Special Issue "Multienzymatic Catalysis and/or Enzyme Co-immobilization"
Deadline for manuscript submissions: 30 June 2021.
Interests: biocatalysis; enzyme immobilization; enzyme stabilization; enzyme chemical modification; bioprocess optimization
Special Issues and Collections in MDPI journals
Special Issue in Molecules: Enzyme Immobilization 2016
Special Issue in Molecules: Enzyme Immobilization and Its Applications
Special Issue in Molecules: Enzyme Immobilization Ⅳ
The importance of biocatalysis is continuously growing, and many multienzymatic processes are being developed. These include cascade reactions, where the product of one enzyme is the substrate of the next enzyme, but also many other biocatalysts (e.g., use of lytic enzymes to prevent contaminations in bioprocesses). This Special Issue intends to address this diversity of multienzymatic reactions: processes where cofactor recycling is required, synergy hydrolysis of proteins and polysaccharides, a process where hydrogen peroxide is substrate or product, etc.
On the other hand, enzyme coimmobilization may produce some kinetic advantages. There is an enormous effort to develop coimmobilization technologies that can permit the specific location of each enzyme, and also to solve some of the inherent problems of coimmobilization. This way, this Special Issue also welcomes papers addressing the preparation of multienzymatic coimmobilized biocatalysts.
Prof. Dr. Roberto Fernandez-Lafuente
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 papers will be 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 2000 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.
- multienzymatic processes
- cellulose hydrolysis
- juice clarification
- cofactor recycling systems
- hydrogen peroxide in biocatalysis
- enzyme coimmobilization
- enzyme location
- enzyme stability
- enzyme reuse
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title: Multi-combilipases: co-immobilizing lipases with very different stabilities combining immobilization via interfacial activation and ion exchange: The reuse of the most stable co-immobilized enzymes after inactivation of the least stable enzymes
Authors: Sara Arana-Peña, Diego Carballares , Vicente Cortes-Corberan and Roberto Fernandez-Lafuente *
Title: GH5 and GH26 endo-mannanases perform the same during lignocellulosic biomass degradation - even though GH26 endo-mannanase is more catalytically active on mannans
Authors: Samkelo Malgas
Affiliation: Enzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa
Abstract: Among endo-mannanases, glycoside hydrolase (GH) family 26 enzymes have been shown to be more catalytically active on mannans than GH5 enzymes. However, only GH5 endo-mannanases have been used for the formulation of enzyme cocktails. In this study, Bacillus sp. derived GH5 and GH26 endo-mannanases were comparatively analysed biochemically for their synergistic action with CTec2 during pre-treated lignocellulose degradation. Substrate specificity and thermo-stability studies on mannans showed that GH26 endo-mannanase was more catalytically active and stable than GH5. GH26 also exhibited higher binding affinity on mannan than GH5, while GH5 showed more affinity on lignocellulosic substrates than GH26. Applying the endo-mannanases in combination with CTec2 for lignocellulose degradation led to synergism with a 1.3-fold increase in reducing sugar release compared to when CTec2 was used alone. This study showed that using the activity of endo-mannanases recorded on model substrates is a poor predictor of their activity and synergism on complex lignocelluloses.