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1.
BMJ Open ; 11(8): e043883, 2021 08 10.
Artigo em Inglês | MEDLINE | ID: mdl-34376438

RESUMO

OBJECTIVE: The transmuscular quadratus lumborum (TQL) block and the oblique subcostal transversus abdominis plane (OSTAP) block both contribute to multimodal analgesia after laparoscopic surgery. The objective of this study was to compare the analgesic effects of the TQL block versus OSTAP block after laparoscopic hysterectomy. DESIGN: Prospective single-centre randomised single-blind trial. SETTING: University-affiliated hospital. PARTICIPANTS: Patients aged between 18 and 65 years scheduled for laparoscopic hysterectomy. INTERVENTIONS: Patients were randomised into two groups (1:1 ratio) and received bilateral TQL block or bilateral OSTAP block with 0.375% ropivacaine 20 mL on each side before surgery. PRIMARY AND SECONDARY OUTCOME MEASURES: The primary outcome measure was the cumulative morphine dose in the first 24 hours. The secondary outcome measures were the morphine consumption at each time interval after surgery, the time from the end of surgery to the first need for morphine, the Numerical Rating Scale (NRS) scores for visceral and incisional pain intensity, and the incidence of adverse events. RESULTS: The cumulative morphine dose was significantly lower in the TQL group than in the OSTAP group (17.2 (12.5) vs 26.1 (13.3) mg, p=0.010). Compared with the OSTAP group, the morphine doses from 6 to 12, 12 to 18, and 18 to 24 hours were significantly lower, the time of first need for morphine was significantly longer and the NRS scores for visceral pain intensity were significantly lower in the TQL group. CONCLUSION: Compared with the OSTAP block, the TQL block reduced morphine consumption and provided better visceral pain relief with a longer duration of effect after laparoscopic hysterectomy. TRIAL REGISTRATION NUMBER: Chinese Clinical Trial Registry (ChiCTR1800017995); pre-results.


Assuntos
Analgesia , Laparoscopia , Músculos Abdominais , Adolescente , Adulto , Idoso , Analgésicos Opioides , Anestésicos Locais , Método Duplo-Cego , Feminino , Humanos , Histerectomia , Pessoa de Meia-Idade , Dor Pós-Operatória/tratamento farmacológico , Dor Pós-Operatória/prevenção & controle , Estudos Prospectivos , Método Simples-Cego , Adulto Jovem
2.
Ann Palliat Med ; 10(6): 6104-6111, 2021 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-34044563

RESUMO

BACKGROUND: A larger volume of local anesthetic provides a wider range of blocked sensory but carries a greater risk. The purpose of this trial was to compare the effect of different volumes of ropivacaine injected to deep serratus anterior plane in patients undergoing breast surgery. METHODS: In this randomized double-blind trial, 60 patients undergoing breast surgery were randomly allocated to R10, R20 and R30 groups (n=20), and received deep serratus anterior plane block with 10, 20 and 30 mL of 0.5% ropivacaine respectively. 30 minutes after block, the cutaneous sensory was tested by cold stimulus in the craniocaudal direction along the midaxillary line. We recorded the numerical rating scale pain scores over 24 h after surgery and estimated the area under curve by numerical rating scale pain scores. The cases of rescue analgesia and the prevalence of adverse events were also recorded. RESULTS: The blocked dermatomes were 3 [3, 4], 6 [5, 7] and 7 [6, 8] in the R10, R20 and R30 groups, respectively (R10 vs. R20, P<0.001; R10 vs. R30, P<0.001; R20 vs. R30, P=0.005). The area under curve of R10 group was significantly higher compared with the R20 and R30 groups (P=0.014, P=0.003, at rest; P<0.001, P<0.001, on movement). CONCLUSIONS: The blocked dermatomes increased with increasing volume when 10, 20 and 30 mL ropivacaine was used for deep serratus anterior plane block. The analgesic effects of 20 and 30 mL were similar to each other and better than 10 mL. Therefore, in breast surgery, volume of 20 mL ropivacaine is considered to be appropriate for deep serratus anterior plane block.


