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Special Issue "Immobilization of Microorganisms and Enzymes"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (27 August 2018).

Special Issue Editors

Prof. Dr. Jose M. Guisan
E-Mail Website1 Website2
Guest Editor
Department of Biocatalysis, Institute of Catalysis, Spanish Research Council, ICP-CSIC, Campus UAM, 28049 Madrid, Spain
Tel. +34 91 585 48 09
Interests: enzyme engineering: purification, immobilization, stabilization, reactivation; hyperactivation; main enzymes: lipases, penicillin G acylase, endoxylanases, beta-xylosidases, etc.; enzyme processes: fine chemistry, food chemistry, analytical chemistry, green energy; enzyme reactors: stirred tanks, packed beds, etc.
Special Issues and Collections in MDPI journals
Dr. Javier Rocha-Martin
E-Mail Website1 Website2 Website3
Guest Editor
Institute of Catalysis and Petrochemistry, Spanish Council for Scientific Research (CSIC), Marie Curie 2, 28049 Madrid, Spain
Interests: protein immobilization; protein engineering; enzyme stabilization; multienzyme systems; cascade reactions
Special Issues and Collections in MDPI journals

Special Issue Information

Dear Colleagues,

Enzymes are able to catalyze the most complex chemical processes under the most benign experimental and environmental conditions. However, enzymes, because of their biological origin, have some characteristics that are not very useful for industrial implementation: For example, they are soluble and unstable. The proposed Special Issue will bring together a number of interesting topics to improve the functional properties of industrial enzymes and microorganisms via immobilization and post-immobilization techniques.

It is anticipated that the following topics will be included in the Special Issue:

  • improvement of enzyme properties by immobilization techniques
  • new immobilization techniques
  • immobilized enzymes in non-conventional media
  • improvement of enzyme properties by post-immobilization techniques
  • improvement of microorganisms properties via immobilization

Prof. Dr. Jose M. Guisan
Dr. Javier Rocha-Martin
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 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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • immobilization of industrial enzymes
  • new immobilization techniques
  • new rigid supports for immobilization
  • enzyme stabilization
  • stability of immobilized microorganisms

Published Papers (7 papers)

