Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 8 de 8
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
Crit Rev Food Sci Nutr ; : 1-13, 2021 Nov 19.
Artigo em Inglês | MEDLINE | ID: mdl-34797201

RESUMO

The controlled release of guest molecules from cyclodextrin (CD) inclusion complexes is very important for specific industrial applications in foods, medicine, cosmetics, textiles, agriculture, environmental protection, and chemical materials. The term "controlled release" encompasses several related methods, including those referred to as immediate release, sustained release and targeted release. Many different CD-based controlled release systems are currently used in practical applications. CD inclusion complexes, CD coupling, supramolecular hydrogels, and supramolecular micelles are among the most common. This review systematically introduces the principles and applications of CD-based controlled release systems, providing a theoretical basis for improving the bioavailability of effective substances and broadening their range of application.

2.
Fish Shellfish Immunol ; 55: 88-105, 2016 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-27164217

RESUMO

This study investigated the effects of exogenous lipase supplementation on the growth performance, intestinal growth and function, immune response and physical barrier function, and related signaling molecules mRNA expression of young grass carp (Ctenopharyngodon idella). A total of 450 grass carp (255.02 ± 0.34 g) were fed five diets for 60 days. There were 5 dietary treatments that included a normal protein and lipid diet containing 30% crude protein (CP) with 5% ether extract (EE), and the low-protein and high-lipid diets (28% CP, 6% EE) supplemented with graded levels of exogenous lipase supplementation activity at 0, 1193, 2560 and 3730 U/kg diet. The results indicated that compared with a normal protein and lipid diet (30% CP, 5% EE), a low-protein and high-lipid diet (28% CP, 6% EE) (un-supplemented lipase) improved lysozyme activities and complement component 3 contents in the distal intestine (DI), interleukin 10 mRNA expression in the proximal intestine (PI), and glutathione S-transferases activity and glutathione content in the intestine of young grass carp. In addition, in low-protein and high-lipid diets, optimal exogenous lipase supplementation significantly increased acid phosphatase (ACP) activities and complement component 3 (C3) contents (P < 0.05), up-regulated the relative mRNA levels of antimicrobial peptides (liver expressed antimicrobial peptide 2 and hepcidin) and anti-inflammatory cytokines (interleukin 10 and transforming growth factor ß1) and signaling molecules inhibitor protein-κBα (IκBα) and target of rapamycin (TOR) (P < 0.05), down-regulated the mRNA levels of pro-inflammatory cytokines (tumor necrosis factor α, interleukin 8, interferon γ2, and interleukin 1ß), and signaling molecules (nuclear factor kappa B p65, IκB kinase ß, IκB kinase γ) (P < 0.05) in the intestine of young grass carp. Moreover, optimal exogenous lipase supplementation significantly decreased reactive oxygen species (ROS), malondialdehyde (MDA) and protein carbonyl (PC) contents (P < 0.05), improved the activities of anti-superoxide anion (ASA) and anti-hydroxyl radical (AHR), glutathione content, and the activities and mRNA levels of antioxidant enzymes (copper/zinc superoxide dismutase, manganese superoxide dismutase, catalase, glutathione peroxidase, glutathione S-transferases and glutathione reductase) (P < 0.05), up-regulated signaling molecule NF-E2-related factor 2 (Nrf2) (P < 0.05), down-regulated signaling molecules (Kelch-like-ECH-associated protein 1a, Kelch-like-ECH-associated protein 1b) (P < 0.05) in the intestine of young grass carp. Furthermore, optimal exogenous lipase supplementation significantly elevated the mRNA levels of tight junction proteins (Occludin, zonula occludens 1, Claudin b, Claudin c and Claudin 3) (P < 0.05), down-regulated the mRNA levels of tight junction proteins (Claudin 12 and Claudin 15a) (P < 0.05), down-regulated signaling molecules myosin light chain kinase (P < 0.05) in the intestine of young grass carp. In conclusion, dietary lipid could partially spare protein, and the low-protein and high-lipid diet could improve growth, intestinal growth and function, immune response and antioxidant capability of fish. Meanwhile, in high-fat and low-protein diets, optimal exogenous lipase supplementation improved growth, intestinal growth and function, intestinal immunity, physical barrier, and regulated the mRNA expression of related signal molecules of fish. The optimal level of exogenous lipase supplementation in young grass carp (255-771 g) was estimated to be 1193 U kg(-1) diet.


