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1.
Waste Manag ; 141: 16-26, 2022 Mar 15.
Artigo em Inglês | MEDLINE | ID: mdl-35085867

RESUMO

Waste food utilization to produce bio-oil through pyrolysis has received increasing attention. The feedstock can be utilized more efficiently as its properties are upgraded. In this work, the mixed food waste (MFW) was pretreated via torrefaction at moderate temperatures (250-275 °C) under an inert atmosphere before fast pyrolysis. The pyrolysis of torrified MFW (T-MFW) was performed in a bubbling fluidized-bed reactor (FBR) to study the influence of torrefaction on the pyrolysis product distribution and bio-oil compositions. The highest liquid yield of 39.54 wt% was observed at a pyrolysis temperature of 450℃. The torrefaction has a significant effect on the pyrolysis process of MFW. After torrefaction, the higher heating values (HHVs) of the pyrolysis bio-oils (POs) ranged from 31.51 to 34.34 MJ/kg, which were higher than those of bio-oils from raw MFW (27.69-31.58 MJ/kg). The POs mainly contained aliphatic hydrocarbons (alkenes and ketones), phenolic, and N-containing derivatives. The pyrolysis of T-MFW was also carried out under the CO2 atmosphere. The application of CO2 as a carrier gas resulted in a decrease in the liquid yield and an increase in the gas product yield. In addition, the carbon and nitrogen content of POs increased, whereas the oxygen was reduced via the release of moisture and CO. Using CO2 in pyrolysis inhibited the generation of nitriles derivatives in POs, which are harmful to the environment. These results indicated that the application of CO2 to the thermal treatment of T-MFW could be feasible in energy production as well as environmental pollution control.

2.
Front Cardiovasc Med ; 7: 582407, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-33134326

RESUMO

Background: No medical therapies exist to treat right ventricular (RV) remodeling and RV failure (RVF), in large part because molecular pathways that are specifically activated in pathologic human RV remodeling remain poorly defined. Murine models have suggested involvement of Wnt signaling, but this has not been well-defined in human RVF. Methods: Using a candidate gene approach, we sought to identify genes specifically expressed in human pathologic RV remodeling by assessing the expression of 28 WNT-related genes in the RVs of three groups: explanted nonfailing donors (NF, n = 29), explanted dilated and ischemic cardiomyopathy, obtained at the time of cardiac transplantation, either with preserved RV function (pRV, n = 78) or with RVF (n = 35). Results: We identified the noncanonical WNT receptor ROR2 as transcriptionally strongly upregulated in RVF compared to pRV and NF (Benjamini-Hochberg adjusted P < 0.05). ROR2 protein expression correlated linearly to mRNA expression (R 2 = 0.41, P = 8.1 × 10-18) among all RVs, and to higher right atrial to pulmonary capillary wedge ratio in RVF (R 2 = 0.40, P = 3.0 × 10-5). Utilizing Masson's trichrome and ROR2 immunohistochemistry, we identified preferential ROR2 protein expression in fibrotic regions by both cardiomyocytes and noncardiomyocytes. We compared RVF with high and low ROR2 expression, and found that high ROR2 expression was associated with increased expression of the WNT5A/ROR2/Ca2+ responsive protease calpain-µ, cleavage of its target FLNA, and FLNA phosphorylation, another marker of activation downstream of ROR2. ROR2 protein expression as a continuous variable, correlated strongly to expression of calpain-µ (R 2 = 0.25), total FLNA (R 2 = 0.67), calpain cleaved FLNA (R 2 = 0.32) and FLNA phosphorylation (R 2 = 0.62, P < 0.05 for all). Conclusion: We demonstrate robust reactivation of a fetal WNT gene program, specifically its noncanonical arm, in human RVF characterized by activation of ROR2/calpain mediated cytoskeleton protein cleavage.

3.
Biotechnol J ; 10(11): 1762-9, 2015 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-26097135

RESUMO

Bacillus thermocatenulatus lipase 2 (BTL2) is a promising industrial enzyme used in biodiesel production. Although BTL2 has high thermostability and good resistance to organic solvents, the activity of BTL2 is suboptimal for industrial processes. To improve BTL2 activity, we engineered BTL2 lipase by modulating hydrophobicity of its lid domain. Through site-directed mutagenesis, we constructed three mutants, namely Y225F+S232A, S232A+T236V and Q185L, to cover all uncharged hydrophilic amino acids within the lid domain. Activities of these mutants were characterized. Our findings suggest that one mutant (Y225F+S232A) showed ∼35% activity increase in catalyzing heterogeneous hydrolytic reactions relevant for industrial applications. A mathematical framework was established to account for different molecular events that contribute to the observed apparent catalytic activities. Increases in hydrophobicity of lid domains were associated with increased interfacial adsorption of lipases and lower molecular enzymatic activities. The measured apparent activities of lipases include contributions from both events. Lid hydrophobicity can thus result in different changes in lipase activities depending on the mutation site. Our work demonstrates the feasibility of increasing BTL2 activity by modulating the hydrophobicity of lid domains and provides some guidelines for further improving BTL2 activity.


Assuntos
Bacillus/enzimologia , Proteínas de Bactérias/química , Lipase/química , Engenharia de Proteínas/métodos , Proteínas de Bactérias/genética , Proteínas de Bactérias/metabolismo , Interações Hidrofóbicas e Hidrofílicas , Lipase/genética , Lipase/metabolismo , Modelos Moleculares , Estrutura Terciária de Proteína , Propriedades de Superfície
4.
Biotechnol Bioeng ; 111(4): 639-53, 2014 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-24284881

RESUMO

Biodiesel is an environment-friendly and renewable fuel produced by transesterification of various feedstocks. Although the lipase-catalyzed biodiesel production has many advantages over the conventional alkali catalyzed process, its industrial applications have been limited by high-cost and low-stability of lipase enzymes. This review provides a general overview of the recent advances in lipase engineering, including both protein modification and production. Recent advances in biotechnology such as in protein engineering, recombinant methods and metabolic engineering have been employed but are yet to impact lipase engineering for cost-effective production of biodiesel. A summary of the current challenges and perspectives for potential solutions are also provided.


Assuntos
Biocombustíveis , Biotecnologia , Enzimas Imobilizadas , Lipase , Engenharia de Proteínas , Proteínas de Bactérias , Estabilidade Enzimática , Esterificação , Proteínas Fúngicas , Engenharia Metabólica
5.
Chemosphere ; 48(4): 437-44, 2002 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-12152746

RESUMO

In the present work, photocatalytic degradation of volatile organic compounds including gas-phase trichloroethylene (TCE), acetone, methanol and toluene over illuminated TiO2 was closely examined in a batch photoreactor as a function of water vapor, molecular oxygen and reaction temperature. Water vapor enhanced the photocatalytic degradation rate of toluene, but was inhibitive for acetone, and, there was an optimum water vapor concentration in the TCE and methanol removal. In a nitrogen atmosphere, it showed lower photocatalytic degradation rate than in air and pure oxygen. Thus, it could be concluded that oxygen is an essential component in photocatalytic reactions by trapping photogenerated electrons on the semiconductor surface and by decreasing the recombination of electrons and holes. As for the influence of reaction temperature, it was found that photocatalytic degradation was more effective at a moderate temperature than at an elevated temperature for each compound.


Assuntos
Acetona/química , Corantes/química , Metanol/química , Solventes/química , Titânio/química , Tolueno/química , Tricloroetileno/química , Catálise , Poluição Ambiental/prevenção & controle , Fotoquímica , Volatilização
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