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Processes
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Application of Proteomics and Enzyme Technologies in Foods
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Application of Proteomics and Enzyme Technologies in Foods

A special issue of Processes (ISSN 2227-9717). This special issue belongs to the section "Food Process Engineering".

Deadline for manuscript submissions: closed (28 February 2022) | Viewed by 14713

Special Issue Editors

Prof. Dr. Jung-Feng Hsieh

E-Mail Website
Guest Editor
Department of Food Science, Fu Jen Catholic University, No. 510, Zhongzheng Rd., Xinzhuang Dist., New Taipei City 242062, Taiwan
Interests: food proteomics; enzymology; enzyme inhibitors
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Tai-Yuan Chen

E-Mail Website
Guest Editor
Department of Food Science, National Taiwan Ocean University, No.2, Beining Rd., Zhongzheng Dist., Keelung City 20224, Taiwan
Interests: proteomics; food chemistry; marine biochemistry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protein from plant and animal sources is among the most important elements in one’s diet. The physical and chemical makeup of a protein determines its functional role in growth, maintenance, nutrient storage, or as an enzyme. For over a decade, the study of dietary proteins has relied on proteomic analysis to identify and quantify the entire complement of proteins expressed by a cell (i.e., the proteome). Much of this work focuses on the separation of complex protein or peptide samples via two-dimensional gel electrophoresis, high-performance liquid chromatography, and mass spectrometry. These methods can be used to monitor changes in the protein composition of processed foods and the study of food allergies. They can also be used to authenticate the quality and safety of food items. At a more fundamental level, proteomics has been used to investigate protein–protein interactions as well as to the interactions between proteins and other food components in raw and processed foods.

This Special Issue, devoted to "Application of Proteomics and Enzyme Technologies in Foods," invites high-quality research papers focusing on the proteomics or/and enzymes within the context of food. Topics of interest include the following:

  • Proteomics for analysis and identification of food allergens;
  • Proteomics for evaluation of food authentication, quality, and safety;
  • Proteomics and enzyme technologies for dairy, egg, meat, and cereals;
  • Enzymes used in food processing;

Prof. Dr. Jung-Feng Hsieh
Prof. Dr. Tai-Yuan Chen
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Processes is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Proteomics
  • Mass spectrometry
  • Two-dimensional gel electrophoresis
  • Protease
  • Transglutaminase
  • Food authentication
  • Food allergens
  • Food safety

Published Papers (8 papers)

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Editorial

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3 pages, 174 KiB  
Editorial
Special Issue: Application of Proteomics and Enzyme Technologies in Foods
by Jung-Feng Hsieh
Processes 2023, 11(6), 1817; https://doi.org/10.3390/pr11061817 - 15 Jun 2023
Viewed by 630
Abstract
This Special Issue entitled “Application of Proteomics and Enzyme Technologies in Foods” explores the latest progress and perspectives on the development and application of enzyme technologies, proteomics, and bioprocessing in the context of food science [...] Full article
(This article belongs to the Special Issue Application of Proteomics and Enzyme Technologies in Foods)

