Effect of amino compounds on the volatile compounds and antioxidant activity of Maillard reaction products of enzymatic hydrolyzed cabbage leaves

Fadel, Hoda H. M.; Lotfy, Shereen N.; Asker, Mohsen S.; Mahmoud, Manal G.; El-Aleem, Fatma Shafik Abd; Ahmed, Mohamad Yehia Sayed; Saad, Rasha

doi:10.1016/j.afres.2023.100327

Cited by 2 publications

(5 citation statements)

References 63 publications

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“…Maillard conjugation led to significant reduction of DPPH RSA while it reached 44.14% and 31.66% for MLPH and MLPHC, respectively. There are diverse findings regarding the Maillard effects on the antioxidant activity, especially in terms of the conjugation of peptides and carbohydrates (Fadel et al., 2023 ; Liu et al., 2012 ; Yu et al., 2018 ). The volatile compounds and low MW heterocyclic compounds might be attributed to the increase of antioxidant activity after Maillard reaction between soybean protein hydrolysates and xylose (Yu et al., 2018 ).…”

Section: Resultsmentioning

confidence: 99%

“…Cross‐linking of GA with LPH and LPHC presumably coated the exposed hydrophobic segments of hydrolysates, thus, reduction of surface hydrophobicity and reduction of interactions with DPPH radicals. Participation of some of the antioxidant amino acid residues in Maillard reaction has demonstrated reduction of antioxidant activity (Fadel et al., 2023 ; Zha, Yang, et al., 2019 ). Therefore, grafting GA with LPH and LPHC formed a strong steric hindrance that decreased the surface hydrophobicity, which was in line with findings of previous studies (Dai et al., 2023 ; Xia et al., 2023 ).…”

Section: Resultsmentioning

confidence: 99%

“…They reported that post-hydrolysis cross-linking rearranged the (poly)peptides in soy protein hydrolysates via glutaminyl modifications, followed by reduction of surface hydrophobicity. activity, especially in terms of the conjugation of peptides and carbohydrates (Fadel et al, 2023;Liu et al, 2012;Yu et al, 2018). The volatile compounds and low MW heterocyclic compounds might be attributed to the increase of antioxidant activity after Maillard reaction between soybean protein hydrolysates and xylose (Yu et al, 2018).…”

Section: Dpph Radical Scavenging Activitymentioning

confidence: 99%

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Conjugation of gum Arabic and lentil protein hydrolysates through Maillard reaction: Antioxidant activity, volatile compounds, functional and sensory properties

Rezvankhah,

Ghanbarzadeh,

Mirzaee

et al. 2024

Food Science & Nutrition

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Lentil protein hydrolysates (LPH) and lentil protein hydrolysates cross‐linked (LPHC) were grafted with gum Arabic (GA) through a wet Maillard reaction at 100°C for 2 h and called MLPH and MLPHC. The samples were assessed for absorption, degree of grafting (DG), surface hydrophobicity, antioxidant activity, molecular weight (MW) profile, chemical alteration, volatile compounds, functional and sensory properties. Results showed that Maillard grafting led to increase in absorption and DG (maximum value: MLPHC), and led to the reduction of the surface hydrophobicity and antioxidant activity (minimum value: MLPHC). MW profiles indicated that MLPH and MLPHC formed new bands at MW >250 kDa. Regarding the Fourier transform infrared spectroscopy (FTIR), Maillard conjugation led to the occurrence of peaks at 1759 and 1765 cm−1, while the intensities of amide I bands at 1637 and 1659 cm−1 and amide II bands at 1498 and 1495 cm−1 were decreased. Hydrolysis, cross‐linking, and especially Maillard grafting provided well‐balanced content of volatile components. Indeed, the proportions of alcohols, ketones, aldehydes, and acids were changed, thereby, the inherent grassy and planty tastes were diminished while new umami taste was developed. Maillard grafting led to significant improvement of functional properties, while MLPH and MLPHC indicated the highest emulsifying activity at pH 10.0 (73.76 and 70.12 m2/g, respectively) and stability (369.64 and 288.22 min), foaming capacity (88.57% and 142.86%) and stability (60.57% and 72%). Sensory analysis has demonstrated that umami taste was highly developed in MLPH and MLPHC, which can be well considered as meat proteins and flavor enhancers such as monosodium glutamate (MSG).