Assuntos
Carpas/fisiologia , Suplementos Nutricionais , Regulação da Expressão Gênica/efeitos dos fármacos , Imunidade nas Mucosas/efeitos dos fármacos , Lipase , Transdução de Sinais/efeitos dos fármacos , Ração Animal/análise , Animais , Carpas/genética , Dieta/veterinária , Dieta com Restrição de Proteínas/veterinária , Relação Dose-Resposta a Droga , Proteínas de Peixes/genética , Proteínas de Peixes/metabolismo , Intestinos/fisiologia , Lipase/metabolismo , RNA Mensageiro/genética , RNA Mensageiro/metabolismo
3.
Microbiologyopen ; 5(4): 687-99, 2016 08.
Artigo em Inglês | MEDLINE | ID: mdl-27098117

RESUMO

This study addressed the effects of dietary Lactobacillus plantarum or/and N-acylated homoserine lactonase (AHL lactonase) on controlling Aeromonas  hydrophila infection in juvenile hybrid tilapia (Oreochromis niloticus♀ × O. aureus ♂). Fish were fed Lb. plantarum subsp. plantarum strain JCM1149 (10(8)  CFU/g feed) or/and AHL lactonase AIO6 (4 U/g) and were exposed to a chronic challenge of A. hydrophila NJ-1 (10(5)  cells/mL) for 14 days. Intestinal (foregut) alkaline phosphatase (IAP) activities were evaluated 1 day post challenge to reflect the resistance of fish against A. hydrophila infection. Parallel groups of fish with the same dietary assignments while unchallenged were also included to investigate the effect of dietary Lb. plantarum or/and AIO6 supplementation on gut health of tilapia. The results showed that IAP activity was significantly lower in fish fed with diets supplemented with Lb. plantarum JCM1149 or the combination of Lb. plantarum JCM1149 and AIO6, indicating enhanced resistance against A. hydrophila. Light microscopy and transmission electron microscopy images of foregut revealed damage caused by A. hydrophila NJ-1, but dietary Lb. plantarumJCM1149 or/and AIO6 significantly alleviated the damages. Compared to the fish immersed in A. hydrophila NJ-1, dietary Lb. plantarum JCM1149 or AIO6 could maintain the microvilli length in the foregut of tilapia. However, among the unchallenged groups of fish, the microvilli length in the foregut of tilapia fed AIO6 (singly or combination) and the microvilli density of tilapia fed AIO6 (singly) were significantly lower than those of the control, though the microvilli density in the combination treatment was significantly improved. Additionally, the dietary Lb. plantarum JCM1149 could down-regulate the expression of stress-related gene in the gut after the acute phase. In conclusion, the dietary Lb. plantarum JCM1149 is recommended to control the A. hydrophila infection in tilapia.


Assuntos
Aeromonas hydrophila/patogenicidade , Hidrolases de Éster Carboxílico/farmacologia , Doenças dos Peixes/terapia , Lactobacillus plantarum/metabolismo , Probióticos/farmacologia , Tilápia/microbiologia , Aeromonas hydrophila/efeitos dos fármacos , Fosfatase Alcalina/metabolismo , Ração Animal/microbiologia , Animais , Aquicultura/métodos , Dieta , Doenças dos Peixes/microbiologia
4.
Biomed Res Int ; 2015: 248680, 2015.
Artigo em Inglês | MEDLINE | ID: mdl-26171389

RESUMO

α-Amylase as an important industrial enzyme has been widely used in starch processing, detergent, and paper industries. To improve expression efficiency of recombinant α-amylase from Bacillus licheniformis (B. licheniformis), the α-amylase gene from B. licheniformis was optimized according to the codon usage of Pichia pastoris (P. pastoris) and expressed in P. pastoris. Totally, the codons encoding 305 amino acids were optimized in which a total of 328 nucleotides were changed and the G+C content was increased from 47.6 to 49.2%. The recombinants were cultured in 96-deep-well microplates and screened by a new plate assay method. Compared with the wild-type gene, the optimized gene is expressed at a significantly higher level in P. pastoris after methanol induction for 168 h in 5- and 50-L bioreactor with the maximum activity of 8100 and 11000 U/mL, which was 2.31- and 2.62-fold higher than that by wild-type gene. The improved expression level makes the enzyme a good candidate for α-amylase production in industrial use.


