Effects of different proteases on the emulsifying capacity, rheological and structure characteristics of preserved egg white hydrolysates

Ai, Minmin; Tang, Ting; Zhou, Ledan; Ling, Ziting; Guo, Shouwu; Jiang, Aimin

doi:10.1016/j.foodhyd.2018.09.023

Cited by 121 publications

(67 citation statements)

References 45 publications

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“…As noted in Table , with enzymatic hydrolysis, the ratio of α ‐helices to β ‐turns increased, while the proportion of β ‐sheets diminished compared with the untreated PPI sample. These outcomes are consistent with those published previously for protein hydrolysis …”

Section: Ftirsupporting

confidence: 93%

“…The native potato protein spectrum in the 3200–3400 cm −1 regions had more intensity than the other specimens and, with increasing DH, a decreasing trend appeared. This change might have been attributed to the destruction of hydrogen bonds of hydroxyl (OH) groups during enzymatic hydrolysis and a reduction in their density and strength …”

Section: Ftirmentioning

confidence: 99%

“…Most processed foods are acidic and close to the food proteins' isoelectric points . For that reason, many researchers have considered altering proteins to modify their functional characteristics over a wide pH range …”

Section: Introductionmentioning

confidence: 99%

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Functional and conformational properties of proteolytic enzyme‐modified potato protein isolate

2019

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BACKGROUND: Potato protein hydrolysates (PPHs) were preparedwith Alcalase on intact potato protein isolates (PPI), with differenthydrolysis times (0.5-4 h), and functional and conformational properties of resultant hydrolysates were investigated. RESULTS:The degree of hydrolysis changed during incubation. Peptide bond cleavage increased and hydrolysis progressed rapidly. Gel electrophoresis showed that, by increasing the hydrolysis time, peptides with an apparent molecular weight below 20 kDa increased. It also revealed that, among potato protein components, patatin was more sensitive to Alcalase ® hydrolysis than protease inhibitors. Enzymatic hydrolysis significantly enhanced the solubility and foam capacity of PPHs, but impaired foam stability (P < 0.05). Limited enzymatic hydrolysates (0.5PPH) at the interface improved the emulsion activity and stability index. These emulsions also had the smallest z-average and polydispersity index and showed the highest zeta potential. Fourier-transform infrared spectrometry (FTIR) analysis indicated extensive disruption of hydrogen bonds in PPHs, besides augmentation of -helices and -turns, and a decline in the -sheets in the secondary structure of the PPHs was shown.CONCLUSION: Potato protein isolate, especially 0.5PPH, has good functional and conformational properties. Overall, our results provide new insights into the use of potato protein hydrolysates as a functional food component in the food industry.

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Section: Ftirsupporting

confidence: 93%

Section: Ftirmentioning

confidence: 99%

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Functional and conformational properties of proteolytic enzyme‐modified potato protein isolate

2019

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“…The hydrophobic effect is considered as the main force that maintains the tertiary structure of the protein. It is important to investigate surface hydrophobicity to further reveal the spatial structure and functional characteristics of the protein . The increase in surface hydrophobicity in the protein enhanced its affinity for the droplet surface, and this led to a stronger binding ability of the protein and oil droplet .…”

Section: Discussionmentioning

confidence: 99%

“…It is important to investigate surface hydrophobicity to further reveal the spatial structure and functional characteristics of the protein. 28 The increase in surface hydrophobicity in the protein enhanced its affinity for the droplet surface, and this led to a stronger binding ability of the protein and oil droplet. 19 Hence, surface hydrophobicity plays an important role in determining the emulsifying properties of proteins and peptides.…”

Section: Discussionmentioning

confidence: 99%

Effect of enzyme types on the stability of oil‐in‐water emulsions formed with rice protein hydrolysates

et al. 2019

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BACKGROUND Common oil‐in‐water plant‐based emulsions are allergenic and unstable to environmental stress, leading to increased consumer concerns about the food industry. To solve the problem of safety and instability, we investigated the influence of environmental stress on the stability of emulsions containing various rice protein hydrolysates, and compared the performance to whey protein, a common food emulsifier. RESULTS Rice protein hydrolysates were obtained by enzymatic hydrolysis with different proteases (neutrase, trypsin and alcalase). We evaluated the stability of emulsions produced with different hydrolysates according to storage, pH, ionic strength and thermal processing. Trypsin hydrolysates formed emulsion as stable as emulsion containing whey protein against a range of environmental stress containing pH (pH 6 to 7), salt (< 150 mmol L–1 NaCl) and temperature (30–90 °C). Moreover, a higher partition coefficient of protein in emulsion showed that the trypsin hydrolysates were easy to adsorb at the oil–water droplet interface, indicating its higher stability. CONCLUSION The results obtained in the present study suggest that trypsin hydrolysates could be utilized as natural emulsifiers to stabilize emulsion instead of traditional animal‐based emulsifiers, opening many opportunities with respect to hypoallergenic emulsion systems in the food industry. © 2019 Society of Chemical Industry

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Brittleness mechanism of pork meatballs revealed from molecular structure to macroscopic performance

Xiao

et al. 2023

Food Bioengineering

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Meatballs are manufactured with great craftsmanship, but the brittle quality of meatballs is not resistant to frozen storage, which limits the large‐scale promotion of meatballs for transportation. Meanwhile, the ‘brittle mechanism’ of meatballs is still unclear and it is difficult to solve the scientific problem of brittle quality loss of meatballs from the root. This study revealed the mechanism underlying the brittleness of pork meatballs gel. In this study, the rheological properties, textural quality, molecular forces and microstructure of meatballs were characterized using fresh meat (FsM group), ambient meat group, frozen meat group, and ground meat group. The results showed that the FsM group presented better sensorial characteristics. The rheological properties of the FsM group exhibited higher storage modulus (G′) and loss modulus (G″), indicating better viscoelastic properties. The results of textural determination reflected that the FsM group showed improved brittleness quality and the brittleness was supported by hydrophobic interactions and disulfide bonds. The FsM group with good brittleness quality formed a ‘large cavity’ microstructure. The correlations analysis revealed a correlation between the texture properties of meatballs and their protein molecular forces. Our findings clearly provide new insights into the mechanism underlying the brittleness of meatballs.

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Effects of different proteases on the emulsifying capacity, rheological and structure characteristics of preserved egg white hydrolysates

Cited by 121 publications

References 45 publications

Functional and conformational properties of proteolytic enzyme‐modified potato protein isolate

Functional and conformational properties of proteolytic enzyme‐modified potato protein isolate

Effect of enzyme types on the stability of oil‐in‐water emulsions formed with rice protein hydrolysates

Brittleness mechanism of pork meatballs revealed from molecular structure to macroscopic performance

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