Assuntos
Neoplasias da Mama , Bloqueio Nervoso , Neoplasias da Mama/tratamento farmacológico , Neoplasias da Mama/cirurgia , Feminino , Humanos , Dor Pós-Operatória/tratamento farmacológico , Dor Pós-Operatória/prevenção & controle , Estudos Prospectivos , Ropivacaina
3.
J Pain Res ; 13: 997-1005, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-32494188

RESUMO

Purpose: Continuous femoral nerve block (cFNB) is effective for analgesia after total knee arthroplasty (TKA). However, it is not clear which low-dose regimen of ropivacaine infusion for cFNB provides adequate analgesia and enables rapid recovery. The aim of this study was to compare the effects of different cFNB regimens on rehabilitation of patients after TKA. Patients and Methods: Sixty patients scheduled for TKA were enrolled in this trial. After surgery, patients in the 0.1%, 0.15%, and 0.2% groups received infusion of 10 mL of 0.1%, 6.7 mL of 0.15%, and 5 mL of 0.2% ropivacaine per hour, respectively (n=20), at the dose of 10 mg/h for 48 h. The primary endpoint was time to readiness for discharge. The secondary endpoints were time to first walk, manual muscle testing (MMT) scores, numerical rating scale (NRS) scores at rest and movement, morphine consumption, rescue analgesia, and the incidence of adverse events. Results: The time to readiness for discharge and the time to first walk of the 0.1% group were significantly longer than that of the 0.15% and 0.2% groups. MMT scores of the 0.2% group at 18 h after surgery were significantly lower than those of the 0.1% group. MMT scores of the 0.2% group at 24 and 48 h after surgery were also significantly lower than those of the 0.1% and 0.15% groups. NRS scores at rest and at movement in the 0.1% group were significantly higher than those in the 0.15% and 0.2% groups. Conclusion: Patients administered the regimens of 0.15% and 0.2% ropivacaine infusion for cFNB were ready for discharge earlier than the 0.1% group after TKA, at the dose of 10 mg/h for 48 h. The regimen of 0.15% ropivacaine, which is associated with less quadriceps muscle strength weakness than 0.2%, is recommended for postoperative analgesia after TKA.

4.
J Pain Res ; 13: 57-64, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-32021395

RESUMO

Purpose: Serratus anterior plane (SAP) block is effective for analgesia after breast surgery. Whether a higher local anesthetic concentration prolongs sensory block duration and improves postoperative analgesia remains unclear. The aim of this study was to compare the analgesic effects of SAP block with different concentrations of ropivacaine. Patients and Methods: Sixty patients scheduled for breast surgery were enrolled in this randomized double-blind trial. SAP block was induced with 20 mL of 0.375%, 0.5%, or 0.75% ropivacaine in Group R0.375, Group R0.5, and Group R0.75, respectively. The primary endpoint was the area under the curve (AUC) of numerical rating scale (NRS) pain intensity scores at rest over time. The secondary endpoints were AUC of NRS pain intensity scores on movement over time, active sensory block duration, tramadol consumption, and the elapsed time between completion of surgery and the first administration of rescue analgesia. Results: The AUC of NRS pain intensity scores at rest of Group R0.375 was significantly higher than that of Groups R0.5 and R0.75 (P=0.025, and P=0.001). The AUC of NRS pain intensity scores on movement of Group R0.375 was also significantly higher than that of Groups R0.5 and R0.75 (both P<0.001). At higher ropivacaine concentrations, the duration of SAP sensory block increased (P<0.001). Tramadol consumption and the elapsed time between completion of surgery and the first administration of rescue analgesia were similar in the three groups (P>0.05). Conclusion: A comparison of 0.5% and 0.75% ropivacaine showed no significant difference in postoperative analgesia, but both were superior to 0.375% ropivacaine, although higher ropivacaine concentration lengthened the duration of SAP block. Therefore, SAP block with 0.5% ropivacaine is recommended for postoperative analgesia in breast surgery.