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Research

Open AccessArticle
Use of Yarrowia lipolytica Lipase Immobilized in Cell Debris for the Production of Lipolyzed Milk Fat (LMF)
Int. J. Mol. Sci. 2018, 19(11), 3413; https://doi.org/10.3390/ijms19113413 - 31 Oct 2018
Cited by 1
Abstract
Lipase immobilized on Yarrowia lipolytica cell debris after sonication of yeast cells (LipImDebri) was used in hydrolysis reaction as a novel strategy to produce lipolyzed milk fat (LMF). Extracellular (4732.1 U/L), intracellular (130.0 U/g), and cell debris (181.0 U/g) lipases were obtained in [...] Read more.
Lipase immobilized on Yarrowia lipolytica cell debris after sonication of yeast cells (LipImDebri) was used in hydrolysis reaction as a novel strategy to produce lipolyzed milk fat (LMF). Extracellular (4732.1 U/L), intracellular (130.0 U/g), and cell debris (181.0 U/g) lipases were obtained in a 4 L bioreactor using residual frying oil as inducer in 24 h fermentation process. LipImDebri showed a good operational stability retaining 70% of lipolytic activity after the second cycle and 40% after the fourth. The highest degree of hydrolysis (28%) was obtained with 500 mg LipImDebri for 6 h of lipolysis of anhydrous milk fat. LMF produced with LipImDebri presented high contents of oleic (35.2%), palmitic (25.0%), and stearic (15.4%) acids and considerable amounts of odor-active short and medium chain fatty acids (C:4–C:10) (8.13%). Full article
(This article belongs to the Special Issue Immobilization of Microorganisms and Enzymes)
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Open AccessArticle
High Catalytic Activity of Lipase from Yarrowia lipolytica Immobilized by Microencapsulation
Int. J. Mol. Sci. 2018, 19(11), 3393; https://doi.org/10.3390/ijms19113393 - 30 Oct 2018
Cited by 2
Abstract
Microencapsulation of lipase from Yarrowia lipolytica IMUFRJ 50682 was performed by ionotropic gelation with sodium alginate. Sodium alginate, calcium chloride and chitosan concentrations as well as complexation time were evaluated through experimental designs to increase immobilization yield (IY) and immobilized lipase activity (ImLipA) [...] Read more.
Microencapsulation of lipase from Yarrowia lipolytica IMUFRJ 50682 was performed by ionotropic gelation with sodium alginate. Sodium alginate, calcium chloride and chitosan concentrations as well as complexation time were evaluated through experimental designs to increase immobilization yield (IY) and immobilized lipase activity (ImLipA) using p-nitrophenyl laurate as substrate. To adjust both parameters (IY and ImLipA), the desirability function showed that microcapsule formation with 3.1%(w/v) sodium alginate, 0.19%(w/v) chitosan, 0.14 M calcium chloride, and 1 min complexation time are ideal for maximal immobilization yield and immobilized lipase activity. A nearly twofold enhancement in Immobilization yield and an increase up to 280 U/g of the lipase activity of the microcapsules were achieved using the experimental design optimization tool. Chitosan was vital for the high activity of this new biocatalyst, which could be reused a second time with about 50% of initial activity and for four more times with about 20% of activity. Full article
(This article belongs to the Special Issue Immobilization of Microorganisms and Enzymes)
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Open AccessArticle
Recombinant Escherichia coli BL21-pET28a-egfp Cultivated with Nanomaterials in a Modified Microchannel for Biofilm Formation
Int. J. Mol. Sci. 2018, 19(9), 2590; https://doi.org/10.3390/ijms19092590 - 31 Aug 2018
Abstract
The application of whole cells as catalytic biofilms in microchannels has attracted increasing scientific interest. However, the excessive biomass formation and structure of biofilms in a reactor limits their use. A microchannel reactor with surface modification was used to colonize recombinant Escherichia coil [...] Read more.
The application of whole cells as catalytic biofilms in microchannels has attracted increasing scientific interest. However, the excessive biomass formation and structure of biofilms in a reactor limits their use. A microchannel reactor with surface modification was used to colonize recombinant Escherichia coil BL21-pET28a-egfp rapidly and accelerated growth of biofilms in the microchannel. The segmented flow system of ‘air/culture medium containing nanomaterials’ was firstly used to modulate the biofilms formation of recombinant E. coil; the inhibitory effects of nanomaterials on biofilm formation were investigated. The results indicated that the segmental flow mode has a significant impact on the structure and development of biofilms. Using the channels modified by silane reagent, the culture time of biofilms (30 h) was reduced by 6 h compared to unmodified channels. With the addition of graphene sheets (10 mg/L) in Luria-Bertani (LB) medium, the graphene sheets possessed a minimum inhibition rate of 3.23% against recombinant E. coil. The biofilms cultivated by the LB medium with added graphene sheets were stably formed in 20 h; the formation time was 33.33% shorter than that by LB medium without graphene. The developed method provides an efficient and simple approach for rapid preparation of catalytic biofilms in microchannel reactors. Full article
(This article belongs to the Special Issue Immobilization of Microorganisms and Enzymes)
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Open AccessArticle
Lipase Immobilization on Silica Xerogel Treated with Protic Ionic Liquid and its Application in Biodiesel Production from Different Oils
Int. J. Mol. Sci. 2018, 19(7), 1829; https://doi.org/10.3390/ijms19071829 - 21 Jun 2018
Cited by 5
Abstract
Treated silica xerogel with protic ionic liquid (PIL) and bifunctional agents (glutaraldehyde and epichlorohydrin) is a novel support strategy used in the effective immobilization of lipase from Burkholderia cepacia (LBC) by covalent binding. As biocatalysts with the highest activity recovery yields, LBC immobilized [...] Read more.
