共查询到20条相似文献,搜索用时 15 毫秒
1.
Dasciana S. Rodrigues George P. Cavalcante Giovanilton F. Silva Andrea L. O. Ferreira Luciana R. B. Gonçalves 《World journal of microbiology & biotechnology》2008,24(6):833-839
In this work, the stabilizing effect of bovine serum albumin (BSA), peptone (PEP), and polyethylene glycol (PEG) during immobilization
of Candida antarctica lipase on activated carbon was investigated. The influence of enzyme concentration and type of additive, added during the
immobilization procedure, was studied using a 22 factorial central composite design. The goal was to maximize the synthetic activity of butyl butyrate, using butyric acid
and butanol as substrate in n-heptane. An increase of 31–58% in the esterification activity was obtained when enzyme concentration on the supernatant was
enhanced from 86.50 U m L−1 to 226.80 U mL−1. An enhancement in esterification activity of 38–68.95% was observed, depending on the initial enzyme concentration, when
PEP was used instead of BSA. No significant increase in the esterification activity was observed when PEP was replaced by
PEG. However, thermal stability tests at 50 °C showed that PEG had a higher stabilizing effect. 相似文献
2.
Dolores Reyes Duarte Edmundo Castillo Eduardo Bárzana Agustín López-Munguía 《Biotechnology letters》2000,22(22):1811-1814
Capsaicin was hydrolysed by lipase B from Candida antarctica into vanillylamine and 8-methyl-6-trans-nonenoic acid. Conversions of 70% were obtained after 72 h at 70 °C in water but decreased to only 15% when capsaicin was solubilized in 15% (v/v) ethanol/water after 72 h at 45 °C. No activity occurred in chloroform/water mixtures. According to our knowledge, this is the first report concerning amide hydrolysis by a lipase. 相似文献
3.
Gerardo Valerio-Alfaro Hugo S. García Héctor Luna Raymundo Cruz Almanza 《Biotechnology letters》2000,22(7):575-578
Candida antarctica lipase catalyzed the aminolysis of 2-hydroxy esters with amines in organic solvents to yield the corresponding 2-hydroxy amides. The reactions proceeded at 28–30 °C in dioxane for 6 h with 3 mM substrates with yields ranging between 45% (w/w) (for branched substrates) to 88% (w/w) (for linear substrates). Although the reaction was not enantioselective, because of its simplicity it represents an alternative method for the synthesis of functionalised amides. 相似文献
4.
Of nine commercially available lipases, lipase SP 435 from Candida antarctica, showed moderate enantioselectivity (E=17) for acetylation of racemic 3,3,3-trifluoro-2-phenylpropane-1,2-diol, 2, with vinyl acetate in diisopropyl ether (S selectivity). The other eight had low selectivities, with E values below 10. The selectivity and reactivity of SP 435 for 2 was markedly improved in dichloroethane (E=41). Moreover, SP 435 had moderate to high selectivity for the related compounds 3,3,3-trifluoro-2-(1-naphthyl)-propane-1,2-diol, 4, (E=20), 3,3,3-trifluoro-2-(indol-3-yl)propane-1,2-diol, 6, (E=80), and 3,3,3-trifluoro-2-(pyrrol-2-yl)-propane-1,2-diol, 8, (E=17). 相似文献
5.
1-Pentyl, 1-hexyl and 1-heptyl ferulates were continuously synthesized at 60–90°C using a reactor system in which a column packed with ferulic acid powders and another column packed with immobilized Candida antarctica lipase particles were connected in series. Conversions greater than 0.9 were achieved for the synthesis of the 1-hexyl and 1-heptyl ferulates at 90°C. The system could be stably operated for the 1-heptyl ferulate synthesis at 90°C for at least two weeks. 相似文献
6.