Assuntos
Bacillus/enzimologia , Códon/genética , Pichia/genética , Proteínas Recombinantes/genética , alfa-Amilases/genética , Bacillus/genética , Sequência de Bases , Dados de Sequência Molecular , Pichia/metabolismo , Engenharia de Proteínas , Proteínas Recombinantes/análise , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo , Alinhamento de Sequência , alfa-Amilases/análise , alfa-Amilases/química , alfa-Amilases/metabolismo
5.
Protein Expr Purif ; 108: 90-96, 2015 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-25434687

RESUMO

A gene encoding xylanase 2 mutant from Trichoderma reesei (T2C/T28C, named mxyn2) was cloned into the Pichia pastoris X33 strain using the vector pPICZαA. Recombinant Mxyn2p was functionally expressed in P. pastoris X33 and secreted into the supernatant. Real time qPCR demonstrated that an increase in gene copy number correlated with higher levels of expression. Supernatant from methanol induced cells was concentrated by ultrafiltration with a 10kDa cut off membrane, and purified with ion exchange chromatography using SP Sepharose Fast Flow chromatography. Recombinant Mxyn2p protein had the highest activity at 75°C, while recombinant protein encoded by the "wild type" xylanase gene xyn2, also expressed in Pichia, was 20°C lower. The Mxyn2p enzyme retained more than 70% of its activity after incubation at 80°C for 10min. The effects of the optimal pH and temperature for higher expression levels in P. pastoris were also determined, 6.0 and 22°C, respectively. The maximum xylanase activity of Mxyn2p was 13,000nkat/mg (9.88g/l) in fed-batch cultivation after 168h induction with methanol in a 50l bioreactor.


Assuntos
Endo-1,4-beta-Xilanases , Proteínas Fúngicas , Expressão Gênica , Pichia/metabolismo , Mutação Puntual , Trichoderma/enzimologia , Endo-1,4-beta-Xilanases/biossíntese , Endo-1,4-beta-Xilanases/química , Endo-1,4-beta-Xilanases/genética , Endo-1,4-beta-Xilanases/isolamento & purificação , Estabilidade Enzimática , Proteínas Fúngicas/biossíntese , Proteínas Fúngicas/química , Proteínas Fúngicas/genética , Proteínas Fúngicas/isolamento & purificação , Pichia/genética , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/isolamento & purificação , Trichoderma/genética
6.
J Agric Food Chem ; 63(2): 562-8, 2015 Jan 21.
Artigo em Inglês | MEDLINE | ID: mdl-25536291

RESUMO

This is the first report concerning the selenium enrichment of Catathelasma ventricosum mycelia. The selenium-containing proteins present in selenium-enriched mycelia (Se-MC) were identified using size-exclusion chromatography-inductively coupled plasma-mass spectrometry (SEC-ICP-MS). The selenium-containing amino acids liberated by hydrolysis of these proteins were identified using anion exchange-ICP-MS. Se-MC was found to contain selenoproteins with molecular weights ranging from 1.7 to 60.5 kDa. The main selenium-containing amino acids within them were selenomethionine and selenocysteine. Furthermore, Se-MC possessed excellent antihyperglycemic and antioxidant properties. Se-MC normalized biochemical parameters like insulin level, blood glucose level, body weight, and antioxidant enzyme activity in streptozocin-induced diabetic mice. It also inhibited the α-amylase and α-glucosidase activities present in in vitro gastric and intestinal models. In conclusion, Se-MC has the potential to serve as a dietary supplement of selenium, an antioxidant, or an ingredient for the formulation of nutraceuticals.