Research

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12 pages, 5277 KiB  
Article
Ultrasound-Assisted Transglutaminase Catalysis of the Cross-Linking and Microstructure of αs-Casein, β-Casein and κ-Casein
by Chun-Chi Chen, Liang-Yu Chen, Wen-Tai Li, Ken-Lin Chang, Hsien-Wei Tseng, Bang-Yuan Chen, Chao-Jung Chen and Jung-Feng Hsieh
Processes 2021, 9(9), 1630; https://doi.org/10.3390/pr9091630 - 09 Sep 2021
Cited by 4 | Viewed by 1812
Abstract
The effects of ultrasonic treatment (UT)-assisted transglutaminase (TGase) catalysis on the physicochemical properties of individual αs-casein (αs-CN), β-casein (β-CN), and κ-casein (κ-CN) were investigated. After 60 min of incubation at 30 °C, αs-CN, β-CN, and κ-CN were [...] Read more.
The effects of ultrasonic treatment (UT)-assisted transglutaminase (TGase) catalysis on the physicochemical properties of individual αs-casein (αs-CN), β-casein (β-CN), and κ-casein (κ-CN) were investigated. After 60 min of incubation at 30 °C, αs-CN, β-CN, and κ-CN were cross-linked with TGase (6.0 units/mL), and high molecular weight polymers (>200 kDa) were formed. The use of TGase in conjunction with UT (20 kHz, power of 400 W, and amplitude 20%) led to an increase in the rate of αs-CN, β-CN, and κ-CN polymerization compared to the individual casein that contained TGase but did not undergo UT. SDS-PAGE scrutiny showed that the intensities of αs-CN, β-CN, and κ-CN incubation with regard to TGase and UT at 30 °C for 60 min noticeably decreased to 5.66 ± 0.39, 3.97 ± 0.43, and 26.07 ± 1.18%, respectively (p < 0.05). Particle size analysis results indicated that the molecule size appropriation for the cross-linking of αs-CN, β-CN, and κ-CN ranged from 6000 to 10,000 nm after 60 min incubation with TGase and UT. Transmission electron microscopy investigation showed network structures of cross-linking αs-CN, β-CN, and κ-CN were formed from αs-CN, β-CN, and κ-CN, respectively. As our results show, the comprehensive utilization of TGase and UT will be a superior method for the polymerization of αs-CN, β-CN, and κ-CN. Full article
(This article belongs to the Special Issue Application of Proteomics and Enzyme Technologies in Foods)
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21 pages, 1382 KiB  
Article
Optimization of Texture-Modified Yellowfin Sole (Pleuronectes aspera) by Enzymatic Treatment and Superheated Steam Treating to Improve Quality Characteristics
by Woo-Hee Cho, Sung-Joon Yoon and Jae-Suk Choi
Processes 2021, 9(5), 763; https://doi.org/10.3390/pr9050763 - 27 Apr 2021
Cited by 6 | Viewed by 1883
Abstract
This study aimed to optimize the texture modification process of yellowfin sole (Pleuronectes aspera) to improve its quality characteristics for easier consumption by the elderly. Yellowfin sole was immersed in enzyme solution (Protamex:Neutrase = 1:2), marinated in herbal extract solution, and [...] Read more.
This study aimed to optimize the texture modification process of yellowfin sole (Pleuronectes aspera) to improve its quality characteristics for easier consumption by the elderly. Yellowfin sole was immersed in enzyme solution (Protamex:Neutrase = 1:2), marinated in herbal extract solution, and roasted by superheated steam. The product was evaluated for microbial, physicochemical, and sensory properties, as well as shelf life. Specifically, the optimal enzymatic treatment comprised a protease concentration of 1.00% (w/v) with an immersion time of 3.16 h. The optimal marination herb was determined to be bay leaves, as indicated by highest overall acceptance. The texture modification process led to lower hardness and higher overall acceptance values (76.23 kN/m2 and 8.38, respectively) compared with nonenzyme processed product (120.43 kN/m2, 7.43), also retaining high nutritional value and low trimethylamine levels. Shelf-life analysis indicated microbial activity was inhibited (not detected), low levels of total volatile basic nitrogen (10.50 mg%), low levels of thiobarbituric acid reactive substances (0.12 mg MDA/kg), and stable pH values (6.5–7.0). Overall, the texture-modified yellowfin sole possessed a soft flesh texture suitable for consumption by the elderly, with acceptable microbial, physicochemical, and sensory qualities. Full article
(This article belongs to the Special Issue Application of Proteomics and Enzyme Technologies in Foods)
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18 pages, 1674 KiB  
Article
Food-Derived Bioactive Peptides with Antioxidative Capacity, Xanthine Oxidase and Tyrosinase Inhibitory Activity
by Anthony Thaha, Bor-Sen Wang, Yu-Wei Chang, Shih-Min Hsia, Tsui-Chin Huang, Chyuan-Yuan Shiau, Deng-Fwu Hwang and Tai-Yuan Chen
Processes 2021, 9(5), 747; https://doi.org/10.3390/pr9050747 - 23 Apr 2021
Cited by 24 | Viewed by 3957
Abstract
Bioactive peptides (BPs) released by proteases from different food protein sources are often served as antioxidants in food applications. This study aims to investigate 11 BPs derived from fish and egg white as potential natural antioxidants by antioxidant activity assays. The kinetic activity [...] Read more.