The mechanism of solvent effect on the positional selectivity of Candida antarctica lipase B during 1,3-diolein synthesis by esterification 总被引:1,自引:0,他引:1
We investigated the influence of solvent on the positional selectivity of Novozym 435 which was the immobilized Candida antarctica lipase B (CALB) during the esterification of oleic acid with glycerol for 1,3-diolein preparation previously. Herein, molecular modeling was used to elucidate the underlying mechanism of the solvent effect on the positional selectivity of the enzyme. The results showed that the binding energy of sn-1 hydroxyl of glycerol molecular with CALB became higher, and the binding energy of sn-2 hydroxyl of glycerol molecular with CALB became lower along with the increase of the solvent log P. It was demonstrated that, increasing log P of the solvent, the enzyme selectivity to sn-1 hydroxyl of glycerol molecular grew weaker, and the selectivity to sn-2 hydroxyl of glycerol molecular grew stronger. 相似文献
7.
Wencheng Li Bo Yang Yonghua Wang Dongqing Wei Chris Whiteley Xiaoning Wang 《Journal of Molecular Catalysis .B, Enzymatic》2009,57(1-4):299-303
Molecular modeling was used to clarify the mechanism of the selectivity of Candida antarctica lipase B and Candida rugosa lipase towards cis9, trans11 (c9, t11-) and trans10, cis12 (t10, c12-) conjugated linoleic acid. Hydrogen bonds network, substrate conformation, binding affinity and water molecules in the binding site were analyzed. Substrate conformation and binding affinity were not correlated with the experimental results of the substrate selectivity. On the contrary, better enzyme preference towards a substrate was correlated with two stronger hydrogen bonds (His-NH-Oa and His-NH-Ser-Oγ) and less water molecules between the substrate the binding pocket. Possible explanation of these was discussed. 相似文献
8.
A process was optimized for the enzymatic synthesis of glyceryl ferulate with a yield of up to 96% using a vacuum-rotary evaporation
strategy under following conditions: 15 mmol glycerol, 1.5 mmol ethyl ferulate, 170 mg Candida antarctica lipase, at 60°C for 10 h and under a vacuum of 10 mm Hg. The immobilized lipase can be used 10 times. 相似文献
9.
A single-step acylation of rutin and naringin, catalyzed by immobilized Candida antarctica lipase B in 2-methyl-2-butanol, occurred preferentially on the primary hydroxyl group. Using palmitic methyl ester as acyl donor, the acylation rate of naringin was 10-fold higher than that of rutin. Under optimal conditions, i.e. a molar ratio acyl donor/naringin of 7:1 and 200 mbar, 92% naringin was acylated. 相似文献
10.
Tanino T Ohno T Aoki T Fukuda H Kondo A 《Applied microbiology and biotechnology》2007,75(6):1319-1325
We isolated the lipase B from Candida antarctica CBS 6678 (CALB CBS6678) and successfully constructed CALB-displaying yeast whole-cell biocatalysts using the Flo1p short
(FS) anchor system. For the display of CALB on a yeast cell surface, the newly isolated CALB CBS6678 exhibited higher hydrolytic
and ester synthesis activities than the well-known CALB, which is registered in GenBank (Z30645). A protease accessibility
assay using papain as a protease showed that a large part of CALB, approximately 75%, was localized on an easily accessible
part of the yeast cell surface. A comparison of the lipase hydrolytic activities of yeast whole cells displaying only mature
CALB (CALB) and those displaying mature CALB with a Pro region (ProCALB) revealed that mature CALB is preferable for yeast
cell surface display using the Flo1p anchor system. Lyophilized yeast whole cells displaying CALB were applied to an ester
synthesis reaction at 60°C using adipic acid and n-butanol as substrates. The amount of dibutyl adipate (DBA) produced increased with the reaction time until 144 h. This indicated
that CALB displayed on the yeast cell surface retained activity under the reaction conditions. 相似文献
11.