5.
Bioprocess Biosyst Eng ; 42(11): 1739-1746, 2019 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-31321527

RESUMO

A rational enhancement of kinetic resolution process for producing (S)-N-(2-ethyl-6-methylphenyl) alanine from racemic methyl ester using lipase B from Candida antarctica (CalB) was investigated. With the benefit results that lipase CalB-catalyzed reactions can be effectively regulated using amino acids (such as histidine and lysine) as additives, CalBs modified (mCalBs) by n-histidines at the N terminal and n-lysines at the C terminal were constructed and expressed. The results show that both soluble and precipitated mCalBs can effectively catalyze the hydrolysis reaction without adding any extra additives. The enantioselective ratio (E value) of soluble and precipitated mCalBs could be improved from 12.1 to 20.3, which were higher than that (E value was only 10.2) of commercial Novozym 435 (immobilized CalB). The study indicated that the amino acid-rich molecules introduced on lipase CalB can produce positive effects on enantioselectivity of enzyme. It provides unusual ideas for reasonable regulation of enzyme-catalyzed reactions.


Assuntos
Enzimas Imobilizadas/química , Proteínas Fúngicas/química , Lipase/química , Catálise , Enzimas Imobilizadas/genética , Enzimas Imobilizadas/metabolismo , Proteínas Fúngicas/genética , Proteínas Fúngicas/metabolismo , Lipase/genética , Lipase/metabolismo , Domínios Proteicos , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo
6.
J Microbiol Biotechnol ; 29(4): 607-616, 2019 Apr 28.
Artigo em Inglês | MEDLINE | ID: mdl-30954031

RESUMO

In this study, functionalized poplar powder (FPP) was used as a support material for the immobilization of enoate reductase (ER) and glucose-6-phosphate dehydrogenase (GDH) by covalent binding. Under optimal conditions, the immobilization efficiency of ER-FPP and GDH-FPP was 95.1% and 84.7%, and the activity recovery of ER and GDH was 47.5% and 37.8%, respectively. Scanning electron microscopy (SEM) and energy dispersive spectroscopy (EDS) analysis indicated that FPP was a suitable carrier for enzyme immobilization. ER-FPP and GDH-FPP exhibit excellent thermal stabilities and superior reusability. Especially, ER-FPP and GDH-FPP enable the continuous conversion of 4-(4-Methoxyphenyl)-3-buten-2-one with NAD+ recycling. While the immobilization strategies established here were simple and inexpensive, they exploited a new method for the immobilization and application of ER and its cofactor recycling system.


Assuntos
Coenzimas/metabolismo , Enzimas Imobilizadas/metabolismo , Imobilização/métodos , Oxirredutases/metabolismo , Populus/química , Estabilidade Enzimática , Etilenodiaminas , Glucosefosfato Desidrogenase/metabolismo , Glutaral , Lignina/química , Regeneração
7.
Int J Biol Macromol ; 133: 226-234, 2019 Jul 15.
Artigo em Inglês | MEDLINE | ID: mdl-30986456

RESUMO

In our previous study, we could achieve high soluble expression of Candida antarctica lipase B (CalB) in E. coli by fusion poly­amino acid tags on CalB (pCalB). Herein, we are surprised to find that pCalB can be easily and directly covalent binding on a simply oxidized aspen powder (OAP) by the aid of poly­lysine tags. Under the optimal conditions, 72.9 ±â€¯3.6% of the total protein could be immobilized, and the activity recovery of immobilized pCalB (pCalB-OAP) was 98.9 ±â€¯3.8%. The analysis of scanning electron microscopy (SEM) and Fourier transform infrared spectroscopy (FTIR) indicated that OAP was a suitable carrier for enzyme immobilization. The immobilized pCalB-OAP could exhibit excellent thermal stabilities, and it retained a residual activity of 58.4 ±â€¯2.8% at 55 °C, whereas only 21.2 ±â€¯2.2% of its initial activity for free pCalB was observed. And it could also display a nice tolerance for the changes of pH environment, compared with that of free pCalB. The results that pCalB-OAP could retained 73.6 ±â€¯2.9% of their initial activity in (R, S)-NEMPAME hydrolysis after the tenth cycles, suggested that pCalB-OAP could be effectively recycled. The immobilization strategies established here were simple and inexpensive.