Bioactive peptides (BPs) released by proteases from different food protein sources are often served as antioxidants in food applications. This study aims to investigate 11 BPs derived from fish and egg white as potential natural antioxidants by antioxidant activity assays. The kinetic activity of the BPs against xanthine oxidase (XOD) and tyrosinase was also analyzed. The antioxidative capacity of the BPs indicated that VWWW (VW4, mackerel meat), followed by IRW (IW3, egg white) and VKAGFAWTANQQLS (VS14, tuna backbone protein), possessed the highest antioxidant activity in 1,1-diphenyl-2-picrylhydrazyl radical (DPPH), 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) and reducing power (RP) assays. Both the free-radical scavenging score predicted from the AnOxPePred algorithm and the DPPH, ABTS and RP results indicated that VW4 was the best antioxidant. Furthermore, the XOD and tyrosinase inhibition by three selected peptides exhibited competitive patterns of effective inhibition. The half maximal inhibitory concentrations (IC50) of the peptides for XOD inhibition were 5.310, 3.935, and 1.804 mM for VW4, IW3, and VS14, respectively, and they could serve as competitive natural XOD inhibitors. The IC50 of the peptides for tyrosinase inhibition were 1.254, 2.895, and 0.595 mM for VW4, IW3, and VS14, respectively. Overall, VW4, IW3, and VS14 are potential antioxidants and natural XOD inhibitors for preventing milk-fat oxidation, and anti-browning sources for inhibiting food-derived tyrosinase oxidation. Full article
(This article belongs to the Special Issue Application of Proteomics and Enzyme Technologies in Foods)
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11 pages, 3698 KiB  
Article
Production of Phenyllactic Acid from Porphyra Residues by Lactic Acid Bacterial Fermentation
by Chung-Hsiung Huang, Wei-Chen Chen, Yu-Huei Gao, Hsin-I Hsiao and Chorng-Liang Pan
Processes 2021, 9(4), 678; https://doi.org/10.3390/pr9040678 - 13 Apr 2021
Cited by 10 | Viewed by 2017
Abstract
The concept of algae biorefinery is attracting attention because of the abundant valuable compounds within algal biomass. Phenyllactic acid (PhLA), a broad-spectrum antimicrobial organic acid that can be produced by lactic acid bacteria (LAB), is considered a potential biopreservative. In this study, a [...] Read more.
The concept of algae biorefinery is attracting attention because of the abundant valuable compounds within algal biomass. Phenyllactic acid (PhLA), a broad-spectrum antimicrobial organic acid that can be produced by lactic acid bacteria (LAB), is considered a potential biopreservative. In this study, a cascading biorefinery approach was developed to harvest PhLA from Porphyra residues by LAB fermentation. LAB strains were cultivated in de Man, Rogosa and Sharpe (MRS) broth to screen their ability to produce PhLA. As the strains of Lactobacillus plantarum KP3 and L. plantarum KP4 produced higher concentrations of PhLA at 0.09 mg/mL, these two strains were employed for fermentation. After phycobiliprotein extraction, the Porphyra residues, ultrafiltration eluate, phenylalanine (Phe) and yeast extract with a volume of 20 mL were inoculated with LAB strain KP3 and fermented at 37 °C for 120 h. The PhLA content of the fermented broth was 1.86 mg. To optimize the biorefinery process, the ultrafiltration eluate was replaced by commercial cellulase. Up to 4.58 mg of PhLA, which was 2.5 times greater than that produced from KP3 cultured in MRS broth, could be harvested. Taken together, the findings provide an optimized process for LAB fermentation, which is shown to be a feasible algae biorefinery approach to obtaining PhLA from Porphyra residues. Full article
(This article belongs to the Special Issue Application of Proteomics and Enzyme Technologies in Foods)
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12 pages, 2459 KiB  
Article
Enzyme-Assisted Method for Phycobiliproteins Extraction from Porphyra and Evaluation of Their Bioactivity
by Chung-Hsiung Huang, Wei-Chen Chen, Yu-Huei Gao, Guan-Wen Chen, Hong-Ting Victor Lin and Chorng-Liang Pan
Processes 2021, 9(3), 560; https://doi.org/10.3390/pr9030560 - 23 Mar 2021
Cited by 10 | Viewed by 2580
Abstract
Due to the poor protein availability of algae in their unprocessed form, development of extraction methods for phycobiliproteins is of great significance. This study aimed to extract phycoerythrin (PE) and phycocyanin (PC) from Porphyra via bacterial enzymatic hydrolysis and to evaluate their bioactivity. [...] Read more.
Due to the poor protein availability of algae in their unprocessed form, development of extraction methods for phycobiliproteins is of great significance. This study aimed to extract phycoerythrin (PE) and phycocyanin (PC) from Porphyra via bacterial enzymatic hydrolysis and to evaluate their bioactivity. To induce enzyme production, Porphyra powder was added into the culture medium of two marine bacterial strains. The pH and enzyme activity of the cultured supernatant, namely crude enzyme solution, were significantly raised. For PE and PC extraction, Porphyra were incubated within crude enzyme solution with homogenization and ultrasonication followed by ultrafiltration process. After distinguishing by fast performance liquid chromatography (FPLC), three major fractions were observed and identified as R-PE, R-PC and small molecular PE by high-performance liquid chromatography (HPLC) and polyacrylamide gel electrophoresis (PAGE) analysis. With respect to bioactivity, these three fractions exhibited free radical scavenging and antioxidant activities in a various degree. In addition, the angiotensin-converting-enzyme (ACE) inhibitory activity of both R-PE and R-PC fractions was observed in a concentration-dependent manner. Taken together, the employed process of bacterial enzymatic hydrolysis is suggested to be a feasible method to obtain PE and PC from Porphyra without limiting their bioactivity. Full article