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Dpph Radical Scavenging Activitymentioning

confidence: 99%

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Conjugation of gum Arabic and lentil protein hydrolysates through Maillard reaction: Antioxidant activity, volatile compounds, functional and sensory properties

Rezvankhah,

Ghanbarzadeh,

Mirzaee

et al. 2024

Food Science & Nutrition

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“…Tastes related MRPs are mainly Maillard-reacted peptides, which are reported to show salt taste-enhancing properties (Yu et al 2022 ). Similarly, aroma related MRPs mainly depend on the types of peptides, amino acids and reducing sugars in the system, and reaction conditions such as temperature, time, and pH (Fadel et al 2023 ). Studies have shown that cysteine can significantly enhance the formation of MRPs with meat-like flavor (Fadel et al 2023 ; Gao et al 2020 ).…”

Section: Introductionmentioning

confidence: 99%

“…Similarly, aroma related MRPs mainly depend on the types of peptides, amino acids and reducing sugars in the system, and reaction conditions such as temperature, time, and pH (Fadel et al 2023 ). Studies have shown that cysteine can significantly enhance the formation of MRPs with meat-like flavor (Fadel et al 2023 ; Gao et al 2020 ). Many studies presented cysteine as a flavor precursor due to its contribution to the production of meaty aroma compounds, such as pyrazines and 2-methyl-3-furanthiol, through pyrolysis or Strecker degradation with dicarbonyl compounds (Gao et al 2020 ; Yu and Zhang 2010 ).…”

Section: Introductionmentioning

confidence: 99%

Flavor improving effects of cysteine in xylose–glycine–fish waste protein hydrolysates (FPHs) Maillard reaction system

Ding,

Yan,

Dai

et al. 2023

Bioresour. Bioprocess.

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A promising way to utilize fish by-products is to develop hydrolysis of fish proteins with enzymes. The obtained fish protein hydrolysates (FPHs) are rich in peptides and amino acids, but bitterness and aroma defects impede further utilization of FPHs. The present study adopted Maillard reaction to improve FPHs’ flavor and illustrated the role of cysteine in this system. We investigated the impact of cysteine (0, 0.25%, 0.5%, 0.75%, and 1%) on the browning intensity, free amino acids (FAAs), molecular weight distribution, structure of MRPs, volatile compounds changes and organoleptic characteristics of xylose–glycine–FPHs Maillard reaction systems. Results showed that the addition of cysteine lowered the browning degree of Maillard reaction products (MRPs) by inhibiting the cross-linking of small peptides and reducing the production of melanin. GC–MS and GC–IMS analysis indicated that cysteine inhibited the formation of furans and nitrogen-containing compounds and facilitated the formation of sulfur-containing compounds contributing to the meaty flavor. Sensory analysis revealed that 0.25–0.75% range of cysteine increased the meaty, caramel, umami, mouthfulness and salty notes, and caused a decrease in bitter taste of the MRPs as confirmed by GC–MS. A highly significant correlation between the organoleptic characteristics and physicochemical indicators of MRPs was found by Mantel test. These results elucidated the influence of cysteine on the formation of Maillard reaction products and will help improve the flavor profile of meat flavorings. Graphical Abstract

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Effect of amino compounds on the volatile compounds and antioxidant activity of Maillard reaction products of enzymatic hydrolyzed cabbage leaves

Cited by 2 publications

References 63 publications

Conjugation of gum Arabic and lentil protein hydrolysates through Maillard reaction: Antioxidant activity, volatile compounds, functional and sensory properties

Conjugation of gum Arabic and lentil protein hydrolysates through Maillard reaction: Antioxidant activity, volatile compounds, functional and sensory properties

Flavor improving effects of cysteine in xylose–glycine–fish waste protein hydrolysates (FPHs) Maillard reaction system

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