Transglutaminase-Mediated Protein Immobilization to Casein Nanolayers Created on a Plastic Surface

Kamiya, Noriho; Doi, Satoshi; Tominaga, Jo; Ichinose, Hirofumi; Goto, Masahiro

doi:10.1021/bm0494895

Cited by 39 publications

(36 citation statements)

References 18 publications

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“…Recently, enzymes are being more fully enlisted for the fabrication and modification of materials [161][162][163][164][165][166][167][168][169][170][171][172][173][174][175][176][177]. Oxidative enzymes especially, tyrosinases, laccases, and peroxidases have been used to generate derivatives of chitosan [178][179][180] and have been extended to generating protein-chitosan conjugates [181].…”

Section: Biofunctionalizing Electrodeposited Chitosan Filmsmentioning

confidence: 99%

Chitosan to Connect Biology to Electronics: Fabricating the Bio-Device Interface and Communicating Across This Interface

et al. 2014

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Individually, advances in microelectronics and biology transformed the way we live our lives. However, there remain few examples in which biology and electronics have been interfaced to create synergistic capabilities. We believe there are two major challenges to the integration of biological components into microelectronic systems: (i) assembly of the biological components at an electrode address, and (ii) communication between the assembled biological components and the underlying electrode. Chitosan OPEN ACCESSPolymers 2015, 7 2 possesses a unique combination of properties to meet these challenges and serve as an effective bio-device interface material. For assembly, chitosan's pH-responsive film-forming properties allow it to "recognize" electrode-imposed signals and respond by self-assembling as a stable hydrogel film through a cathodic electrodeposition mechanism. A separate anodic electrodeposition mechanism was recently reported and this also allows chitosan hydrogel films to be assembled at an electrode address. Protein-based biofunctionality can be conferred to electrodeposited films through a variety of physical, chemical and biological methods. For communication, we are investigating redox-active catechol-modified chitosan films as an interface to bridge redox-based communication between biology and an electrode. Despite significant progress over the last decade, many questions still remain which warrants even deeper study of chitosan's structure, properties, and functions.

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Section: Biofunctionalizing Electrodeposited Chitosan Filmsmentioning

confidence: 99%

Chitosan to Connect Biology to Electronics: Fabricating the Bio-Device Interface and Communicating Across This Interface

et al. 2014

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“…[24,25] Recently, biological approaches based on enzymatic methodologies have attracted much attention; these techniques enable site-specific modification of the target (reporter) protein due to substrate specificity of the modifying enzyme. [26][27][28] Hereby, we focused on sortase A (SrtA), a transpeptidase derived from Staphylococcus aureus. [29] SrtA recognizes the Leu-Pro-Xaa-Thr-Gly amino acid sequence (LP tag) in a protein, cleaves between Thr and Gly, and subsequently tethers the Thr carboxyl group to an amino group of N-terminal Gly oligomers through a native peptide bond.…”

Section: Introductionmentioning

confidence: 99%

C‐Terminal‐oriented Immobilization of Enzymes Using Sortase A‐mediated Technique

Hata

Matsumoto

Tanaka

et al. 2015

Macromolecular Bioscience

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In the present study, sortase A-mediated immobilization of enzymes was used for the preparation of immobilized enzymes. Thermobifida fusca YX β-glucosidase (BGL) or Streptococcus bovis 148 α-amylase (AmyA) were produced with C-terminal sortase A recognition sequences. The resulting fusion proteins were successfully immobilized on nanoparticle surfaces using sortase A. Some properties (activity, stability, and reusability) of the immobilized fusion proteins were evaluated. Both immobilized BGL and immobilized AmyA prepared by the sortase A-mediated technique retained their catalytic activity, exhibiting activities 3.0- or 1.5-fold (respectively) of those seen with the same enzymes immobilized by chemical crosslinking. Immobilized enzymes prepared by the sortase A-mediated technique did not undergo dramatic changes in stability compared with the respective free enzymes. Thus, the sortase A-mediated technique provides a promising method for immobilization of active, stable enzymes.

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“…Most microbial TGase (MTGase)-catalyzed reactions can be used to modify the functional properties of food proteins [11], such as texture, viscosity, foaming and emulsifying properties, and lead to improvements in their nutritional value [12,13]. In addition, MTGases have extensive uses in biomedical research, human diagnostics and therapeutics, such as biomaterial cross-linking [14], protein immobilization [15], fabricating microfluidic devices for cell culture [16], MTGase-mediated gelatin matrices for tissue engineering [17], cross-linking enhancement in cell attachment [18], enzymatic biotinylation of antibodies [19], and formation of novel erythropoietin (EPO) conjugates [20].…”

Section: Introductionmentioning

confidence: 99%

Characterization and large-scale production of recombinant Streptoverticillium platensis transglutaminase

Lin

Hsieh

Lai

et al. 2008

J Ind Microbiol Biotechnol

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Recombinant Streptomyces platensis transglutaminase (MtgA) produced by the Streptomyces lividans transformant 25-2 was purified by ammonium sulfate fractionation, followed by CM-Sepharose CL-6B fast flow, and blue-Sepharose fast flow chromatography. The purification factor was approximately 33.2-fold, and the yield was 65%. The molecular weight of the purified recombinant MtgA was 40.0 KDa as estimated by SDS-PAGE. The optimal pH and the temperature for the enzyme activity were 6.0 and 55 degrees C, respectively, and the enzyme was stable at pH 5.0-6.0 and at temperature 45-55 degrees C. Enzyme activity was not affected by Ca(2+), Li(+), Mn(2+), Na(+), Fe(3+), K(+), Mg(2+), Al(3+), Ba(2+), Co(2+), EDTA, or IAA but was inhibited by Fe(2+), Pb(2+), Zn(2+), Cu(2+), Hg(2+), PCMB, NEM, and PMSF. Optimization of the fermentation medium resulted in a twofold increase of recombinant MtgA activity in both flasks (5.78 U/ml) and 5-l fermenters (5.39 U/ml). Large-scale productions of the recombinant MtgA in a 30-l air-lift fermenter and a 250-l stirred-tank fermenter were fulfilled with maximal activities of 5.36 and 2.54 U/ml, respectively.

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Transglutaminase-Mediated Protein Immobilization to Casein Nanolayers Created on a Plastic Surface

Cited by 39 publications

References 18 publications

Chitosan to Connect Biology to Electronics: Fabricating the Bio-Device Interface and Communicating Across This Interface

Chitosan to Connect Biology to Electronics: Fabricating the Bio-Device Interface and Communicating Across This Interface

C‐Terminal‐oriented Immobilization of Enzymes Using Sortase A‐mediated Technique

Characterization and large-scale production of recombinant Streptoverticillium platensis transglutaminase

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