Physicochemical and flavour characteristics of Maillard reaction products derived from <i>Aloididae aloidi</i> muscle enzymatic hydrolysates coupled with High‐Pressure Processing

Bu, Ying; Zhu, Lunwei; Xu, Wenting; Zhu, Wenhui; Liu, He; Lǐ, Jiànróng; Li, Xuepeng

doi:10.1111/ijfs.14802

Cited by 6 publications

(7 citation statements)

References 36 publications

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“…Because the structure of glycine is relatively simple, glycine-containing peptides are commonly used as the main model peptides [ 16 ]. However, peptides composed of other amino acids can generate various specific volatile compounds [ 17 , 18 , 19 , 20 , 21 , 22 , 23 ].…”

Section: Introductionmentioning

confidence: 99%

Formation of Pyrazines in Maillard Model Systems: Effects of Structures of Lysine-Containing Dipeptides/Tripeptides

Wang

Shen

Liu

et al. 2021

Foods

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At present, most investigations involving the Maillard reaction models have focused on free amino acids (FAAs), whereas the effects of peptides on volatile products are poorly understood. In our study, the formation mechanism of pyrazines, which were detected as characteristic volatiles in sunflower seed oil, from the reaction system of glucose and lysine-containing dipeptides and tripeptides was studied. The effect of the amino acid sequences of the dipeptides and tripeptides on pyrazine formation was further highlighted. Four different dipeptides and six tripeptides were selected. The results showed that the production of pyrazines in the lysine-containing dipeptide models was higher than that in the tripeptide and control models. Compounds 2,5(6)-Dimethylpyrazine and 2,3,5-trimethylpyrazine were the main pyrazine compounds in the dipeptide models. Furthermore, the C- or N-terminal amino acids of lysine-containing dipeptides can exert an important effect on the formation of pyrazines. In dipeptide models with lysine at the C-terminus, the content of total pyrazines followed the order of Arg−Lys > His−Lys; the order of the total pyrazine content was Lys−His > Lys−Arg in dipeptide models with N-terminal lysine. Additionally, for the tripeptide models with different amino acid sequences, more pyrazines and a greater variety of pyrazines were detected in the tripeptide models with N-terminal lysine/arginine than in the tripeptide models with N-terminal histidine. However, the total pyrazine content and the percentage of pyrazines in the total volatiles were similar in the tripeptide models with the same amino acids at the N-terminus. This study clearly illustrates the ability of dipeptides and tripeptides containing lysine, arginine and histidine to form pyrazines, improving volatile formation during sunflower seed oil processing.

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Section: Introductionmentioning

confidence: 99%

Formation of Pyrazines in Maillard Model Systems: Effects of Structures of Lysine-Containing Dipeptides/Tripeptides

Wang

Shen

Liu

et al. 2021

Foods

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“…aloidi muscle enzymatic hydrolysates coupled with Ultra‐high pressure (MRPF 1 ) was prepared according to the method of Bu et al . (2020).…”

Section: Methodsmentioning

confidence: 99%

“…In previous studies, we confirmed that the enzymatic hydrolysis coupled with high‐pressure processing and Maillard reaction can better improve the flavour of A . aloidi muscle (Bu et al ., 2020).…”

Section: Introductionmentioning

confidence: 99%

Effects of different wall materials on stability and umami release of microcapsules of Maillard reaction products derived from Aloididae aloidi

Zhu

et al. 2021

Int J of Food Sci Tech

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Umami has a fast release in the long time high temperature cooking process. Microencapsulation technology can be used to control the release of aromas, and spray drying is the method most commonly used for preparing microcapsules. In this study, the Maillard reaction products from the enzymatic hydrolysate of the Aloididae aloidi were combined with chitosan (C); maltodextrin (M); chitosan and gum arabic (C + GA); M + GA; and C + M + GA via spray drying. Characterisation, flavour characteristics and umami release of microcapsules were analysed and determined. The results showed that the obtained microcapsules had the characteristics of low water content and high solubility, and had good embedding effect and thermal stability (especially M C + GA ). Scanning electron microscopy results showed that the addition of wall material increased the diameter of the particles. The microcapsules in M C group and M C + GA group showed the best apparent structure, which was round without pits or pores. In the controlled release study of umami, M C + GA group showed the best sustained umami release, released 13.95%, 38.08% and 80% umami at 0.5, 4 and 32 min, respectively. In conclusion, adding C + GA as wall material of microcapsules had the best stability, flavour and taste sustained-release effect.

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“…Further advancements will lead to the designs combining the physicochemical and biological technologies for the purpose of producing high‐quality products (Su et al., 2021). Combining physicochemical and biological methods is a promising approach to the debittering of protein hydrolysates; this combination has better debittering effects and efficiency than when using the methods separately (Bu et al., 2020; Fu et al., 2020; Siewe, et al., 2020).…”

Section: Introductionmentioning

confidence: 99%

Review on the release mechanism and debittering technology of bitter peptides from protein hydrolysates

Liu

Chen

et al. 2022

Comp Rev Food Sci Food Safe

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Recent scientific evidence indicates that protein hydrolysates contain bioactive peptides that have potential benefits for human health. However, the bittertasting hydrophobic peptides in protein hydrolysates negatively affect the sensory quality of resulting products and limit their utilization in food and pharmaceutical industries. The approaches to reduce, mask, and remove bitter taste from protein hydrolysates have been extensively reported. This review paper focuses on the advances in the knowledge regarding the structure-bitterness relationship of peptides, the release mechanism of bitter peptides, and the debittering methods for protein hydrolysates. Bitter tastes generating with enzymatic hydrolysis of protein is influenced by the type, concentration, and bitter taste threshold of bitterness peptides. A "bell-shaped curve" is used to describe the relationship between the bitterness intensity of the hydrolysates and the degree of hydrolysis. The bitter receptor perceives bitter potencies of bitter peptides by the hydrophobicity recognition zone. The intensity of bitterness is influenced by hydrophobic and electronic properties of amino acids and the critical spatial structure of peptides. Compared to physicochemical debittering (i.e., selective separation, masking of bitter taste, encapsulation, Maillard reaction, and encapsulation) and other biological debittering (i.e., enzymatic hydrolysis, enzymatic deamidation, plastein reaction), enzymatic hydrolysis is a promising debittering approach as it combines protein hydrolyzation and debittering into a one-step process, but more work should be done to advance the knowledge on debittering mechanism of enzymatic hydrolysis and screening of suitable proteases. Further

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Physicochemical and flavour characteristics of Maillard reaction products derived from Aloididae aloidi muscle enzymatic hydrolysates coupled with High‐Pressure Processing

Cited by 6 publications

References 36 publications

Formation of Pyrazines in Maillard Model Systems: Effects of Structures of Lysine-Containing Dipeptides/Tripeptides

Formation of Pyrazines in Maillard Model Systems: Effects of Structures of Lysine-Containing Dipeptides/Tripeptides

Effects of different wall materials on stability and umami release of microcapsules of Maillard reaction products derived from Aloididae aloidi

Review on the release mechanism and debittering technology of bitter peptides from protein hydrolysates

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