Cysteine's effects on chlorogenic acid quinone induced greening and browning: Mechanism and effect on antioxidant reducing capacity. (30th March 2020)
- Record Type:
- Journal Article
- Title:
- Cysteine's effects on chlorogenic acid quinone induced greening and browning: Mechanism and effect on antioxidant reducing capacity. (30th March 2020)
- Main Title:
- Cysteine's effects on chlorogenic acid quinone induced greening and browning: Mechanism and effect on antioxidant reducing capacity
- Authors:
- Liang, Yundi
Were, Lilian - Abstract:
- Highlights: Cysteine concentration, pH and incubation time affected color and antioxidant capacity. Cysteine inhibited chlorogenic acid (CGA)-lysine greening primarily by reduction. Cysteinyl thiols had a higher affinity for CGA quinones than lysyl ɛ-amines. Lysyl amine-CGA conjugate was the main green trihydroxy benzacridine precursor ion. The effect of CGA on CGA-amine greening and Maillard browning was decoupled. Abstract: Formation of green trihydroxy benzacridine (TBA) derivatives when chlorogenic acid (CGA) quinones and amino acids react can be unappealing for some consumers. Cysteine was studied as an anti-greening strategy, given that cysteine-CGA conjugates are colorless. Buffered 2.55 mM CGA: 5.09 mM lysine: (0–5.09) mM cysteine solutions at pH 8 and 9 were prepared and incubated for a maximum of 48 h at 22 C. Color intensity and conjugate formation was monitored spectrophotometrically, and by HPLC and LC-MS respectively, while antioxidant capacity was measured by Folin-Ciolcateau and Trolox equivalent antioxidant capacity assays. Green TBA formation was promoted at higher pH and inhibited as cysteine concentration increased. Concentration-dependent cysteine inhibition of CGA-lysine greening was attributed to redox diphenol regeneration and formation of cysteinyl-CGA conjugates, which also contributed to antioxidant capacity. pH had a greater effect on antioxidant capacity than added cysteine. Results suggested a potential anti-greening approach for alkaline CGAHighlights: Cysteine concentration, pH and incubation time affected color and antioxidant capacity. Cysteine inhibited chlorogenic acid (CGA)-lysine greening primarily by reduction. Cysteinyl thiols had a higher affinity for CGA quinones than lysyl ɛ-amines. Lysyl amine-CGA conjugate was the main green trihydroxy benzacridine precursor ion. The effect of CGA on CGA-amine greening and Maillard browning was decoupled. Abstract: Formation of green trihydroxy benzacridine (TBA) derivatives when chlorogenic acid (CGA) quinones and amino acids react can be unappealing for some consumers. Cysteine was studied as an anti-greening strategy, given that cysteine-CGA conjugates are colorless. Buffered 2.55 mM CGA: 5.09 mM lysine: (0–5.09) mM cysteine solutions at pH 8 and 9 were prepared and incubated for a maximum of 48 h at 22 C. Color intensity and conjugate formation was monitored spectrophotometrically, and by HPLC and LC-MS respectively, while antioxidant capacity was measured by Folin-Ciolcateau and Trolox equivalent antioxidant capacity assays. Green TBA formation was promoted at higher pH and inhibited as cysteine concentration increased. Concentration-dependent cysteine inhibition of CGA-lysine greening was attributed to redox diphenol regeneration and formation of cysteinyl-CGA conjugates, which also contributed to antioxidant capacity. pH had a greater effect on antioxidant capacity than added cysteine. Results suggested a potential anti-greening approach for alkaline CGA quinone-amine greening. … (more)
- Is Part Of:
- Food chemistry. Volume 309(2020)
- Journal:
- Food chemistry
- Issue:
- Volume 309(2020)
- Issue Display:
- Volume 309, Issue 2020 (2020)
- Year:
- 2020
- Volume:
- 309
- Issue:
- 2020
- Issue Sort Value:
- 2020-0309-2020-0000
- Page Start:
- Page End:
- Publication Date:
- 2020-03-30
- Subjects:
- Antioxidant capacity -- Browning -- Chlorogenic acid quinones -- Cysteine -- Greening
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2019.125697 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 23135.xml