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Biocatalysts and Biocatalysis in Food Industry
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Biocatalysts and Biocatalysis in Food Industry

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (30 September 2021) | Viewed by 21305

Special Issue Editor

Dr. Marek Adamczak

E-Mail Website
Guest Editor
Department of Process Engineering, Equipment and Food Biotechnology, University of Warmia and Mazury in Olsztyn, Jan Heweliusz St. 1, 10-718 Olsztyn, Poland
Interests: food enzymes; biocatalysis; medium engineering; food compounds modification; enzyme inhibition; lignocellulose hydrolysis; fermentation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

There are about 7800 enzymes classified in the BRENDA database, and a few thousand described in the literature. Enzymes and whole-cell catalysts, active under mild conditions, are traditionally used in food production. The application of enzymes in the food industry ensures the production of high-quality products, food safety and security, and the production of functional food. It also preserves products; increases nutritive values; and improves the taste, flavor, and texture of the food. Enzymes in the food industry play an important role as food processing aids, and in the valorization of waste- and by-products. New enzymes are required for specific applications, and available enzymes need to be improved by using a new toolbox, that is, protein engineering and molecular biology techniques and mutagenesis. Traditional methods of medium engineering are also used (e.g., immobilization). A paradigm shift in designing biocatalytic processes has been observed, and tailoring enzymes to the processing conditions is required. 

This Special Issue collects original research papers, reviews, and opinions focused on the biocatalysts and biocatalysis in the food industry. Submissions are also welcome from outside the areas presented above.

Dr. Marek Adamczak
Guest Editor

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. Catalysts 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 2700 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

  • Enzyme
  • Biocatalysis
  • Food industry
  • Immobilized enzymes
  • Structured food compounds
  • Modification of food compounds
  • Waste- and by-product valorization
  • Enzyme synthesis
  • Enzyme modification
  • Metagenome
  • Directed evolution
  • Adaptive laboratory evolution

Published Papers (6 papers)