(This article belongs to the Special Issue Application of Proteomics and Enzyme Technologies in Foods)
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12 pages, 1601 KiB  
Article
A Fructan Sucrase Secreted Extracellular and Purified in One-Step by Gram-Positive Enhancer Matrix Particles
by Jingyue Wang, Huazhi Xiao, Fangkun Zhao, Bo Zhao, Min Xu, Zhijiang Zhou and Ye Han
Processes 2021, 9(1), 95; https://doi.org/10.3390/pr9010095 - 05 Jan 2021
Cited by 7 | Viewed by 1974
Abstract
Fructan sucrase is a kind of biological enzyme that catalyzes the synthesis of fructan, and fructan is a polysaccharide product with important industrial application value. In this study, the Fructan sucrase gene of Bacillus subtilis was cloned to plasmid PET-28A-ACMA-Z, and three clones [...] Read more.
Fructan sucrase is a kind of biological enzyme that catalyzes the synthesis of fructan, and fructan is a polysaccharide product with important industrial application value. In this study, the Fructan sucrase gene of Bacillus subtilis was cloned to plasmid PET-28A-ACMA-Z, and three clones were obtained after the transformation of Escherichia coli BL21, namely BS-FF, BSO, and BS. The clones BS-FF and BSO secreted the recombinant enzymes outside the cells, while the clone BS expressed them inside the cells. The induction experiment results showed that the optimum IPTG concentration in the medium was 0.5 mM and 1.0 mM for clones BS-FF and BSO, respectively, while the incubation conditions were at 28 °C for 8 h. The recombinant fructan sucrase was purified one step using a material called GEM particles. The results indicated that 95.25% of fructan sucrase expressed by the clone BS-FF could be secreted into the extracellular area, and even 98.78% by the clone BSO. With the above purification system, the receiving rate of the recombinant enzyme for clones BS-FF and BSO was 97.70% and 84.99%, respectively. As for the bioactivity of recombinant fructan sucrase, the optimum temperature and pH were 50 °C and 5.6, respectively. The Km and Vmax of it were 33.96 g/L and 0.63 g/(L·min), respectively. The engineered strains with the high extracellular secretion of fructan sucrase were constructed, and a one-step method for the purification of the recombinant enzyme was established. The results might provide a novel selection for the enzymatic production of fructan on a large scale. Full article
(This article belongs to the Special Issue Application of Proteomics and Enzyme Technologies in Foods)
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13 pages, 1429 KiB  
Article
Improved Phenolic Compositions and Sensory Attributes of Red Wines by Saccharomyces cerevisiae Mutant CM8 Overproducing Cell-Wall Mannoproteins
by Phoency F.-H. Lai, Po-Chun Hsu, Bo-Kang Liou, Rupesh D. Divate, Pei-Ming Wang and Yun-Chin Chung
Processes 2020, 8(11), 1483; https://doi.org/10.3390/pr8111483 - 17 Nov 2020
Cited by 2 | Viewed by 1597
Abstract
The objective of this study was to improve the quality attributes of red wines by Saccharomyces cerevisiae (BCRC 21685) mutant CM8 with overexpression of high-mannose mannoproteins, with respective to phenolic compositions, colorimetric parameters, and consumer sensory attributes. The CM8 was mutated by ethyl [...] Read more.
The objective of this study was to improve the quality attributes of red wines by Saccharomyces cerevisiae (BCRC 21685) mutant CM8 with overexpression of high-mannose mannoproteins, with respective to phenolic compositions, colorimetric parameters, and consumer sensory attributes. The CM8 was mutated by ethyl methane sulfonate and showed the ability of overproducing cell wall mannoproteins selected by killer-9 toxin-containing YPD plates. Kyoho grapes were used as raw materials. It is interesting to find that the cell wall mannoproteins isolated from CM8 mutant possessed a significantly higher mannose content in the polysaccharide fraction (81% w/w) than that did from parent strain (66% w/w). The red wines made of winter grapes and CM8 (CM8-WIN) showed significantly greater total tannins, flavonols, and anthocyanins levels, as well as higher color, higher flavor, and higher consumer preference than those by its SC counterpart (SC-WIN). The characteristics of the red wines studied were further elucidated by principal component analysis. Conclusively, using CM8 starter could effectively endow the red wine with high-quality attributes via the interactions of high-mannose mannoproteins with wine compounds. Full article
(This article belongs to the Special Issue Application of Proteomics and Enzyme Technologies in Foods)
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