Assuntos
Biomassa , Enzimas Imobilizadas/química , Enzimas Imobilizadas/metabolismo , Proteínas Fúngicas/química , Proteínas Fúngicas/metabolismo , Lipase/química , Lipase/metabolismo , Polilisina/química , Populus/química , Estabilidade Enzimática , Oxirredução , Pós
8.
J Biotechnol ; 289: 64-70, 2019 Jan 10.
Artigo em Inglês | MEDLINE | ID: mdl-30468819

RESUMO

Herein, three aldo/ketoreductases (AKRs) were obtained and used to prepare N- ethyl-methyl-carbamic acid-3-[(1S)-hydroxy-ethyl]-phenyl ester ((S)-NEMCA-HEPE), which is a key intermediate of (S)-Rivastigmine. To avoid the usage of extra cofactors, the recombinant whole-cells containing AKRs and glucose dehydrogenase (GDH) were constructed and applied in the reduction reaction. The excellent conversion of 83.3% and enantiomeric excess (e.e.p) of 99.9% for (S)-NEMCA-HEPE was obtained when the recombinant whole cell (iolS-GDH) was selected as a catalyst. Additional introduction of 1-butyl-3-methylimidazolium tetrafluoroborate ([BMIm]BF4) in the whole cell-catalyzed reaction system, the reaction rates can be further enhanced, and the reaction conversion can be increased to 98.3% only in 1 h. The analysis of flow cytometry (FCM) and ultraviolet spectrum shows that [BMIm]BF4 can greatly enhance the whole cell-catalyzed reaction activities by affecting the permeability of cell membrane. This study provided a low-cost and efficient process for preparation of (S)-NEMCA-HEPE with high optical purity.


Assuntos
Aldo-Ceto Redutases/metabolismo , Glucose 1-Desidrogenase/metabolismo , Rivastigmina/metabolismo , Aldo-Ceto Redutases/genética , Bacillus subtilis/enzimologia , Bacillus subtilis/genética , Escherichia coli/genética , Glucose 1-Desidrogenase/genética , Estereoisomerismo
9.
Enzyme Microb Technol ; 109: 66-73, 2018 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-29224628

RESUMO

Herein we established co-immobilized methods for enoate reductases (ERs) and glucose dehydrogenase (GDH), forming a cofactor regeneration system. In cross-linked enzyme aggregates (CLEAs), ammonium sulfate and oxidized dextran were selected as a precipitant and a cross-linker, respectively. In biomimetic immobilization (BI), ER-GDH-silica particles (ER-GDH-SPs) were rapidly formed through a one-step approach by using a silicic acid precursor. Under the optimal conditions, the ER activity recovery in ER-GDH-CLEAs and ER-GDH-SPs were 44.9±1.8% and 44.5±2.1%, and the immobilization efficiency was 93.5±1.2% and 92.4±1.2%, respectively. ER-GDH-CLEAs and ER-GDH-SPs exhibit excellent thermal and pH stability, and superior reusability. The activity of ER-GDH-SPs toward the substrate is also better than that of free ER and GDH in reduction of 4-(4-Methoxyphenyl)-3-buten-2-one. This study introduces simple and inexpensive co-immobilization strategies to construct novel and efficient ER-GDH-CLEAs and ER-GDH-SPs with high activity and stability.


Assuntos
Reagentes para Ligações Cruzadas/metabolismo , Enzimas Imobilizadas/metabolismo , Glucose 1-Desidrogenase/metabolismo , Oxirredutases atuantes sobre Doadores de Grupo CH-CH/metabolismo , Dióxido de Silício/química , Estabilidade Enzimática , Cinética , Oxirredução
10.
J Biotechnol ; 249: 1-9, 2017 May 10.
Artigo em Inglês | MEDLINE | ID: mdl-28323015

RESUMO

Polyamine tags fused in Candida antarctica lipase B (CalB) can help achieve high soluble expression of CalB in E. coli and can directly mediate silicification, which leads to rapid formation of a CalB-silica particle complex through a one-step approach. After optimization experiments, the fused lipase CalB tagged with 6-histidine at the N terminal and 10-lysine at the C terminal (6His-CalB-10Lys) is effectively expressed with high solubility (0.1mg/mL) and specific activity (10.1U/mg), and easily cross-linked in silica particles with a high immobilization efficiency of 96.8% and activity recovery of 81.5%. The immobilized lipase 6His-CalB-10Lys exhibits excellent performance at broad temperature ranges, high thermal and storage stabilities, and superior reusability. Michaelis-Menten kinetics indicates that the affinity and enantioselectivity of the free and immobilized 6His-CalB-10Lys toward the substrate are better than that of commercial Novozym 435 in enantioselective resolution of (S)-N-(2-ethyl-6-methylphenyl) alanine ((S)-NEMPA). The strategies described in this paper are useful for the facile expression and construction of diverse enzyme systems with high efficiency and excellent recyclability.