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Research

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17 pages, 3637 KiB  
Article
Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins
by Marko Jonović, Milena Žuža, Verica Đorđević, Nataša Šekuljica, Milan Milivojević, Branimir Jugović, Branko Bugarski and Zorica Knežević-Jugović
Catalysts 2021, 11(3), 305; https://doi.org/10.3390/catal11030305 - 26 Feb 2021
Cited by 6 | Viewed by 2725
Abstract
Enzymatic hydrolysis of food proteins is convenient method to improve their functional properties and physiological activity. Herein, the successful covalent attachment of alcalase on alginate micron and submicron beads using the carbodiimide based chemistry reaction and the subsequent application of the beads for [...] Read more.
Enzymatic hydrolysis of food proteins is convenient method to improve their functional properties and physiological activity. Herein, the successful covalent attachment of alcalase on alginate micron and submicron beads using the carbodiimide based chemistry reaction and the subsequent application of the beads for egg white and soy proteins hydrolysis were studied. In addition to the electrostatic extrusion technique (EE) previously used by others, the potential utilization of a novel ultrasonic spray atomization technique without drying (UA) and with drying (UAD) for alginate submicron beads production has been attempted. The immobilization parameters were optimized on microbeads obtained by EE technique (803 ± 23 µm) with respect to enzyme loading and alcalase activity. UA and UAD techniques resulted in much smaller particles (607 ± 103 nm and 394 ± 51 nm in diameter, respectively), enabling even higher enzyme loading of 671.6 ± 4 mg g−1 on the carrier and the highest immobilized alcalase activity of 2716.1 IU g−1 in the standard reaction. The UAD biocatalyst exhibited also better performances in the real food system based on egg white or soy proteins. It has been shown that the immobilized alcalase can be reused in seven successive soy protein hydrolysis cycles with a little decrease in the activity. Full article
(This article belongs to the Special Issue Biocatalysts and Biocatalysis in Food Industry)
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12 pages, 2264 KiB  
Article
Effective Glycosylation of Cucurbitacin Mediated by UDP-Glycosyltransferase UGT74AC1 and Molecular Dynamics Exploration of Its Substrate Binding Conformations
by Shicheng Mu, Jiao Li, Cui Liu, Yan Zeng, Yan Men, Yi Cai, Ning Chen, Hongwu Ma and Yuanxia Sun
Catalysts 2020, 10(12), 1466; https://doi.org/10.3390/catal10121466 - 15 Dec 2020
Cited by 3 | Viewed by 2440
Abstract
Cucurbitacins, a group of diverse tetracyclic triterpenes, display a variety of biological effects. Glycosylation mediated by glycosyltransferases (UGTs) plays a vital role in structural and functional diversity of natural products and influences their biological activities. In this study, GT-SM, a mutant of UGT74AC1 [...] Read more.
Cucurbitacins, a group of diverse tetracyclic triterpenes, display a variety of biological effects. Glycosylation mediated by glycosyltransferases (UGTs) plays a vital role in structural and functional diversity of natural products and influences their biological activities. In this study, GT-SM, a mutant of UGT74AC1 from Siraitia grosvenorii, was chosen as a potential catalyst in glycosylation of cucurbitacins, and its optimal pH, temperature, and divalent metal ions were detected. This enzyme showed high activity (kcat/Km, 120 s−1 µM−1) toward cucurbitacin F 25-O-acetate (CA-F25) and only produced CA-F25 2-O-β-d-glucose which was isolated and confirmed by 1D and 2D nuclear magnetic resonance. A pathway for uridine diphosphate glucose (UDP-Glc) regeneration and cucurbitacin glycoside synthesis was constructed by combing GT-SM and sucrose synthase to cut down the costly UDP-Glc. The molar conversion of CA-F25 was 80.4% in cascade reaction. Molecular docking and dynamics simulations showed that CA-F25 was stabilized by hydrophobic interactions, and the C2-OH of CA-F25 showed more favorable catalytic conformation than that of C3-OH, explaining the high regioselectivity toward the C2-OH rather than the ortho-C3-OH of CA-F25. This work proved the important potential application of UGT74AC1 in cucurbitacins and provided an understanding of glycosylation of cucurbitacins. Full article
(This article belongs to the Special Issue Biocatalysts and Biocatalysis in Food Industry)
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11 pages, 1995 KiB  
Article
Nanoencapsulated Laccases Obtained by Double-Emulsion Technique. Effects on Enzyme Activity pH-Dependence and Stability
by Rocío Chong-Cerda, Laura Levin, Rocío Castro-Ríos, Carlos Eduardo Hernández-Luna, Azucena González-Horta, Guadalupe Gutiérrez-Soto and Abelardo Chávez-Montes
Catalysts 2020, 10(9), 1085; https://doi.org/10.3390/catal10091085 - 18 Sep 2020
Cited by 15 | Viewed by 3241
Abstract
One primary drawback of enzyme catalysis at industrial scale is the short-term service life of the enzymes, they lose their activity due to oxidation or other processes which results in less stability and a shorter lifetime thereby rendering them less efficient. An effective [...] Read more.
One primary drawback of enzyme catalysis at industrial scale is the short-term service life of the enzymes, they lose their activity due to oxidation or other processes which results in less stability and a shorter lifetime thereby rendering them less efficient. An effective way to increase the stability of the enzymes is to attach them to nanoparticles. In this work, the polymer Eudragit® L 100-55 sensitive to pH was used to prepare laccase polymeric nanoparticles by the double-emulsion solvent evaporation approach. The size and morphology of the nanoparticles obtained were evaluated—as well as the encapsulation efficiency and zeta potential. pH effect on activity and stability was compared between free and immobilized laccase. Their stability was also determined in a sequential assay involving acidic pHs up to alkaline ones. The nanoparticles had a spherical shape with a mean size of 147 nm, zeta potential of −22.7 mV at pH 7.0 and load efficiency of 87%. The optimum pH of both free and immobilized laccases was 3.0, being the nanoparticles more stable at acidic pHs. Thus, this would be the first report of obtaining laccase nanoparticles with potential application in animal feed due to the stability conferred to enzymatic activity at pHs similar to those present in the gastrointestinal tract of rabbits, which would allow their potential use in animal feed. Full article
(This article belongs to the Special Issue Biocatalysts and Biocatalysis in Food Industry)
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14 pages, 885 KiB  
Article
Reducing Immunoreactivity of Gliadins and Coeliac-Toxic Peptides Using Peptidases from L. acidophilus 5e2 and A. niger
by Bartosz Brzozowski, Katarzyna Stasiewicz, Mateusz Ostolski and Marek Adamczak
Catalysts 2020, 10(8), 923; https://doi.org/10.3390/catal10080923 - 11 Aug 2020
Cited by 6 | Viewed by 3809
Abstract
Wheat storage proteins and products of their hydrolysis may cause coeliac sprue in genetically predisposed individuals with high expression of main histocompatibility complex HLA-DQ2 or DQ8, since by consuming wheat, they become exposed to proline- (P) and glutamine (Q)-rich gluten. In bread-making, the [...] Read more.
Wheat storage proteins and products of their hydrolysis may cause coeliac sprue in genetically predisposed individuals with high expression of main histocompatibility complex HLA-DQ2 or DQ8, since by consuming wheat, they become exposed to proline- (P) and glutamine (Q)-rich gluten. In bread-making, the hydrolysis of gliadins and coeliac-toxic peptides occurs with varied efficiency depending on the fermentation pH and temperature. Degradation of gliadins catalysed by Lactobacillus acidophilus 5e2 peptidases and a commercial prolyl endopeptidase synthesised by A. niger, carried out at pH 4.0 and 37 °C, reduces the gliadin concentration over 110-fold and decreases the relative immunoreactivity of the hydrolysate to 0.9% of its initial value. Hydrolysis of coeliac-toxic peptides: LGQQQPFPPQQPY (P1) and PQPQLPYPQPQLP (P2) under the same conditions occurs with the highest efficiency, reaching 99.8 ± 0.0% and 97.5 ± 0.1%, respectively. The relative immunoreactivity of peptides P1 and P2 was 0.8 ± 0.0% and 3.2 ± 0.0%, respectively. A mixture of peptidases from L. acidophilus 5e2 and A. niger may be used in wheat sourdough fermentation to reduce the time needed for degradation of proteins and products of their hydrolysis. Full article
(This article belongs to the Special Issue Biocatalysts and Biocatalysis in Food Industry)
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8 pages, 808 KiB  
Article
Biocatalytic Synthesis of a Novel Bioactive Ginsenoside Using UDP-Glycosyltransferase from Bacillus subtilis 168
by Yumei Hu, Hao Li, Yingying Qu, Xiao Zhang, Juankun Zhang and Longhai Dai
Catalysts 2020, 10(3), 289; https://doi.org/10.3390/catal10030289 - 03 Mar 2020
Cited by 6 | Viewed by 2425
Abstract
Ginsenoside Rg3 is a bioactive compound from Panax ginseng and exhibits diverse notable biological properties. Glycosylation catalyzed by uridine diphosphate-dependent glycosyltransferase (UGT) is the final biosynthetic step of ginsenoside Rg3 and determines its diverse pharmacological activities. In the present study, promiscuous UGT Bs-YjiC [...] Read more.
Ginsenoside Rg3 is a bioactive compound from Panax ginseng and exhibits diverse notable biological properties. Glycosylation catalyzed by uridine diphosphate-dependent glycosyltransferase (UGT) is the final biosynthetic step of ginsenoside Rg3 and determines its diverse pharmacological activities. In the present study, promiscuous UGT Bs-YjiC from Bacillus subtilis 168 was expressed in Escherichia coli and purified via one-step nickel chelate affinity chromatography. The in vitro glycosylation reaction demonstrated Bs-Yjic could selectively glycosylate the C12 hydroxyl group of ginsenoside Rg3 to synthesize an unnatural ginsenoside Rd12. Ginsenoside Rd12 was about 40-fold more water-soluble than that of ginsenoside Rg3 (90 μM). Furthermore, in vitro cytotoxicity of ginsenoside Rd12 against diverse cancer cells was much stronger than that of ginsenoside Rg3. Our studies report the UGT-catalyzed synthesis of unnatural ginsenoside Rd12 for the first time. Ginsenoside Rd12 with antiproliferative activity might be further exploited as a potential anticancer drug. Full article
(This article belongs to the Special Issue Biocatalysts and Biocatalysis in Food Industry)
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Review

