Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 4 de 4
Filtrar
Más filtros

Bases de datos
Tipo del documento
Asunto de la revista
País de afiliación
Intervalo de año de publicación
1.
Environ Res ; 215(Pt 1): 114291, 2022 12.
Artículo en Inglés | MEDLINE | ID: mdl-36103929

RESUMEN

Fermentable sugar production from lignocellulosic biomass has received considerable attention and has been dramatic progress recently. However, due to low enzymatic hydrolysis (EH) yields and rates, a high dosage of the costly enzyme is required, which is a bottleneck for commercial applications. Over the last decades, various strategies have been developed to reduce cellulase enzyme costs. The progress of the non-catalytic additive proteins in mitigating inhibition in EH is discussed in detail in this review. The low efficiency of EH is mostly due to soluble lignin compounds, insoluble lignin, and harsh thermal and mechanical conditions of the EH process. Adding non-catalytic proteins into the EH is considered a simple and efficient approach to boost hydrolysis yield. This review discussed the multiple mechanical steps involved in the EH process. The effect of physicochemical properties of modified lignin on EH and its interaction with cellulase and cellulose are identified and discussed, which include hydrogen bonding, hydrophobic, electrostatic, and cation-π interactions, as well as physical barriers. Moreover, the effects of different conditions of EH that lead to cellulase deactivation by thermal and mechanical mechanisms are also explained. Finally, recent advances in the development, potential mechanisms, and economic feasibility of non-catalytic proteins on EH are evaluated and perspectives are presented.


Asunto(s)
Celulasa , Lignina , Biomasa , Celulasa/química , Celulasa/metabolismo , Celulosa/química , Celulosa/metabolismo , Hidrólisis , Lignina/química , Estudios Prospectivos , Azúcares
2.
Bioresour Technol ; 362: 127861, 2022 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-36041679

RESUMEN

This study proposed a mild chlorination-sulfonation approach to synthesize magnetic carbon acid bearing with catalytic SO3H and adsorption Cl bifunctional sites on polydopamine coating. The catalysts exerted good textural structure and surface chemical properties (i.e., porosity, high specific surface area of >70 m2/g, high catalytic activity with 0.86-1.1 mmol/g of SO3H sites and 0.8%-1.9% of Cl sites, and abundant hydrophilic functional groups), rendering a maximum cellobiose adsorption efficiency of ∼40% within 6 h. Moreover, the catalysts had strong fracture characteristics on different α-/ß-glycosidic bonds with 85.4%-93.9% of disaccharide conversion, while selectively fractionating hemicellulose from wheat straw with 64.3% of xylose yield and 93.4% of cellulose retention. Due to the stable interaction between parent polydopamine support with Fe core and functional groups, the catalysts efficiently recovered by simple magnetic separation had good reusability with minimal losses in catalytic activity.


Asunto(s)
Carbono , Glicósidos , Carbono/química , Catálisis , Polisacáridos
3.
J Agric Food Chem ; 66(40): 10628-10639, 2018 Oct 10.
Artículo en Inglés | MEDLINE | ID: mdl-30192539

RESUMEN

The roles of microRNAs (miRNAs) related to ethylene response in banana fruits remain unknown because many miRNAs are differentially expressed as the fruit ripens, making the identification of ethylene-responsive miRNAs difficult. Using newly harvested banana fruits (within 5 h after harvest) as material, we found that these fruit did not ripen when treated with 5 µL/L of ethylene for 12 h at 22 °C. Two miRNA libraries were generated from newly harvested banana fruits with and without ethylene treatment and sequenced. In total, 128 known miRNAs belonging to 42 miRNA families were obtained, and 12 novel miRNAs were identified. Among them, 22 were differentially expressed in response to ethylene treatment, among which 6 known miRNAs and their putative targets were validated using qRT-PCR. These putative targets encoded proteins including GATA, ARF, DLC, and AGO, etc. KEGG and GO analyses showed that miRNAs differentially expressed in response to ethylene mainly function in the molecular and biological processes.


Asunto(s)
Etilenos/farmacología , MicroARNs/genética , Musa/efectos de los fármacos , Reguladores del Crecimiento de las Plantas/farmacología , Proteínas de Plantas/genética , Frutas/efectos de los fármacos , Frutas/genética , Frutas/metabolismo , Regulación de la Expresión Génica de las Plantas/efectos de los fármacos , Secuenciación de Nucleótidos de Alto Rendimiento , MicroARNs/metabolismo , Musa/genética , Musa/metabolismo , Proteínas de Plantas/metabolismo
4.
J Agric Food Chem ; 58(18): 10195-201, 2010 Sep 22.
Artículo en Inglés | MEDLINE | ID: mdl-20718432

RESUMEN

Longan polyphenoloxidase (PPO) was extracted and partially purified using ammonium sulfate precipitation and dialysis. The PPO characterizations were compared using endogenous substrate (-)-epicatechin and exogenous substrate catechol. The optimal pH and optimal temperature for the PPO activity were different when reacting with both substrates. The addition of ethylenediaminetetraacetic acid disodium salt into both substrate-enzyme systems exhibited the same lowest inhibition of the PPO activity. L-ascorbic acid and L-cysteine were the best inhibitors to endogenous substrate-enzyme system, while L-ascorbic acid and glutathione were most effective inhibitors to exogenous substrate-enzyme system. Cupric (Cu2+), ferric (Fe3+), and ferrous (Fe2+) ions accelerated the enzymatic-catalyzed reactions of both substrates. Kinetic analysis indicated that longan PPO strongly bound endogenous substrate but possessed a higher catalytic efficiency to exogenous substrate, and moreover, (-)-epicatechin was determined as the optimal substrate for longan PPO. This study is useful to exactly illuminate the enzymatic-catalyzed browning mechanism of postharvest longan fruit.


Asunto(s)
Catecol Oxidasa/metabolismo , Frutas/enzimología , Proteínas de Plantas/metabolismo , Sapindaceae/enzimología , Catequina/metabolismo , Catecol Oxidasa/antagonistas & inhibidores , Catecol Oxidasa/aislamiento & purificación , Catecoles/metabolismo , Cinética , Proteínas de Plantas/antagonistas & inhibidores , Proteínas de Plantas/aislamiento & purificación , Especificidad por Sustrato
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA