…”
Section: Introductionmentioning
confidence: 99%
“…High pH, temperatures, and long exposure times favoured the formation of LAL in proteincontaining foods. LAL has been determined in foods using ion-exchange chromatography [30,31], GC [32][33][34][35][36], thin layer chromatography and HPLC [18,[37][38][39][40][41][42][43].…”
Section: Introductionmentioning
confidence: 99%