Effect of transglutaminase on taste characteristics of pea protein hydrolysates through altering the composition of amino acids and peptides

Su, Guowan; Xie, Yuxi; Liu, Ruili; Cui, Guodong; Zhao, Mouming; Zhang, Jianan

doi:10.1016/j.fbio.2023.103261

Cited by 10 publications

(4 citation statements)

References 28 publications

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“…51 The bitter peptides contain a high proportion of hydrophobic amino acids at both ends, leading to a bitter taste. 52 As shown in Fig. 5(B), compared to SPIA, the overall content of FAAs in SPIACP-M2 increased by 28% (P < 0.05).…”

Section: Effects Of Metal Ions and Inhibitors On Enzyme Activitymentioning

confidence: 75%

Enhancing the catalytic efficiency of M32 carboxypeptidase by semi‐rational design and its applications in food taste improvement

Wang,

Lu,

Zhuge

et al. 2024

J Sci Food Agric

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BackgroundCarboxypeptidase is an exopeptidase that hydrolysis amino acids at the C‐terminal end of the peptide chain and has a wide range of applications in food. However, in industrial applications, the relatively low catalytic efficiency of carboxypeptidases is one of the main limiting factors for industrialization.ResultsThe study has elevated the catalytic efficiency of Bacillus megaterium M32 carboxypeptidase (BmeCPM32) through semi‐rational design. Firstly, the optimal mutant, BmeCPM32‐M2, obtained through single‐site mutagenesis and combinatorial mutagenesis, specific activity was 2.2‐fold higher than that of the wild type (187.9 vs. 417.8 U mg−1), and catalytic efficiency was 2.9‐fold higher (110.14 vs. 325.75 s−1 mM−1). Secondly, compared to the wild type, BmeCPM32‐M2 exhibited a 1.8‐fold increase in half‐life at 60 °C, with no significant changes in its enzymatic properties (optimal pH, optimal temperature). Finally, BmeCPM32‐M2 significantly increased the umami intensity of soy protein isolate hydrolysate (SPIA) by 55% and reduced bitterness by 83%, indicating its potential in developing tasty protein components.ConclusionOur research has revealed that the strategy based on protein sequence evolution and computational residue mutation energy has improved the catalytic efficiency of BmeCPM32. Molecular dynamics simulations have revealed that a smaller substrate binding pocket and increased enzyme‐substrate affinity are the reasons for enhancing catalytic efficiency, Furthermore the number of hydrogen bonds and solvent and surface area, which may contribute to the improvement of thermostability. Finally, the de‐bittering effect of BmeCPM32‐M2 in soy protein isolate hydrolysate suggests its potential in developing palatable protein components.This article is protected by copyright. All rights reserved.

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Section: Effects Of Metal Ions and Inhibitors On Enzyme Activitymentioning

confidence: 75%

Enhancing the catalytic efficiency of M32 carboxypeptidase by semi‐rational design and its applications in food taste improvement

Wang,

Lu,

Zhuge

et al. 2024

J Sci Food Agric

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“…The two-dimensional diagrams of the eight peptides are displayed in Figure 5, and the molecular docking scores are provided in Table 2. These scores demonstrate that all eight peptides can bind to the Venus flytrap (VFT) binding domains of T1R1/T1R3 [47]. Throughout the docking process, the T1R1/T1R3 receptor structure remains fixed, while the peptide structure adapts its conformation.…”

Section: Identification and Molecular Docking Of Peptidesmentioning

confidence: 94%

Taste-Active Peptides from Triple-Enzymatically Hydrolyzed Straw Mushroom Proteins Enhance Salty Taste: An Elucidation of Their Effect on the T1R1/T1R3 Taste Receptor via Molecular Docking

