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Enzymes Function and Application in Food Products and Biomaterials
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Enzymes Function and Application in Food Products and Biomaterials

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Biotechnology".

Deadline for manuscript submissions: closed (31 January 2023) | Viewed by 9463

Special Issue Editors

Prof. Dr. Rotimi Aluko

grade E-Mail Website
Guest Editor
Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, MB R3T 2N2, Canada
Interests: food proteins; functional properties; bioactive peptides; spontaneously hypertensive rats; circular dichroism; protein hydrolysates; enzyme inhibition kinetics; angiotensin converting enzyme; renin; QSAR; antioxidants; antihypertensive
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Chibuike C. Udenigwe

E-Mail Website
Guest Editor
1. School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, Ottawa, ON K1H 8M5, Canada
2. Department of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, ON K1N 6N5, Canada
Interests: food biochemistry; protein chemistry; bioactive peptides; functional foods; bioprocessing; food matrix interaction; bioaccessibility; nanodelivery systems; biomolecular interactions
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzymes are biological tools that enable the synthesis or modification of compounds and polymers that are of critical relevance to the food system. However, more importantly, enzymes can be used to create new ingredients or bioactive compounds suitable for high-quality food product development or improved human health, respectively. In this Special Issue, we welcome original research or review manuscripts that showcase the utility of enzymes as efficient tools for various aspects of food research. Specifically, the role of enzymes in creating new food materials will also be a focus. In addition, manuscripts that report on the structure-function properties of enzymes, especially as targets for bioactive molecules are strongly encouraged.

Prof. Dr. Rotimi Aluko
Prof. Dr. Chibuike C. Udenigwe
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 submissions that pass pre-check are 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. Foods is an international peer-reviewed open access semimonthly 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 2900 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

  • food enzymes
  • enzymatic processing
  • sustainable processing
  • immobilized enzymes
  • biocatalysis
  • bioprocessing
  • enzymatic modification
  • enzyme technology
  • microbial enzymes
  • plant enzymes
  • novel enzymes

Published Papers (4 papers)

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Research

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12 pages, 1260 KiB  
Article
Bati Butter as a Potential Substrate for Lipase Production by Aspergillus terreus NRRL-255
by Karen dos Santos Barros, Cristiane Fernandes de Assis, Millena Cristiane de Medeiros Bezerra Jácome, Wendell Medeiros de Azevedo, Adriana M. Zanbotto Ramalho, Everaldo Silvino dos Santos, Thaís Souza Passos, Francisco Canindé de Sousa Junior and Karla Suzanne Florentino da Silva Chaves Damasceno
Foods 2023, 12(3), 564; https://doi.org/10.3390/foods12030564 - 27 Jan 2023
Viewed by 1653
Abstract
This study evaluated bati butter (Ouratea parviflora) as a substrate for lipase production by solid-state fermentation (SSF) using Aspergillus terreus NRRL-255. A gas chromatograph with a flame ionization detector determined the bati butter fatty acid profile. Lipase production and spore count [...] Read more.
This study evaluated bati butter (Ouratea parviflora) as a substrate for lipase production by solid-state fermentation (SSF) using Aspergillus terreus NRRL-255. A gas chromatograph with a flame ionization detector determined the bati butter fatty acid profile. Lipase production and spore count were optimized using a 32 experimental design and evaluated using the response surface methodology. Moreover, the crude enzyme extract was evaluated against different pH, temperature, and activating and inhibitors reagents. Regarding the fatty acids identified, long-chain accounted for 78.60% of the total lipids. The highest lipase production was obtained at 35 °C and 120 h of fermentation, yielding 216.9 U g−1. Crude enzyme extract presented more significant activity at 37 °C and pH 9. β-Mercaptoethanol increased the enzyme activity (113.80%), while sodium dodecyl sulfate inactivated the enzyme. Therefore, bati butter proved to be a potential substrate capable of inducing lipase production by solid-state fermentation. Full article
(This article belongs to the Special Issue Enzymes Function and Application in Food Products and Biomaterials)
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14 pages, 5215 KiB  
Article
A Novel Endo-Polygalacturonase from Penicillium rolfsii with Prebiotics Production Potential: Cloning, Characterization and Application
by Meng-Jie Hao, Dan Wu, Yan Xu, Xiu-Mei Tao, Ning Li and Xiao-Wei Yu
Foods 2022, 11(21), 3469; https://doi.org/10.3390/foods11213469 - 01 Nov 2022
Cited by 1 | Viewed by 1931
Abstract
In this study, a potential producer of prebiotics, a novel endo-polygalacturonase pePGA from Penicillium rolfsii BM-6, was successfully expressed in Komagataella phaffii, characterized and applied to produce pectic oligosaccharides. The optimum temperature and pH of pePGA were 60 °C and 6.0. The [...] Read more.
In this study, a potential producer of prebiotics, a novel endo-polygalacturonase pePGA from Penicillium rolfsii BM-6, was successfully expressed in Komagataella phaffii, characterized and applied to produce pectic oligosaccharides. The optimum temperature and pH of pePGA were 60 °C and 6.0. The purified recombinant enzyme showed a good pH stability and was stable from pH 3.5 to 8.0. The Km, Vmax and kcat values of pePGA were 0.1569 g/L, 12,273 μmol/min/mg and 7478.4 s−1, respectively. More importantly, pePGA-POS, the pePGA hydrolysis products from commercial pectin, had good prebiotic and antibacterial activities in vitro. The pePGA-POS was able to significantly promote the growth of probiotics; meanwhile, the growth of Escherichia coli JM109, Staphylococcus aureus and Bacillus subtilis 168 was effectively inhibited by pePGA-POS. In addition, pePGA-POS also had the DPPH radical scavenging capacity. These properties of pePGA-POS make pePGA attractive for the production of prebiotics. Full article
(This article belongs to the Special Issue Enzymes Function and Application in Food Products and Biomaterials)
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23 pages, 4566 KiB  
Article
Development of a Tailored Sol-Gel Immobilized Biocatalyst for Sustainable Synthesis of the Food Aroma Ester n-Amyl Caproate in Continuous Solventless System
by Corina Vasilescu, Cristina Paul, Simona Marc, Iosif Hulka and Francisc Péter
Foods 2022, 11(16), 2485; https://doi.org/10.3390/foods11162485 - 17 Aug 2022
Cited by 4 | Viewed by 1786
Abstract
This study reports the synthesis of a hybrid sol-gel material, based on organically modified silanes (ORMOSILs) with epoxy functional groups, and its application in the stabilization of lipase type B from Candida antarctica (CalB) through sol-gel entrapment. The key immobilization parameters in the [...] Read more.
This study reports the synthesis of a hybrid sol-gel material, based on organically modified silanes (ORMOSILs) with epoxy functional groups, and its application in the stabilization of lipase type B from Candida antarctica (CalB) through sol-gel entrapment. The key immobilization parameters in the sol-gel entrapment of lipase using epoxysilanes were optimized by the design of numerous experiments, demonstrating that glycidoxypropyl-trimethoxysilane can allow the formation of a matrix with excellent properties in view of the biocatalytic esterifications catalyzed by this lipase, at an enzyme loading of 25 g/mol of silane. The characterization of the immobilized biocatalyst and the correlation of its catalytic efficiency with the morphological and physicochemical properties of the sol-gel matrix was accomplished through scanning electron microscopy (SEM), fluorescence microscopy (FM), as well as thermogravimetric and differential thermal analysis (TGA/DTA). The operational and thermal stability of lipase were increased as a result of immobilization, with the entrapped lipase retaining 99% activity after 10 successive reaction cycles in the batch solventless synthesis of n-amyl caproate. A possible correlation of optimal productivity and yield was attempted for this immobilized lipase via the continuous flow synthesis of n-amyl caproate in a solventless system. The robustness and excellent biocatalytic efficiency of the optimized biocatalyst provide a promising solution for the synthesis of food-grade flavor esters, even at larger scales. Full article
(This article belongs to the Special Issue Enzymes Function and Application in Food Products and Biomaterials)
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Review

