A novel type laccase from Shewanella putrefaciens was identified, expressed in Escherichia coli, characterized, prepared in cross-linked enzyme aggregates (CLEA) for industrial applications and investigated of decolorization activity on malchite green dye. Enzyme characterization was investigated by enzyme assay, SDS-PAGE and other biochemical reactions. Moreover, cross-linked enzyme aggregates were prepared and characterized. Saturated ammonium sulphate solution was used as the precipitating agent and cross linked with glutaraldehyde. These CLEA-laccase aggregates showed more catalytic efficiency and more stabilities compared to free laccase against harsh conditions of thermal and chemical agents as well as high reusability. Also it showed more decolorization ability. These results suggest that this CLEA is potentially usable in industrial applications.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.biortech.2013.08.032 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The serum level of sclerostin decreases in radiographic axial spondyloarthritis patients with fatty lesions.
Arthritis Res Ther
January 2025
Department of Rheumatology, the Fifth Affiliated Hospital of Sun Yat-sen University, 52 Meihua East Road, Zhuhai, People's Republic of China.
Background: Currently, the pathophysiology of new bone formation in radiographic axial spondyloarthritis (r-axSpA) remains unclear. Cellular elements and their secreted bone turnover markers might be one of the underlying mechanisms that drive the new bone formation. Our study aimed to investigate the role of bone turnover markers in r-axSpA patients with fatty lesions.
View Article and Find Full Text PDFBone Enzyme-Responsive Biodegradable Poly(propylene fumarate) and Polycaprolactone Polyphosphoester Dendrimer Cross-Linked via Click Chemistry for Bone Tissue Engineering.
Biomacromolecules
January 2025
Department of Physiology and Biomedical Engineering, Mayo Clinic, Rochester, Minnesota 55905, United States.
Traditional polymer systems often rely on toxic initiators or catalysts for cross-linking, posing significant safety risks. For bone tissue engineering, another issue is that the scaffolds often take a longer time to degrade, inconsistent with bone formation pace. Here, we developed an enzyme-responsive biodegradable poly(propylene fumarate) (PPF) and polycaprolactone (PCL) polyphosphoester (PPE) dendrimer cross-linked utilizing click chemistry (EnzDeg-click-PFCLPE scaffold) for enhanced biocompatibility and degradation.
View Article and Find Full Text PDFInter-assay variability in the measurement of urinary C-terminal cross-linked telopeptide of type II collagen following anterior cruciate ligament reconstruction.
Osteoarthr Cartil Open
March 2025
OrthoSport Victoria, Level 5, 89 Bridge Rd, Richmond, Victoria, Australia.
Objective: To compare urinary C-terminal cross-linked telopeptide of type II collagen (u-CTX-II) concentrations and trends as measured by two different commercially available enzyme-linked immunosorbent assays (ELISA) in a cohort of patients in the first year following anterior cruciate ligament (ACL) reconstruction.
Design: 22 ACL-injured patients undergoing reconstructive surgery (mean age 25.2 (SD 8.
Transducing chemical energy through catalysis by an artificial molecular motor.
Nature
January 2025
Department of Chemistry, University of Manchester, Manchester, UK.
Cells display a range of mechanical activities generated by motor proteins powered through catalysis. This raises the fundamental question of how the acceleration of a chemical reaction can enable the energy released from that reaction to be transduced (and, consequently, work to be done) by a molecular catalyst. Here we demonstrate the molecular-level transduction of chemical energy to mechanical force in the form of the powered contraction and powered re-expansion of a cross-linked polymer gel driven by the directional rotation of artificial catalysis-driven molecular motors.
View Article and Find Full Text PDFEfficient Cytosolic Delivery of Single-Chain Polymeric Artificial Enzymes for Intracellular Catalysis and Chemo-Dynamic Therapy.
J Am Chem Soc
January 2025
The State Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200438, P. R China.
Designing artificial enzymes for in vivo catalysis presents a great challenge due to biomacromolecule contamination, poor biodistribution, and insufficient substrate interaction. Herein, we developed single-chain polymeric nanoparticles with Cu/N-heterocyclic carbene active sites (SCNP-Cu) to function as peroxidase mimics for in vivo catalysis and chemo-dynamic therapy (CDT). Compared with the enzyme mimics based on unfolded linear polymer scaffold and multichain cross-linked scaffold, SCNP-Cu exhibits improved tumor accumulation and CDT efficiency both in vitro and in vivo.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!