Enzyme Application in Sustainable Processes and Industrial Biocatalysis

A special issue of Processes (ISSN 2227-9717). This special issue belongs to the section "Catalysis Enhanced Processes".

Deadline for manuscript submissions: closed (30 March 2024) | Viewed by 4733

Special Issue Editors


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Guest Editor
Department of Applied Physical Chemistry, Departmental Section of Food Science, Universidad Autónoma de Madrid, 28049 Madrid, Spain
Interests: green chemistry; advanced extraction; biocatalysis; food science
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Guest Editor
Institute of Food Science Research (CIAL-CSIC), C/Nicolás Cabrera, 9, Campus de Cantoblanco, 28049 Madrid, Spain
Interests: enzyme engineering; enzyme biotransformations; food chemistry; analytical chemistry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzymes are a class of macromolecules with a wide range of applications in industrial processes due to their catalytic activity, as they can selectively modify a unique substrate in a complex matrix under mild experimental conditions. Compared with other catalysts, these biocatalysts have multiple advantages including sustainability, specificity, activity, and catalytic efficiency.

At present, only a small number of the known enzymes present in nature are used in industry. Moreover, they must be optimized for biotechnological use. For this reason, enzyme engineering has emerged as an interesting technology to customize biocatalysts with improved properties to obtain new ingredients and high-quality products under the principles of green chemistry.

Thus, this Special Issue is focused on enzyme application in industrial processes; original research articles and reviews are welcome and encouraged.

Dr. Paz Garcia-Garcia
Dr. Gloria Fernandez-Lorente
Guest Editors

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Keywords

  • biocatalysis
  • bioprocessing
  • immobilized enzymes
  • enzyme engineering
  • enzymatic modification
  • sustainable processes
  • green chemistry
  • industrial processes

Published Papers (3 papers)

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Research

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15 pages, 2887 KiB  
Article
Immobilization of Pseudomonas fluorescens Lipase on Hollow Poly(o-phenylenediamine) Microspheres and Its Application in the Preparation of Citronellyl Acetate
by Jian Xiong, Qi Wang, Hanghang Xu and Wenyuan Sun
Processes 2023, 11(6), 1842; https://doi.org/10.3390/pr11061842 - 19 Jun 2023
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Abstract
In order to address the challenges associated with free lipase in organic solvents, including aggregation, poor stability, and low catalytic efficiency, this study developed two types of poly(o-phenylenediamine) microspheres (solid and hollow) as supports for immobilizing lipase. The immobilization process utilized an adsorption [...] Read more.
In order to address the challenges associated with free lipase in organic solvents, including aggregation, poor stability, and low catalytic efficiency, this study developed two types of poly(o-phenylenediamine) microspheres (solid and hollow) as supports for immobilizing lipase. The immobilization process utilized an adsorption method, with the poly(o-phenylenediamine) hollow microspheres being identified as the optimal support in a 2:5 enzyme-to-support ratio. On this basis, the lipase was immobilized by the covalent binding method. The immobilization conditions consisted of treating the support with 2% glutaraldehyde and immobilization at 40 °C for 2 h in pH 7.0 buffer. The specific activity of the immobilized enzyme was 5.3 times higher than that of the free enzyme. Covalent-binding immobilized lipase was also used for the preparation of citronellyl acetate by transesterification reaction, and, in optimized reaction conditions where the amount of immobilized enzyme was 0.1 g/mL, the reaction temperature was 50 °C and the shaking speed was 200 r/min during the reaction. Under these conditions, the citronellyl acetate yields can exceed 99% after 2 h. Furthermore, the stability of the immobilized lipase was investigated, and the residual activity of the immobilized enzyme was 95% after seven repetitions, while that of the free enzyme was only 70%. After 56 days of storage at room temperature, the immobilized enzyme retained 60% of its original viability, while the free enzyme retained only 31%. Full article
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13 pages, 3078 KiB  
Article
Preparation of Alginate Oligosaccharides from Laminaria japonica Biomass by a Novel Biofunctional Alginate Lyase with pH and Salt Tolerance
by Lei Song, Yan-Feng Guo, Yi-Lei Wang, Chuan-Bao Wang, Jing-Hua Liu, Guo-Qing Meng and Zhi-Peng Wang
Processes 2023, 11(5), 1495; https://doi.org/10.3390/pr11051495 - 15 May 2023
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Abstract
Enzymatic alginate oligosaccharides were proved with various biological activities. Developing robust alginate lyase with high production is essential for its industrial application. In this study, a novel alginate lyase gene, AL07, was successfully screened and expressed in Pichia pastoris, and its characteristics were [...] Read more.
Enzymatic alginate oligosaccharides were proved with various biological activities. Developing robust alginate lyase with high production is essential for its industrial application. In this study, a novel alginate lyase gene, AL07, was successfully screened and expressed in Pichia pastoris, and its characteristics were characterized. The secreted alginate lyase has a molecular weight of approximately 40.0 kDa and an activity of 45.4 U/mL. AL07 exhibits superior biological activity at pH 7.0 and 40 °C, with a preference for polyG substrates. Notably, the enzyme exhibits more than 60% relative activity over a pH range of 5.0 to 10.0. AL07 is also independent of ions and exhibits salt tolerance properties. The main degradation product of AL07 is DP2 oligosaccharide. Using AL07-based enzyme cocktail, Laminaria japonica can be degraded within 120 min. Therefore, AL07 has been demonstrated to be an efficient tool for the preparation of alginate oligosaccharides and the degradation of L. japonica. Full article
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Review

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12 pages, 938 KiB  
Review
Use of Potential Immobilized Enzymes for the Modification of Liquid Foods in the Food Industry
by Ernestina Garcia-Quinto, Raquel Aranda-Cañada, Paz García-García and Gloria Fernández-Lorente
Processes 2023, 11(6), 1840; https://doi.org/10.3390/pr11061840 - 19 Jun 2023
Cited by 4 | Viewed by 2428
Abstract
Enzymes are complex proteins that carry out biochemical reactions. Apart from being necessary for life, they are used in numerous industrial processes, especially in the textile, pharmaceutical, food and chemical sectors. One of the longest-lived industries regarding the use of enzymes is the [...] Read more.
Enzymes are complex proteins that carry out biochemical reactions. Apart from being necessary for life, they are used in numerous industrial processes, especially in the textile, pharmaceutical, food and chemical sectors. One of the longest-lived industries regarding the use of enzymes is the food industry. Enzymes have always been used, mainly in their free form, to obtain new products and to improve the organoleptic qualities in different industries, such as in dairy, fruit and vegetables, and beverages. However, today, immobilized enzymes are the focus of attention in the liquid food industry, as they offer numerous advantages, such as stabilization and reuse, which enable cost reduction. Full article
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