A Single-Center, Prospective, Randomized, Investigator-Initiated Exploratory Clinical Trial Comparing the Improvement of Knee Joint Range of Motion in Patients Undergoing Total Knee Arthroplasty Between the Experimental Group Using the Musculoskeletal Rehabilitation Software (re-R) and the Control Group Performing Self-Rehabilitation Exercises

开始日期2025-03-01

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Sun Moon University

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3,361

项与 Sun Moon University 相关的文献（医药）

2025-06-01·Carbohydrate Polymer Technologies and Applications

CAZyme analysis and functional characterization of a new GH18 chitin hydrolase from Gelidibacter salicanalis PAMC21136

作者: Pardhe, Bashu Dev ; Han, So-Ra ; Lee, Jun Hyuck ; Oh, Tae-Jin ; Paudel, Lakshan

Gelidibacter salicanalis strains remain poorly understood in terms of their genomic attributes and are rarely reported for the degradation of polysaccharides within the niche.Gelidibacter salicanalis PAMC21136, an Antarctic isolate, was sequenced and functionally annotated. 251 genes were classified into the CAZyme families, which includes the highest number of GH family, highlighting peculiarity towards various macro biopolymers.Further, based on domain architecture and multiple sequence alignment, gene belonging to the family18 glycoside hydrolase was identified as chitinase.The gene encoding chitinase (MBJ7879808.1) was successfully cloned and expressed in Escherichia coli BL21 cells.MBJ7879808.1 demonstrated activity towards colloidal chitin but there was no detectable activity towards microcrystalline crab shell chitin.Enzyme exhibited an exo-pattern of hydrolysis on both colloidal chitin, and shorter chain GlcNAc oligomers namely [(GlcNAc)₃, (GlcNAc)_4, (GlcNAc)₅, and (GlcNAc)₆] producing GlcNAc as a single final product.Biochem. characterization revealed an optimum activity at 25 °C and pH 7.0.Mn²⁺ ions significantly enhanced the activity by 1.7-fold.Turnover number (K_cat) was 8.6 min^-1 and catalytic efficiency (K_cat/K_m) was 2.0ml/mg/min towards the substrate colloidal chitin.These findings expanded the polysaccharide degradation capability of Gelidibacter salicanalis PAMC21136 and highlight the biotechnol. potential of the GH18 enzyme towards production of chitooligomers.

2025-06-01·Biochemical and Biophysical Research Communications

Crystal structure and biochemical characterization of aldehyde dehydrogenase isolated from Rhodococcus sp. PAMC28705

Article

作者: Kim, Subin ; Park, Hyun Ho ; Thapa, Gobinda ; Oh, Tae-Jin

Aldehyde dehydrogenase (ALDH) is a widely recognized oxidoreductase that converts toxic aldehydes into harmless carboxylic acids, making it highly valuable for industrial applications. However, the effectiveness of ALDHs derived from Rhodococcus species in processing a range of aliphatic and aromatic aldehydes is still largely unexamined. Therefore, we cloned the ALDH gene from the cold-adapted strain Rhodococcus sp. PAMC28705 to address this gap and subsequently identified the crystal structure of rhALDH. By analyzing the unique structural features of the rhALDH active site, we evaluated its ability to process a wide range of aldehydes, with a focus on substrate specificity. Biochemical characterization revealed that at an optimal temperature of 30 °C and a pH of 8.0, it exhibited the highest catalytic efficiency, with a k_cat/K_m value of 1.12 μM^-1 s^-1 for propionaldehyde, which was higher than that of its homologous ALDHs. This indicates a strong affinity for this substrate, as demonstrated by a low K_m of 321.9 μM and a rapid turnover rate k_cat of 359.2 s^-1. Adding disulfide reductants, such as dithiothreitol, 2-mercaptoethanol, and the metal ion Mg²⁺, further enhanced its activity. Working at mesophilic temperatures with good stability and substrate-specific catalytic efficiency, this novel rhALDH, which favors the conversion of propionaldehyde and benzaldehyde, provides a promising catalyst for biotechnological and sustainable bio-aldehyde elimination technologies. Thus, this study lays a foundation for future structure-function analyses of rhALDH, facilitating molecular modifications, the generation of mutants for improved stability, and the development of ALDH-targeted antibiotics.

2025-05-01·Ceramics International

Ultraviolet photon upconversion in Er–SiAlON under 1550 nm excitation

作者: Murali, G. ; Regmi, Chhabilal ; Thapa, Rocky ; Kim, Hak Soo ; Torii, Shuki ; Kshetri, Yuwaraj K. ; Kamiyama, Takashi ; Choi, Jinhyuk ; Kim, Tae-Ho ; Chaudhary, Bina

SiAlON ceramics are well known for their exceptional mech., thermal, and chem. stability, making them ideal for demanding industrial applications such as cutting tools, equipment for molten metal handling, extrusion molds, gas turbine engines, etc.Despite these applications, the potential for photonic applications such as photon upconversion (UC) in SiAlON ceramics remains less explored.This report demonstrates broad spectral photon UC properties in Er-doped SiAlON (Er-SiAlON) ceramics, covering the UV to near-IR (NIR) range upon 1550 nm excitation.The Er-SiAlON ceramic was synthesized by hot press sintering.X-ray diffraction (XRD), transmission electron microscopy (TEM) and elemental mapping results confirmed the stabilization of the α-SiAlON phase by Er³⁺ ions.Optical spectra showed distinct transitions of Er³⁺ ions and high transparency of over 70 % in the mid-IR range for the sample thickness of 0.49 mm.Under 1550 nm excitation, UC emission spectra revealed UV, violet, blue, green, red, and NIR emissions.The Er³⁺ ions exhibited self-sensitization, acting both as sensitizers and activators for the UC luminescence.Decay curve anal. showed long excited state lifetimes, with ground state absorption (GSA), excited state absorption (ESA), and energy transfer UC (ETU) processes facilitating multi-photon absorption and diverse spectral emissions.Given the inherent mech. properties of SiAlON ceramics, these findings highlight the potential of Er-SiAlON ceramics for advanced UC photonic devices operating in high-temperature and harsh environments.

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