Studies on the gas chromatographic analysis of lysinoalanine in alkali-treated food proteins.

Hasegawa, Kiyozo; Okamoto, Nobuhiko

doi:10.1271/bbb1961.44.649

Cited by 12 publications

(3 citation statements)

References 4 publications

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“…In the case of KOH, 0.2 N KOH produced more lysinoalanine than 0.1 N KOH (Nos. 7,8). The amount of lysinoalanine produced by 0.2 N KOH corresponded approximately to 3 mol per mol of lysozyme.…”

Section: Factors Which Influenced the Lysinoalanine Formation In Lysomentioning

confidence: 87%

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Limits and Sites of Lysinoalanine Formation in Lysozyme, α-Lactalbumin and α_s1- and β-Caseins by Alkali Treatment

Hasegawa

Okamoto

Ozawa

et al. 1981

Agricultural and Biological Chemistry

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Section: Factors Which Influenced the Lysinoalanine Formation In Lysomentioning

confidence: 87%

“…Isothermal gas-liquid chromatography of BTFA-derivatives of lysinoalanine was carried out on a Shimadzu GC-6AM gas chromatograph, equipped with a flame-ionization· detector, according to the method of Hasegawa et al 8 ) The separation column used was a glass column (1.5 m x 3 mm J.D.) packed with 2% OV-17/1 % OV-210 on 100/120 Supelcoport.…”

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Limits and Sites of Lysinoalanine Formation in Lysozyme, α-Lactalbumin and α_s1- and β-Caseins by Alkali Treatment

Hasegawa

Okamoto

Ozawa

et al. 1981

Agricultural and Biological Chemistry

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“…In the case of KOH, 0.2n KOH produced more lysinoalanine than 0.1 n KOH (Nos. 7,8). The amount of lysinoalanine produced by 0.2n KOH corresponded approximately to 3mol per mol of lysozyme.…”

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confidence: 85%

Limits and sites of lysinoalanine formation in lysozyme, .ALPHA.-lactalbumin and .ALPHA.s1- and .BETA.-caseins by alkali treatment.

Hasegawa

Okamoto

Ozawa

et al. 1981

Agricultural and Biological Chemistry

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Lysinoalanine was determined by gas chromatography. Lysinoalanine formation in lysozyme depended on alkali concentration, pH, temperature and exposure time. The upper limits of lysinoalanine formation in lysozyme and a-lactalbumin were related to the number of lysine residues with a cystine disulfide bond in the adjacent position rather than the individual contents of these residues. In cases of asl-and^-caseins, the upper limits were related to the number of phosphoserine residues, regardless of their sequential relationship to lysine residues. Gel electrophoresis suggested that intermolecular cross-linking took place in the a-lactalbumin and caseins. Alkali treatment has been used not only in traditional food processing and cooking,1~4) but also in modern food industry.5) Noting the decrease of cysteine on the alkali treatment of protein, Bohak6) first isolated a cross-linked amino acid, Ar£-(DL-2-amino-2-carboxyethyl)

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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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Studies on the gas chromatographic analysis of lysinoalanine in alkali-treated food proteins.

Cited by 12 publications

References 4 publications

Limits and Sites of Lysinoalanine Formation in Lysozyme, α-Lactalbumin and α_s1- and β-Caseins by Alkali Treatment

Limits and Sites of Lysinoalanine Formation in Lysozyme, α-Lactalbumin and α_s1- and β-Caseins by Alkali Treatment

Limits and sites of lysinoalanine formation in lysozyme, .ALPHA.-lactalbumin and .ALPHA.s1- and .BETA.-caseins by alkali treatment.

Determination of lysinoalanine by high performance liquid chromatography

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Studies on the gas chromatographic analysis of lysinoalanine in alkali-treated food proteins.

Cited by 12 publications

References 4 publications

Limits and Sites of Lysinoalanine Formation in Lysozyme, α-Lactalbumin and αs1- and β-Caseins by Alkali Treatment

Limits and Sites of Lysinoalanine Formation in Lysozyme, α-Lactalbumin and αs1- and β-Caseins by Alkali Treatment

Limits and sites of lysinoalanine formation in lysozyme, .ALPHA.-lactalbumin and .ALPHA.s1- and .BETA.-caseins by alkali treatment.

Determination of lysinoalanine by high performance liquid chromatography

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Limits and Sites of Lysinoalanine Formation in Lysozyme, α-Lactalbumin and α_s1- and β-Caseins by Alkali Treatment

Limits and Sites of Lysinoalanine Formation in Lysozyme, α-Lactalbumin and α_s1- and β-Caseins by Alkali Treatment