Assuntos
Enzimas Imobilizadas , Proteínas Fúngicas , Lipase , Poliaminas , Proteínas Recombinantes de Fusão , Biomimética , Enzimas Imobilizadas/química , Enzimas Imobilizadas/genética , Enzimas Imobilizadas/metabolismo , Escherichia coli/genética , Proteínas Fúngicas/química , Proteínas Fúngicas/genética , Proteínas Fúngicas/metabolismo , Histidina/química , Histidina/genética , Histidina/metabolismo , Lipase/química , Lipase/genética , Lipase/metabolismo , Oligopeptídeos/química , Oligopeptídeos/genética , Oligopeptídeos/metabolismo , Poliaminas/química , Poliaminas/metabolismo , Proteínas Recombinantes de Fusão/química , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Dióxido de Silício
11.
Enzyme Microb Technol ; 84: 32-40, 2016 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-26827772

RESUMO

The first Novozym 435 lipase-catalyzed Morita-Baylis-Hillman (MBH) reaction with amides as co-catalyst was realized. Results showed that neither Novozym 435 nor amide can independently catalyze the reaction. This co-catalytic system that used a catalytic amount of Novozym 435 with a corresponding amount of amide was established and optimized. The MBH reaction strongly depended on the structure of aldehyde substrate, amide co-catalyst, and reaction additives. The optimized reaction yield (43.4%) was achieved in the Novozym 435-catalyzed MBH reaction of 2, 4-dinitrobenzaldehyde and cyclohexenone with isonicotinamide as co-catalyst and ß-cyclodextrin as additive only in 2 days. Although enantioselectivity of Novozym 435 was not found, the results were still significant because an MBH reaction using lipase as biocatalyst was realized for the first time.


Assuntos
Lipase/metabolismo , Aldeídos/química , Aldeídos/metabolismo , Amidas/química , Amidas/metabolismo , Biocatálise , Ciclodextrinas/química , Ciclodextrinas/metabolismo , Enzimas Imobilizadas/metabolismo , Modelos Biológicos , Niacinamida/química , Niacinamida/metabolismo , Estereoisomerismo , Especificidade por Substrato
12.
J Microbiol Biotechnol ; 26(1): 80-8, 2016 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-26437947

RESUMO

The enzyme-catalyzed Henry reaction was realized using deep eutectic solvents (DESs) as a reaction medium. The lipase from Aspergillus niger (lipase AS) showed excellent catalytic activity toward the substrates aromatic aldehydes and nitromethane in choline chloride:glycerol at a molar ratio of 1:2. Addition of 30 vol% water to DES further improved the lipase activity and inhibited DES-catalyzed transformation. A final yield of 92.2% for the lipase AS-catalyzed Henry reaction was achieved under optimized reaction conditions in only 4 h. In addition, the lipase AS activity was improved by approximately 3-fold in a DES-water mixture compared with that in pure water, which produced a final yield of only 33.4%. Structural studies with fluorescence spectroscopy showed that the established strong hydrogen bonds between DES and water may be the main driving force that affects the spatial conformation of the enzyme, leading to a change in lipase activity. The methodology was also extended to the aza-Henry reaction, which easily occurred in contrast to that in pure water. The enantioselectivity of both Henry and aza-Henry reactions was not found. However, the results are still remarkable, as we report the first use of DES as a reaction medium in a lipase-catalyzed Henry reaction.


Assuntos
Aspergillus niger/enzimologia , Colina/química , Proteínas Fúngicas/química , Lipase/química , Aspergillus niger/química , Biocatálise , Isomerismo , Solventes/química
13.
J Biotechnol ; 168(4): 552-9, 2013 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-24056082