Assuntos
Agaricales/química , Antioxidantes/química , Diabetes Mellitus Experimental/tratamento farmacológico , Hipoglicemiantes/química , Compostos de Selênio/química , Animais , Antioxidantes/administração & dosagem , Glicemia/metabolismo , Diabetes Mellitus Experimental/metabolismo , Humanos , Hipoglicemiantes/administração & dosagem , Insulina/metabolismo , Masculino , Camundongos , Camundongos Endogâmicos ICR , Micélio/química , Compostos de Selênio/administração & dosagem
7.
Int J Mol Sci ; 15(1): 203-17, 2013 Dec 24.
Artigo em Inglês | MEDLINE | ID: mdl-24368519

RESUMO

A gene encoding Rhizopus oryzae lipase containing prosequence (ProROL) was cloned into the pPICZαA and electrotransformed into the Pichia pastoris X-33 strain. The lipase was functionally expressed and secreted in Pichia pastoris with a molecular weight of 35 kDa. The maximum lipase activity of recombinant lipase (rProROL) was 21,000 U/mL, which was obtained in a fed-batch cultivation after 168 h induction with methanol in a 50-L bioreactor. After fermentation, the supernatant was concentrated by ultrafiltration with a 10 kDa cut off membrane and purified with ion exchange chromatography using SP Sepharose Fast Flow chromatography. The optimum pH and temperature of the rProROL were pH 9.0 and 40 °C, respectively. The lipase was stable from pH 4.0 to 9.0 and from 25 to 55 °C. The enzyme activity was enhanced by Ca(2+) and inhibited by Hg(2+) and Ag(+). The lipase showed high activity toward triglyceride-Tripalmitin (C16:0) and triglyceride-Trilaurin (C12:0).


Assuntos
Proteínas Fúngicas/metabolismo , Lipase/metabolismo , Pichia/metabolismo , Rhizopus/enzimologia , Técnicas de Cultura Celular por Lotes , Cromatografia por Troca Iônica , Clonagem Molecular , Proteínas Fúngicas/química , Proteínas Fúngicas/genética , Concentração de Íons de Hidrogênio , Íons/química , Lipase/química , Lipase/genética , Metais/química , Metais/metabolismo , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/química , Proteínas Recombinantes/isolamento & purificação , Especificidade por Substrato , Temperatura , Ultrafiltração
8.
Food Chem Toxicol ; 62: 285-91, 2013 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-24007742

RESUMO

Se-polysaccharide from Catathelasma ventricosum (SPC-2) was purified by DEAE-52 and Sephadex G-100 column chromatography. The average size of SPC-2 was 1.6×10(5) Da, and it was mainly composed of glucose (87.4%) with the conformation of ß-pyran ring. The branched structure of SPC-2 was proved intuitively by atomic force microscope (AFM). The antidiabetic potential of SPC-2 was tested in STZ-induced diabetic mice. After STZ-induced diabetic mice being administered of SPC-2 for 30 days, SPC-2 treatment significantly reduced the levels of malondialdehyde (MDA) and low-density lipoprotein cholesterol (LDL-C) that were increased by the STZ treatment. Further, the SPC-2 treatment led to increased activity of antioxidant enzymes in liver and kidney and high-density lipoprotein cholesterol (HDL-C) that were decreased by the STZ. The results of histopathology also showed SPC-2 protected tissues (pancreas, liver and kidney) against peroxidation damage and maintained tissue integrity.


Assuntos
Agaricales/química , Diabetes Mellitus Experimental/tratamento farmacológico , Hipoglicemiantes/farmacologia , Polissacarídeos/química , Polissacarídeos/farmacologia , Selênio/farmacologia , Animais , Antioxidantes/metabolismo , Glicemia/metabolismo , Peso Corporal/efeitos dos fármacos , Diabetes Mellitus Experimental/induzido quimicamente , Enzimas/metabolismo , Glicogênio/metabolismo , Hipoglicemiantes/química , Insulina/metabolismo , Rim/efeitos dos fármacos , Rim/metabolismo , Lipídeos/sangue , Fígado/efeitos dos fármacos , Fígado/metabolismo , Fígado/patologia , Masculino , Camundongos Endogâmicos ICR , Monossacarídeos/análise , Micélio , Pâncreas/efeitos dos fármacos , Pâncreas/patologia , Polissacarídeos/isolamento & purificação , Substâncias Protetoras/química , Substâncias Protetoras/farmacologia , Selênio/química , Estreptozocina
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...