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18 pages, 2631 KiB  
Review
Progress in the Conversion of Ginsenoside Rb1 into Minor Ginsenosides Using β-Glucosidases
by Hongrong Zhu, Rui Zhang, Zunxi Huang and Junpei Zhou
Foods 2023, 12(2), 397; https://doi.org/10.3390/foods12020397 - 13 Jan 2023
Cited by 7 | Viewed by 2886
Abstract
In recent years, minor ginsenosides have received increasing attention due to their outstanding biological activities, yet they are of extremely low content in wild ginseng. Ginsenoside Rb1, which accounts for 20% of the total ginsenosides, is commonly used as a precursor to produce [...] Read more.
In recent years, minor ginsenosides have received increasing attention due to their outstanding biological activities, yet they are of extremely low content in wild ginseng. Ginsenoside Rb1, which accounts for 20% of the total ginsenosides, is commonly used as a precursor to produce minor ginsenosides via β-glucosidases. To date, many research groups have used different approaches to obtain β-glucosidases that can hydrolyze ginsenoside Rb1. This paper provides a compilation and analysis of relevant literature published mainly in the last decade, focusing on enzymatic hydrolysis pathways, enzymatic characteristics and molecular mechanisms of ginsenoside Rb1 hydrolysis by β-glucosidases. Based on this, it can be concluded that: (1) The β-glucosidases that convert ginsenoside Rb1 are mainly derived from bacteria and fungi and are classified as glycoside hydrolase (GH) families 1 and 3, which hydrolyze ginsenoside Rb1 mainly through the six pathways. (2) Almost all of these β-glucosidases are acidic and neutral enzymes with molecular masses ranging from 44–230 kDa. Furthermore, the different enzymes vary widely in terms of their optimal temperature, degradation products and kinetics. (3) In contrast to the GH1 β-glucosidases, the GH3 β-glucosidases that convert Rb1 show close sequence-function relationships. Mutations affecting the substrate binding site might alter the catalytic efficiency of enzymes and yield different prosapogenins. Further studies should focus on elucidating molecular mechanisms and improving overall performances of β-glucosidases for better application in food and pharmaceutical industries. Full article
(This article belongs to the Special Issue Enzymes Function and Application in Food Products and Biomaterials)
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