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1.
Bioorg Chem ; 147: 107418, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38703441

ABSTRACT

A key approach in developing green chemistry involves converting solar energy into chemical energy of biomolecules through photocatalysis. Photocatalysis can facilitate the regeneration of nicotinamide cofactors during redox processes. Nicotinamide cofactor biomimetics (NCBs) are economical substitutes for natural cofactors. Here, photocatalytic regeneration of NADH and reduced NCBs (NCBsred) using graphitic carbon nitride (g-C3N4) was developed. The process involves g-C3N4 as the photocatalyst, Cp*Rh(bpy)H2O2+ as the electron mediator, and Triethanolamine as the electron donor, facilitating the reduction of NAD+ and various oxidative NCBs (NCBsox) under light irradiation. Notably, the highest reduction yield of 48.32 % was achieved with BANA+, outperforming the natural cofactor NAD+. Electrochemical analysis reveals that the reduction efficiency and capacity of cofactors relies on their redox potentials. Additionally, a coupled photo-enzymatic catalysis system was explored for the reduction of 4-Ketoisophorone by Old Yellow Enzyme XenA. Among all the NCBsox and NAD+, the highest conversion ratio of over 99 % was obtained with BANA+. After recycled for 8 times, g-C3N4 maintained over 93.6 % catalytic efficiency. The photocatalytic cofactor regeneration showcases its outstanding performance with NAD+ as well as NCBsox. This work significantly advances the development of photocatalytic cofactor regeneration for artificial cofactors and its potential application.


Subject(s)
Biocatalysis , Oxidation-Reduction , Photochemical Processes , Biomimetic Materials/chemistry , Biomimetic Materials/metabolism , Molecular Structure , NAD/chemistry , NAD/metabolism , Biomimetics , Niacinamide/chemistry , Niacinamide/metabolism , Nitrogen Compounds/chemistry , Graphite
2.
Article in English | MEDLINE | ID: mdl-38381625

ABSTRACT

A large number of 3D spectral descriptors have been proposed in the literature, which act as an essential component for 3D deformable shape matching and related applications. An outstanding descriptor should have desirable natures including high-level descriptive capacity, cheap storage, and robustness to a set of nuisances. It is, however, unclear which descriptors are more suitable for a particular application. This paper fills the gap by comprehensively evaluating nine state-of-the-art spectral descriptors on ten popular deformable shape datasets as well as perturbations such as mesh discretization, geometric noise, scale transformation, non-isometric setting, partiality, and topological noise. Our evaluated terms for a spectral descriptor cover four major concerns, i.e., distinctiveness, robustness, compactness, and computational efficiency. In the end, we present a summary of the overall performance and several interesting findings that can serve as guidance for the following researchers to construct a new spectral descriptor and choose an appropriate spectral feature in a particular application.

3.
Enzyme Microb Technol ; 170: 110286, 2023 Oct.
Article in English | MEDLINE | ID: mdl-37499311

ABSTRACT

ZEN lactone hydrolase (ZHD) can hydrolyze zearalenone (ZEN) to less or non-toxic product, providing an environment-friendly way for food or feeds-containing ZENs detoxification. Here, a newly identified ZHD from Phialophora attinorum, annotated as Zhd11D, was characterized to exhibit highest activity against ZEN at pH 8.0 and 35 â„ƒ with a specific activity of 304.7 U/mg, which was far higher than most of the reported ZHDs. A nonspecific protein engineering method was introduced through fusing a segment of amphiphilic short peptide S1 at the N-terminus of Zhd11D, resulting in both improved activity (1.5-fold) and thermostability (2-fold at 40 â„ƒ). Biochemical analysis demonstrated that self-aggregation caused by intermolecular interactions between S1 contributed to the improvement of the enzymatic properties of Zhd11D. Additionally, S1-Zhd11D showed a higher hydrolysis rate of ZEN than Zhd11D in peanut oil.


Subject(s)
Zearalenone , Zearalenone/chemistry , Zearalenone/metabolism , Phialophora/metabolism , Hydrolases/metabolism , Lactones
4.
Affect Sci ; 4(2): 332-349, 2023 Jun.
Article in English | MEDLINE | ID: mdl-37293682

ABSTRACT

Effectively communicating pain is crucial for human beings. Facial expressions are one of the most specific forms of behavior associated with pain, but the way culture shapes expectations about the intensity with which pain is typically facially conveyed, and the visual strategies deployed to decode pain intensity in facial expressions, is poorly understood. The present study used a data-driven approach to compare two cultures, namely East Asians and Westerners, with respect to their mental representations of pain facial expressions (experiment 1, N=60; experiment 2, N=74) and their visual information utilization during the discrimination of facial expressions of pain of different intensities (experiment 3; N=60). Results reveal that compared to Westerners, East Asians expect more intense pain expressions (experiments 1 and 2), need more signal, and do not rely as much as Westerners on core facial features of pain expressions to discriminate between pain intensities (experiment 3). Together, those findings suggest that cultural norms regarding socially accepted pain behaviors shape the expectations about pain facial expressions and decoding visual strategies. Furthermore, they highlight the complexity of emotional facial expressions and the importance of studying pain communication in multicultural settings. Supplementary Information: The online version contains supplementary material available at 10.1007/s42761-023-00186-1.

5.
Article in English | MEDLINE | ID: mdl-32309279

ABSTRACT

Pectate lyases (Pels) can be used in the textile industrial process for cotton scouring and ramie degumming, and its hydrolyzed products oligo galacturonic acid, are high-value added agricultural and health products. In our previous studies, an alkaline pectate lyase PEL168 mutant, PEL3, was obtained with improved specific activity and thermostability. Here, a facile and rapid method for preparing an immobilized PEL3-inorganic hybrid nanoflower was developed, as it could improve its biocatalytic performance. With 0.02 mg/mL (112.2 U/mL) PEL3 in PBS buffer, five different divalent ions, including Mn2+, Ca2+, Co2+, Zn2+, and Cu2+, were used as inorganic component. The results showed that PEL3/Cu3(PO4)2 hybrid nanoflowers presented the highest relative activity with 2.5-fold increase, compared to the free PEL3. X-ray diffraction analysis confirmed that the composition of PEL3/Cu3(PO4)2 hybrid nanoflowers were pectate lyase PEL3 and Cu3(PO4)2⋅5H2O. The optimum temperature and pH of PEL3/Cu3(PO4)2 hybrid nanoflowers were ascertained to be 55°C and pH 9.0, respectively, exhibiting subtle difference from the free PEL3. However, the PEL3/Cu3(PO4)2 hybrid nanoflowers maintained 33% residual activity after 24 h incubation at 55°C, while the free PEL3 completely lost its activity after 18 h incubation at 55°C. Furthermore, over 50% residual activity of the PEL3/Cu3(PO4)2 hybrid nanoflowers was remained, even after four times of repetitive utilization, demonstrating its promising stability for practical application.

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