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Catalysts
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Biocatalysis for Tasty Food
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Biocatalysis for Tasty Food

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

Deadline for manuscript submissions: closed (20 March 2022) | Viewed by 6783

Special Issue Editors

Dr. Cinzia Calvio

E-Mail Website
Guest Editor
Department of Biology and Biotechnology, University of Pavia, Pavia, Italy
Interests: microbial genetics and biotechnology; Bacillus subtilis; sustainable fermentations
Dr. Carlo F Morelli

E-Mail Website
Guest Editor
Department of Chemistry, University of Milan, Milan, Italy
Interests: bioorganic chemistry; biocatalysis; natural products chemistry; organic synthesis

Special Issue Information

Dear Colleagues,

The production of new flavor enhancers and aroma compounds is a topic of paramount interest in the food industry, as they ensure product homogeneity, favorable consumer acceptance, and can support programs aimed at reducing salt and fat intake. The exposure of consumers to new flavors, as a consequence of the growth of the ethnic food sector with consequent changes in consumers’ lifestyle, and concerns about some of the flavor enhancers currently in use, boosts the search for highly acceptable, possibly naturally occurring, alternatives. Biocatalytic methods may offer a viable, sustainable, and convenient entry to these products, particularly with compounds of biotechnological origin, or the use of waste by-products from other processes’ streams as raw material.

We are pleased to invite you to submit original research papers, short communications, letters, or review articles focused on the biocatalyzed synthesis of taste-active compounds, aroma compounds, flavor enhancers, or food additives aimed at improving food acceptance and/or organoleptic properties.

Dr. Cinzia Calvio
Dr. Carlo F Morelli
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. 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 2200 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

  • Taste-active compounds
  • Flavor enhancers
  • Aroma compounds
  • Umami
  • Kokumi
  • Food industry
  • Enzyme
  • Biocatalysis
  • Biocatalyzed synthesis
  • Enzyme modification
  • Immobilized enzymes

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Published Papers (2 papers)

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Research

14 pages, 4160 KiB  
Article
Biochemical Characterisation and Structure Determination of a Novel Cold-Active Proline Iminopeptidase from the Psychrophilic Yeast, Glaciozyma antarctica PI12
by Shazilah Kamaruddin, Rohaiza Ahmad Redzuan, Nurulermila Minor, Wan Mohd Khairulikhsan Wan Seman, Mahzan Md Tab, Nardiah Rizwana Jaafar, Nazahiyah Ahmad Rodzli, Mohd Anuar Jonet, Izwan Bharudin, Nur Athirah Yusof, Doris Quay Huai Xia, Nor Muhammad Mahadi, Abdul Munir Abdul Murad and Farah Diba Abu Bakar
Catalysts 2022, 12(7), 722; https://doi.org/10.3390/catal12070722 - 30 Jun 2022
Cited by 5 | Viewed by 2898
Abstract
Microbial proteases constitute one of the most important groups of industrially relevant enzymes. Proline iminopeptidases (PIPs) that specifically release amino-terminal proline from peptides are of major interest for applications in food biotechnology. Proline iminopeptidase has been extensively characterised in bacteria and filamentous fungi. [...] Read more.
Microbial proteases constitute one of the most important groups of industrially relevant enzymes. Proline iminopeptidases (PIPs) that specifically release amino-terminal proline from peptides are of major interest for applications in food biotechnology. Proline iminopeptidase has been extensively characterised in bacteria and filamentous fungi. However, no similar reports exist for yeasts. In this study, a protease gene from Glaciozyma antarctica designated as GaPIP was cloned and overexpressed in Escherichia coli. Sequence analyses of the gene revealed a 960 bp open reading frame encoding a 319 amino acid protein (35,406 Da). The purified recombinant GaPIP showed a specific activity of 3561 Umg−1 towards L-proline-p-nitroanilide, confirming its identity as a proline iminopeptidase. GaPIP is a cold-active enzyme with an optimum activity of 30 °C at pH 7.0. The enzyme is stable between pH 7.0 and 8.0 and able to retain its activity at 10–30 °C. Although GaPIP is a serine protease, only 25% inhibition by the serine protease inhibitor, phenylmethanesulfonylfluoride (PMSF) was recorded. This enzyme is strongly inhibited by the presence of EDTA, suggesting that it is a metalloenzyme. The dimeric structure of GaPIP was determined at a resolution of 2.4 Å. To date, GaPIP is the first characterised PIP from yeasts and the structure of GaPIP is the first structure for PIP from eukaryotes. Full article
(This article belongs to the Special Issue Biocatalysis for Tasty Food)
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12 pages, 1469 KiB  
Article
Optimization of Hydroperoxide Lyase Production for Recombinant Lipoxygenase Pathway Cascade Application
by Veronika Kazimírová, Viktória Zezulová, Vladimír Krasňan, Vladimír Štefuca and Martin Rebroš
Catalysts 2021, 11(10), 1201; https://doi.org/10.3390/catal11101201 - 1 Oct 2021
Cited by 5 | Viewed by 3134
Abstract
Cis-3-hexenal and its more stable isomer, trans-2-hexenal, are highly valued chemicals used in the food and perfume industries. They are produced by the plant lipoxygenase pathway, where two enzymes, lipoxygenase (LOX) and hydroperoxide lyase (HPL), are involved. However, the application of [...] Read more.
Cis-3-hexenal and its more stable isomer, trans-2-hexenal, are highly valued chemicals used in the food and perfume industries. They are produced by the plant lipoxygenase pathway, where two enzymes, lipoxygenase (LOX) and hydroperoxide lyase (HPL), are involved. However, the application of this pathway is limited, especially due to the instability of HPL. This enzyme belongs to the cytochrome P450 enzyme family and needs heme as a prosthetic group. Its synthesis must be effectively performed by a host organism in order to produce an active protein. In this work, Pseudomonas aeruginosa LOX was expressed in Escherichia coli BL21(DE3), and whole cells were used for the synthesis of 13(S)-hydroperoxy-(Z,E,Z)-9,11,15-octadecatrienoic acid (13-HPOT) as a substrate for HPL. Expression of Psidium guajava HPL was carried out by recombinant E. coli JM109(DE3) in autoinduction media, and the influence of the addition of heme precursors δ-ALA and FeII+ was studied. Specific activity of whole cells expressing HPL was measured by the direct use of a synthesized 13-HPOT solution (2.94 mM of total hydroperoxides, 75.35% of 13-HPOT (2.22 mM)) and increased 2.6-fold (from 61.78 U·mg−1 to 159.95 U·mg−1) with the addition of 1 mM FeII+ to the autoinduction media. Productivity and activity were further enhanced by an increase in the expression temperature, and a total of 3.30·105 U·dm−3 of culture media was produced in the optimized process. Full article
(This article belongs to the Special Issue Biocatalysis for Tasty Food)
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