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34 pages, 2405 KiB  
Review
β-N-Acetylhexosaminidases for Carbohydrate Synthesis via Trans-Glycosylation
by Jan Muschiol, Marlene Vuillemin, Anne S. Meyer and Birgitte Zeuner
Catalysts 2020, 10(4), 365; https://doi.org/10.3390/catal10040365 - 29 Mar 2020
Cited by 20 | Viewed by 4063
Abstract
β-N-acetylhexosaminidases (EC 3.2.1.52) are retaining hydrolases of glycoside hydrolase family 20 (GH20). These enzymes catalyze hydrolysis of terminal, non-reducing N-acetylhexosamine residues, notably N-acetylglucosamine or N-acetylgalactosamine, in N-acetyl-β-D-hexosaminides. In nature, bacterial β-N-acetylhexosaminidases are mainly involved in [...] Read more.
β-N-acetylhexosaminidases (EC 3.2.1.52) are retaining hydrolases of glycoside hydrolase family 20 (GH20). These enzymes catalyze hydrolysis of terminal, non-reducing N-acetylhexosamine residues, notably N-acetylglucosamine or N-acetylgalactosamine, in N-acetyl-β-D-hexosaminides. In nature, bacterial β-N-acetylhexosaminidases are mainly involved in cell wall peptidoglycan synthesis, analogously, fungal β-N-acetylhexosaminidases act on cell wall chitin. The enzymes work via a distinct substrate-assisted mechanism that utilizes the 2-acetamido group as nucleophile. Curiously, the β-N-acetylhexosaminidases possess an inherent trans-glycosylation ability which is potentially useful for biocatalytic synthesis of functional carbohydrates, including biomimetic synthesis of human milk oligosaccharides and other glycan-functionalized compounds. In this review, we summarize the reaction engineering approaches (donor substrate activation, additives, and reaction conditions) that have proven useful for enhancing trans-glycosylation activity of GH20 β-N-acetylhexosaminidases. We provide comprehensive overviews of reported synthesis reactions with GH20 enzymes, including tables that list the specific enzyme used, donor and acceptor substrates, reaction conditions, and details of the products and yields obtained. We also describe the active site traits and mutations that appear to favor trans-glycosylation activity of GH20 β-N-acetylhexosaminidases. Finally, we discuss novel protein engineering strategies and suggest potential “hotspots” for mutations to promote trans-glycosylation activity in GH20 for efficient synthesis of specific functional carbohydrates and other glyco-engineered products. Full article
(This article belongs to the Special Issue Biocatalysts and Biocatalysis in Food Industry)
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