Insight into the advantages of premixing yeast-wheat gluten and combining ultrasound and transglutaminase pretreatments in producing umami enzymatic protein hydrolysates

Su, Guowan; Zheng, Xin; Zou, Jin; Waterhouse, Geoffrey I.N.; Sun‐Waterhouse, Dongxiao

doi:10.1016/j.foodchem.2020.128317

Cited by 16 publications

(6 citation statements)

References 31 publications

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“…The Alcalase hydrolyzes OVA called HOVA, the Alcalase hydrolyzes OVA treated with PEF called HOVA-P, the Alcalase treated with PEF hydrolyzes OVA called HOVA-P′, the Alcalase treated with PEF hydrolyzes OVA treated called HOVA-PP′. 19 Determination of Degree of Hydrolysis. Determination of the effect of PEF-assisted Alcalase hydrolysis on the DH of OVA by OPA method.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

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Mechanism of Targeted Regulation of Ovalbumin Epitopes by Pulsed Electric Field-Assisted Alcalase Treatment

Ding

Dong

et al. 2023

J. Agric. Food Chem.

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Egg is one of the eight major food allergens, and ovalbumin (OVA) is the most abundant allergenic protein in eggs. In this study, the effects of pulsed electric field (PEF)-assisted Alcalase hydrolysis on the spatial conformation and potential allergenicity of OVA were studied, and the mechanism of its inhibiting allergic reactions effect was revealed. PEF-assisted Alcalase hydrolysis increased the degree of hydrolysis, surface hydrophobicity, and free sulfhydryl group content. Moreover, the reduction in the α-helix content, fluorescence intensity, and disulfide bond content suggested that PEF promoted the OVA hydrolysis by Alcalase. Additionally, enzyme-linked immunosorbent assay data indicated that PEF-assisted Alcalase hydrolysis hindered OVA binding to immunoglobulins E and G1. Finally, based on bioinformatics combined with mass spectrometry, PEF-assisted Alcalase reduced OVA-induced allergic reactions by destroying epitopes in OVA. Overall, PEF technology further destroyed the epitopes of allergens by targeting the binding sites of substrates and enzymes to improve the affinity of enzymes and substrates, reducing allergic reactions.

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Section: ■ Materials and Methodsmentioning

confidence: 99%

“…Finally, the HOVA, HOVA-P, HOVA-P′, and HOVA-PP′ powder samples were obtained by freeze-drying. The Alcalase hydrolyzes OVA called HOVA, the Alcalase hydrolyzes OVA treated with PEF called HOVA-P, the Alcalase treated with PEF hydrolyzes OVA called HOVA-P′, the Alcalase treated with PEF hydrolyzes OVA treated called HOVA-PP′ …”

Section: Methodsmentioning

confidence: 99%

Mechanism of Targeted Regulation of Ovalbumin Epitopes by Pulsed Electric Field-Assisted Alcalase Treatment

Ding

Dong

et al. 2023

J. Agric. Food Chem.

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“…Liu et al (2010) Transglutaminase applied alone or in combination with ultrasound significantly reduced the bitterness of the resulting hydrolysates. (Su, et al, 2021) Pumpkin seed protein Alcalase, papain flavourzyme, bacillus axarquiensis SWJSX8 aminopeptidase Sequential hydrolysis with alcalase and aminopeptidase was designed to prepare low-bitterness powders.…”

Section: Maillard Reactionmentioning

confidence: 99%

“…Understanding the mechanism of biological debittering can help inform the selection of a certain type of enzyme preparation and determine the degree of hydrolysis to generate hydrolysates with adequate sensory properties (Daher et al., 2021). 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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“…Food protein is a good source of taste‐active compounds, which can release amino acids and peptides with sensory properties 1 . Currently, it is repoted that the taste‐active amino acids and peptides can be released from proteins of various raw materials, such as soybean, 2 fish, 3 meat, 4 yeast, 5 via fermentation, hydrolyzation, or aqueous extraction. Furthermore, hydrolysis was extensively applied in the preparation of the degradation products of fish proteins to improve the flavor and the quality of the food.…”

Section: Introductionmentioning

confidence: 99%

Fish proteins as potential precursors of taste‐active compounds: an in silico study

Xiao

et al. 2022

J Sci Food Agric

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BACKGROUND: Fish protein is a good source of amino acids and peptides with sensory properties. Theoretically, the type of protein affects the taste quality of the protein hydrolysates. To better use fish protein in the food ingredients industry, an in silico approach was adopted to evaluate the potential of fish protein to release taste-active compounds.RESULTS: Six types of protein from seven commercial fishes were screened from the Uniprot knowledge base. The results showed that a remarkable number of umami fragments presented in myosin and parvalbumin (PB), such as glutamic acid (Glu), aspartic acid (Asp), and Asp-and Glu-containing peptides, whereas sweet amino acids and bitter peptides (e.g., Proand Gly-containing peptides) were mainly found in collagen (CGI) in all fish samples. After the in silico proteolysis by papain, a difference in the profile of taste-active fragments was observed among the six types of proteins. Amino acids were the main hydrolysis products of these proteins, especially umami, sweet, and bitter amino acids, significantly contributing to the taste formation of protein hydrolysates. Besides, the myosin and CGI hydrolysates were abundant in taste active peptides both in types and quantities.CONCLUSION: Myosin is a promising protein source for producing umami fragments, and CGI seems to be a good precursor of sweet and bitter fragments. Different types of protein have an essential effect on the taste of protein hydrolysates.

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Insight into the advantages of premixing yeast-wheat gluten and combining ultrasound and transglutaminase pretreatments in producing umami enzymatic protein hydrolysates

Cited by 16 publications

References 31 publications

Mechanism of Targeted Regulation of Ovalbumin Epitopes by Pulsed Electric Field-Assisted Alcalase Treatment

Mechanism of Targeted Regulation of Ovalbumin Epitopes by Pulsed Electric Field-Assisted Alcalase Treatment

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

Fish proteins as potential precursors of taste‐active compounds: an in silico study

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