Song,

Cheng,

Wangzhang

et al. 2024

Foods

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The objective of our study was to analyze and identify enzymatic peptides from straw mushrooms that can enhance salty taste with the aim of developing saltiness enhancement peptides to reduce salt intake and promote dietary health. We isolated taste-related peptides from the straw mushroom extract using ultrafiltration and identified them using UPLC-Q-TOF-MS/MS. The study found that the ultrafiltration fraction (500–2000 Da) of straw mushroom peptides had a saltiness enhancement effect, as revealed via subsequent E-tongue and sensory analyses. The ultrafiltration fractions (500–2000 Da) were found to contain 220 peptides, which were identified through UPLC-Q-TOF-MS/MS analysis. The interaction of these peptides with the T1R1/T1R3 receptor was also assessed. The investigation highlighted the significant involvement of Asp223, Gln243, Leu232, Asp251, and Pro254 in binding peptides from triple-enzymatically hydrolyzed straw mushrooms to T1R1/T1R3. Based on the binding energy and active site analysis, three peptides were selected for synthesis: DFNALPFK (−9.2 kcal/mol), YNEDNGIVK (−8.8 kcal/mol), and VPGGQEIKDR (−8.9 kcal/mol). Importantly, 3.2 mmol of VPGGQEIKDR increased the saltiness level of a 0.05% NaCl solution to that of a 0.15% NaCl solution. Additionally, the addition of 0.8 mmol of YNEDNGIVK to a 0.05% NaCl solution resulted in the same level of saltiness as a 0.1% NaCl solution.

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“…To investigate its hydrolysis efficiency, the protein recovery and DH of elastin hydrolysates obtained at different hydrolysis times by Alcalase ® 2.4L were evaluated. The former denotes the retained protein post-hydrolysis, the latter measures the extent to which protein is broken down into peptides and amino acids [7]. As shown in Figure 1A, the protein recovery increased rapidly with prolonging hydrolysis time (from 27.75% to 44.19%) and then tended to plateau (48.44% at 24 h).…”

Section: Introductionmentioning

confidence: 97%

“…They are predominantly procured through the enzymatic hydrolysis of protein-abundant food materials [6]. This hydrolysis, however, produces a myriad of products, with peptide profiles that differ based on enzyme specificity and hydrolytic conditions [7]. Such variations can directly influence the bioactivity of the resulting hydrolysates.…”

Section: Introductionmentioning

confidence: 99%

Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping

Zhang,

Liu,

Jiang

et al. 2023

Molecules

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To enhance the understanding of enzymatic hydrolysis and to accelerate the discovery of key bioactive peptides within enzymatic products, this research focused on elastin as the substrate and investigated the variations in peptide profiles and the production of key bioactive peptides (those exceeding 5% of the total) and their impacts on the biological activity of the hydrolysates. Through the application of advanced analytical techniques, such as stop-flow two-dimensional liquid chromatography and ultra-high-performance liquid chromatography-tandem mass spectrometry, the research tracks the release and profiles of peptides within elastin hydrolysates (EHs). Despite uniform peptide compositions, significant disparities in peptide concentrations were detected across the hydrolysates, hinting at varying levels of bioactive efficacy. A comprehensive identification process pinpointed 403 peptides within the EHs, with 18 peptides surpassing 5% in theoretical maximum content, signaling their crucial role in the hydrolysate’s bioactivity. Of particular interest, certain peptides containing sequences of alanine, valine, and glycine were released in higher quantities, suggesting Alcalase® 2.4L’s preference for these residues. The analysis not only confirms the peptides’ dose-responsive elastase inhibitory potential but also underscores the nuanced interplay between peptide content, biological function, and their collective synergy. The study sets the stage for future research aimed at refining enzymatic treatments to fully exploit the bioactive properties of elastin.

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Effect of transglutaminase on taste characteristics of pea protein hydrolysates through altering the composition of amino acids and peptides

Cited by 10 publications

References 28 publications

Enhancing the catalytic efficiency of M32 carboxypeptidase by semi‐rational design and its applications in food taste improvement

Enhancing the catalytic efficiency of M32 carboxypeptidase by semi‐rational design and its applications in food taste improvement

Taste-Active Peptides from Triple-Enzymatically Hydrolyzed Straw Mushroom Proteins Enhance Salty Taste: An Elucidation of Their Effect on the T1R1/T1R3 Taste Receptor via Molecular Docking

Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping

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