BioTech

Special Issue Editors

Dr. Ana Paula Tavares

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Guest Editor

CICECO – Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal
Interests: enzymatic biocatalysis; proteins; enzymes; biopharmaceuticals; ionic liquids; biomolecules purification; aqueous biphasic systems; fermentation processes; enzyme immobilization; nanomaterials
Special Issues, Collections and Topics in MDPI journals

Dr. Mafalda R. Almeida

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Guest Editor

CICECO – Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal
Interests: microbial enzymes production; biopharmaceuticals (enzymes and antibodies) purification using liquid–liquid or solid–liquid approaches; centrifugal parti-tion chromatography

Special Issue Information

Dear Colleagues,

Microbial enzymes are recognized worldwide for their widespread applications in medicine, food, agriculture, and chemical fields, among others. Additionally, industrial processes mediated by enzymes are of high interest due to their nontoxic and eco-friendly properties, reduced process time and cost-effectiveness. At present, advances in genetic and protein engineering have improved the production of microbial enzymes to meet the increased demand, designing and producing enzymes with desired properties and functionalities. In addition, novel purification techniques with improved resolution, simplicity and speed, which are easy to scale-up and able to operate in continuous mode, have been developed to purify microbial enzymes from the complex media.

This Special Issue aims to cover promising, recent, and novel research trends in the production, purification and applications of microbial enzymes.

Dr. Ana Paula Tavares
Dr. Mafalda R. Almeida
Guest Editors

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Keywords

microbial enzymes
genetic and protein engineering
enzymes production
enzymes purification
industrial applicattions

Published Papers (2 papers)

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Research

12 pages, 2309 KiB

Open AccessArticle

Xylanase Production by Talaromyces amestolkiae Valuing Agroindustrial Byproducts

by Giórgia S. Barbieri, Heitor B. S. Bento, Fernanda de Oliveira, Flávio P. Picheli, Lídia M. Dias, Fernando Masarin and Valéria C. Santos-Ebinuma

BioTech 2022, 11(2), 15; https://0-doi-org.brum.beds.ac.uk/10.3390/biotech11020015 - 17 May 2022

Cited by 8 | Viewed by 3074

Abstract

In general, agroindustrial byproducts can be easily assimilated by several microorganisms due to their composition, which is rich in carbohydrates. Therefore, they could be appropriate for use as raw materials in a sustainable refinery concept, including the production of hydrolytic enzymes with industrial applicability. In this work, xylanase production by the filamentous fungi Talaromyces amestolkiae in submerged culture was evaluated using five agroindustrial byproducts, namely, wheat bran, citrus pulp, rice bran, peanut skin, and peanut shell. Firstly, the aforementioned byproducts were characterized in terms of cellulose, xylan, lignin, and extractives. Next, production studies were performed, and wheat bran generated the highest enzymatic activity (5.4 U·mL⁻¹), probably because of its large amount of xylan. Subsequently, a factorial design was performed to evaluate the independent variables yeast extract, wheat bran, K₂HPO₄, and pH, aiming to improve the variable response, xylanase activity. The condition that promoted the highest production, 13.02 U·mL⁻¹ (141% higher than the initial condition), was 20 g·L⁻¹ wheat bran, 2.5 g·L⁻¹ yeast extract, 3 g·L⁻¹ K₂HPO₄, and pH 7. Thus, industrial byproducts with a high content of xylan can be used as a culture medium to produce xylanase enzymes with a Talaromyces strain through an economical and sustainable approach. Full article

(This article belongs to the Special Issue Progress on the Production, Purification and Applications of Microbial Enzymes)

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20 pages, 3166 KiB

Open AccessArticle

Immobilization and Characterization of L-Asparaginase over Carbon Xerogels

by Rita A. M. Barros, Raquel O. Cristóvão, Sónia A. C. Carabineiro, Márcia C. Neves, Mara G. Freire, Joaquim L. Faria, Valéria C. Santos-Ebinuma, Ana P. M. Tavares and Cláudia G. Silva

BioTech 2022, 11(2), 10; https://doi.org/10.3390/biotech11020010 - 14 Apr 2022

Cited by 8 | Viewed by 3281

Abstract

L-asparaginase (ASNase) is an aminohydrolase currently used in the pharmaceutical and food industries. Enzyme immobilization is an exciting option for both applications, allowing for a more straightforward recovery and increased stability. High surface area and customizable porosity make carbon xerogels (CXs) promising materials for ASNase immobilization. This work describes the influence of contact time, pH, and ASNase concentration on the immobilization yield (IY) and relative recovered activity (RRA) using the Central Composite Design methodology. The most promising results were obtained using CX with an average pore size of 4 nm (CX-4), reaching IY and RRA of 100%. At the optimal conditions (contact time 49 min, pH 6.73, and [ASNase] 0.26 mg·mL⁻¹), the ASNase-CXs biocomposite was characterized and evaluated in terms of kinetic properties and operational, thermal, and pH stabilities. The immobilized ASNase onto CX-4 retained 71% of its original activity after six continuous reaction cycles, showed good thermal stability at 37 °C (RRA of 91% after 90 min), and was able to adapt to both acidic and alkaline environments. Finally, the results indicated a 3.9-fold increase in the immobilized ASNase affinity for the substrate, confirming the potential of CXs as a support for ASNase and as a cost-effective tool for subsequent use in the therapeutic and food sectors. Full article

(This article belongs to the Special Issue Progress on the Production, Purification and Applications of Microbial Enzymes)

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