Treated silica xerogel with protic ionic liquid (PIL) and bifunctional agents (glutaraldehyde and epichlorohydrin) is a novel support strategy used in the effective immobilization of lipase from Burkholderia cepacia (LBC) by covalent binding. As biocatalysts with the highest activity recovery yields, LBC immobilized by covalent binding with epichlorohydrin without (203%) and with PIL (250%), was assessed by the following the hydrolysis reaction of olive oil and characterized biochemically (Michaelis–Menten constant, optimum pH and temperature, and operational stability). Further, the potential transesterification activity for three substrates: sunflower, soybean, and colza oils, was also determined, achieving a conversion of ethyl esters between 70 and 98%. The supports and the immobilized lipase systems were characterized using Fourier transform infrared spectra (FTIR), scanning electron microscopy (SEM), elemental analysis, and thermogravimetric (TG) analysis. Full article
(This article belongs to the Special Issue Immobilization of Microorganisms and Enzymes)
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Open AccessArticle
Hierarchical ZIF-8 toward Immobilizing Burkholderia cepacia Lipase for Application in Biodiesel Preparation
Int. J. Mol. Sci. 2018, 19(5), 1424; https://doi.org/10.3390/ijms19051424 - 10 May 2018
Cited by 5
Abstract
A hierarchical mesoporous zeolitic imidazolate framework (ZIF-8) was processed based on cetyltrimethylammonium bromide (CTAB) as a morphological regulating agent and amino acid (l-histidine) as assisting template agent. Burkholderia cepacia lipase (BCL) was successfully immobilized by ZIF-8 as the carrier via an [...] Read more.
A hierarchical mesoporous zeolitic imidazolate framework (ZIF-8) was processed based on cetyltrimethylammonium bromide (CTAB) as a morphological regulating agent and amino acid (l-histidine) as assisting template agent. Burkholderia cepacia lipase (BCL) was successfully immobilized by ZIF-8 as the carrier via an adsorption method (BCL-ZIF-8). The immobilized lipase (BCL) showed utmost activity recovery up to 1279%, a 12-fold boost in its free counterpart. BCL-ZIF-8 was used as a biocatalyst in the transesterification reaction for the production of biodiesel with 93.4% yield. There was no significant lowering of conversion yield relative to original activity for BCL-ZIF-8 when continuously reused for eight cycles. This work provides a new outlook for biotechnological importance by immobilizing lipase on the hybrid catalyst (ZIF-8) and opens the door for its uses in the industrial field. Full article
(This article belongs to the Special Issue Immobilization of Microorganisms and Enzymes)
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Open AccessArticle
Stabilization of Immobilized Lipases by Intense Intramolecular Cross-Linking of Their Surfaces by Using Aldehyde-Dextran Polymers
Int. J. Mol. Sci. 2018, 19(2), 553; https://doi.org/10.3390/ijms19020553 - 12 Feb 2018
Cited by 7
Abstract
Immobilized enzymes have a very large region that is not in contact with the support surface and this region could be the target of new stabilization strategies. The chemical amination of these regions plus further cross-linking with aldehyde-dextran polymers is proposed here as [...] Read more.
Immobilized enzymes have a very large region that is not in contact with the support surface and this region could be the target of new stabilization strategies. The chemical amination of these regions plus further cross-linking with aldehyde-dextran polymers is proposed here as a strategy to increase the stability of immobilized enzymes. Aldehyde-dextran is not able to react with single amino groups but it reacts very rapidly with polyaminated surfaces. Three lipases—from Thermomyces lanuginosus (TLL), Rhizomucor miehiei (RML), and Candida antarctica B (CALB)—were immobilized using interfacial adsorption on the hydrophobic octyl-Sepharose support, chemically aminated, and cross-linked. Catalytic activities remained higher than 70% with regard to unmodified conjugates. The increase in the amination degree of the lipases together with the increase in the density of aldehyde groups in the dextran-aldehyde polymer promoted a higher number of cross-links. The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of those conjugates demonstrates the major role of the intramolecular cross-linking on the stabilization of the enzymes. The highest stabilization was achieved by the modified RML immobilized on octyl-Sepharose, which was 250-fold more stable than the unmodified conjugate. The TLL and the CALB were 40-fold and 4-fold more stable than the unmodified conjugate. Full article
(This article belongs to the Special Issue Immobilization of Microorganisms and Enzymes)
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Open AccessArticle
New Strategy for the Immobilization of Lipases on Glyoxyl–Agarose Supports: Production of Robust Biocatalysts for Natural Oil Transformation
Int. J. Mol. Sci. 2017, 18(10), 2130; https://doi.org/10.3390/ijms18102130 - 12 Oct 2017
Cited by 7
Abstract
Immobilization on Glyoxyl–agarose support (Gx) is one of the best strategies to stabilize enzymes. However, the strategy is difficult to apply at neutral pH when most enzymes are stable and, even when possible, produces labile derivatives. This work contributes to overcoming this hurdle [...] Read more.
Immobilization on Glyoxyl–agarose support (Gx) is one of the best strategies to stabilize enzymes. However, the strategy is difficult to apply at neutral pH when most enzymes are stable and, even when possible, produces labile derivatives. This work contributes to overcoming this hurdle through a strategy that combines solid-phase amination, presence of key additives, and derivative basification. To this end, aminated industrial lipases from Candida artarctica (CAL), Thermomyces lunuginosus (TLL), and the recombinant Geobacillus thermocatenulatus (BTL2) were immobilized on Gx for the first time at neutral pH using anthranilic acid (AA) or DTT as additives (immobilization yields >70%; recovered activities 37.5–76.7%). The spectroscopic evidence suggests nucleophilic catalysis and/or adsorption as the initial lipase immobilization events. Subsequent basification drastically increases the stability of BTL2–glyoxyl derivatives under harsh conditions (t1/2, from 2.1–54.5 h at 70 °C; from 10.2 h–140 h in 80% dioxane). The novel BTL2-derivatives were active and selective in fish oil hydrolysis (1.0–1.8 μmol of polyunsaturated fatty acids (PUFAs) min-1·g-1) whereas the selected TLL-derivative was as active and stable in biodiesel production (fatty ethyl esters, EE) as the commercial Novozyme®-435 after ten reaction cycles (~70% EE). Therefore, the potential of the proposed strategy in producing suitable biocatalysts for industrial processes was demonstrated. Full article
(This article belongs to the Special Issue Immobilization of Microorganisms and Enzymes)
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