RESUMO

In this study, a new method was developed to prepare enantiopure caffeic acid amides by enzyme-catalyzed asymmetric aminolysis reaction. Methoxymethyl chloride (MOMCl) was first introduced as a protective and esterified reagent to obtain the MOM-protected caffeic acid MOM ester 1d. Aminolysis reaction occurred between 1d and (R, S)-α-phenylethylamine in the presence of an immobilized lipase (Novozym 435) from Candida antarctica. Compared with the methyl-protected caffeic acid methyl ester 1c, 1d as substrate improved the lipase-catalyzed reaction rate by 5.5-fold. After Novozym 435-catalyzed aminolysis reaction was established, we evaluated the effects of synthesis parameters on the catalytic activity and enantioselectivity of Novozym 435. A reaction conversion rate of 25.5% and an E value of >100 were achieved under the following optimum conditions: reaction solvent, anhydrous isooctane; reaction temperature, 70°C; reaction time, 24h; ester-to-amine substrate molar ratio, 1:40; and enzyme additive amount, 40 mg. Kinetic and thermodynamic analyses were conducted to determine the main factors affecting enantiomeric discrimination. Novozym 435 still showed 80% of its initial activity after recycling five times. Highly optically pure caffeic acid amides with an enantiomeric excess of 98.5% were finally obtained by HCl deprotection. The established enzyme-catalyzed asymmetric aminolysis method in this study might be used to prepare other caffeic acid amides.


Assuntos
Amidas/síntese química , Biocatálise , Ácidos Cafeicos/química , Ácidos Cafeicos/síntese química , Enzimas Imobilizadas/química , Proteínas Fúngicas/química , Proteínas Fúngicas/metabolismo , Íons/química , Cinética , Lipase/química , Lipase/metabolismo , Solventes/química , Temperatura
14.
J Mol Model ; 18(8): 3783-92, 2012 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-22395649

RESUMO

Acetyl-coenzyme A carboxylase (ACCase) has been identified as one of the most important targets of herbicide Aryloxyphenoxypropionates (APPs). ACCase shows different enantioselectivity toward APPs, and only (R)-enantiomers of APPs have the herbicidal activity. In order to deeply understand the enantioselective recognition mechanism of ACCase, (R)-haloxyfop, which is a typical commercial herbicide from APPs, is selected and the relative binding free energy between ACCase and (R)-haloxyfop is investigated and compared with that between ACCase and (S)-haloxyfop by homology modeling and molecular mechanics-Poisson-Boltzmann surface area (MM-PBSA) method. Further free energy analysis reveals that the preference of ACCase toward (R)-haloxyfop is mainly driven by Van der Waals interaction. The analysis of the interaction between the active site residues of ACCase CT domain and (R)-haloxyfop shows the van der Waals interactions have a close relationship with the addition effect of each residue. An understanding of the enantioselective recognition mechanism between ACCase and haloxyfop is desirable to discover novel chiral herbicides.


Assuntos
Acetil-CoA Carboxilase/química , Herbicidas/química , Simulação de Dinâmica Molecular , Proteínas de Plantas/química , Piridinas/química , Acetil-CoA Carboxilase/antagonistas & inibidores , Sequência de Aminoácidos , Sequência Conservada , Ligação de Hidrogênio , Dados de Sequência Molecular , Poaceae/enzimologia , Distribuição de Poisson , Estrutura Terciária de Proteína , Estereoisomerismo , Homologia Estrutural de Proteína , Termodinâmica
15.
Biochem Biophys Res Commun ; 372(4): 650-5, 2008 Aug 08.
Artigo em Inglês | MEDLINE | ID: mdl-18510948

RESUMO

Lipases were adsorbed in siliceous mesocellular foams containing different amounts of residual template in the nanopores. It is found that the hydrolytic activities of the adsorbed lipases are increased with increasing the contents of template in the mesopores. The triacetin hydrolytic activity of the lipase adsorbed in the foam containing 46% of template can be 13 times higher than that of the lipase adsorbed in the foam without template in the nanopores, and its specific activity is about three times higher than that of the free lipase, showing the hyperactivation effect on lipase resulting from the interaction between the lipase and the surfactant in the nanopores. The immobilized lipase cross-linked with glutaraldehyde can retain up to 88% of its original activity after six hydrolysis reaction test. This work provides a new strategy to enhance the activity of immobilized lipase in mesoporous materials.


Assuntos
Proteínas de Bactérias/química , Burkholderia cepacia/enzimologia , Enzimas Imobilizadas/química , Lipase/química , Nanoestruturas/química , Nanotecnologia/métodos , Catálise , Hidrólise , Porosidade
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