Rafael C. Rodrigues Cesar A. Godoy Giandra Volpato Marco A.Z. Ayub Roberto Fernandez-Lafuente Jose M. Guisan 《Process Biochemistry》2009,44(9):963-968
This paper describes the immobilization and stabilization of the lipase from Thermomyces lanuginosus (TLL) on glyoxyl agarose. Enzymes attach to this support only by the reaction between several aldehyde groups of the support and several Lys residues on the external surface of the enzyme molecules at pH 10. However, this standard immobilization procedure is unsuitable for TLL lipase due to the low stability of TLL at pH 10 and its low content on Lys groups that makes that the immobilization process was quite slow. The chemical amination of TLL, after reversible immobilization on hydrophobic supports, has been shown to be a simple and efficient way to improve the multipoint covalent attachment of this enzyme. The modification enriches the enzyme surface in primary amino groups with low pKb, thus allowing the immobilization of the enzyme at lower pH values. The aminated enzyme was rapidly immobilized at pH 9 and 10, with activities recovery of approximately 70%. The immobilization of the chemically modified enzyme improved its stability by 5-fold when compared to the non-modified enzyme during thermal inactivation and by hundreds of times when the enzyme was inactivated in the presence of organic solvents, being both glyoxyl preparations more stable than the enzyme immobilized on bromocyanogen. 相似文献
12.
Mohd. Basyaruddin Abdul Rahman Noor Mona Md Yunus Mohd Zobir Hussein Raja Noor Zaliha Raja Abdul Rahman Abu Bakar Salleh Mahiran Basri 《Biocatalysis and Biotransformation》2013,31(3-4):233-239
Ni/Al-layered double hydroxides (Ni-LDHs) and Ni/Al-sodium dodecyl sulfonate layered double hydroxide nanocomposites (Ni-SDS-LDHs) with a molar ratio of Ni:Al (4:1) have been prepared by a co-precipitation (or salt-base) method. Their structures were determined using Powder X-Ray Diffractometer (PXRD) and the spectra showed that basal spacings for Ni-LDHs and Ni-SDS-LDHs synthesised were around 8.1?Å and 34.8?Å, respectively. Lipase from Candida rugosa was immobilised onto these advanced materials, by physical adsorption. The activity of immobilised lipase was investigated through esterification of palmitic acid and isopropyl alcohol in hexane. The effects of reaction temperature, thermostability, stability in organic solvent, operational stability, leaching and storage studies of the immobilised lipase were investigated. These biocatalysts exhibited higher activities than the native lipase with an optimum temperature of 40°C. Immobilised lipases showed higher storage stability than native lipase (up to 60 days) and during operational studies at 30°C for 5?h, more than 50% of its activity was retained. Leaching studies showed that physical adsorption is suitable for the attachment of enzymes onto LDHs. 相似文献
13.
Novel chitosan membranes as support for lipases immobilization: Characterization aspects 总被引:1,自引:0,他引:1
C.E. Orrego N. Salgado J.S. Valencia G.I. Giraldo O.H. Giraldo C.A. Cardona 《Carbohydrate polymers》2010,79(1):9-16
Membranes of chitosan (QS), chitosan treated with glutaraldehyde (QGA) and chitosan crown ether (QCE) were utilized as carriers for immobilization of Candida antarctica and Candida rugosa lipases. Membrane supports were characterized by several techniques (Raman spectroscopy, elemental analysis by CHN determination and Energy Dispersive X-ray (EDX), water sorption isotherms, and surface area from nitrogen sorption data). To verify the presence of enzymes, some of these techniques were also used for lipase on chitosan biocatalytic systems. Measurements of protein load from Biuret assays and catalytic activity in esterification in nonaqueous media were also made for the immobilized enzymes. Sorption isotherms at 20, 30, 40 and 50 °C for QS, QGA and QCE supports were fitted to the Guggenheim, Anderson and Böer model. GAB monolayer moisture parameter, Xm, varied between 0.029 and 0.051 for QS, 0.039 and 0.058 for QGA and 0.039–0.075 g of water g−1 s.s. for QCE membranes. Elemental analysis and Raman spectra measurements of the lipase, supports and immobilized lipase systems gave evidence of the presence of enzymes on supports. Chitosan supports with internal surface area (m2 g−1) among 3.31 and 1.26 were obtained. Regardless of these low values, acceptable protein load (0.61 to 3.21%) and esterification initial rates were achieved (0.88–2.75 mmol min−1 g of protein−1). 相似文献
14.
Modified Candida rugosa and Pseudomonas cepacia lipase (CRL and PCL) were co-lyophilized with two pairs of synthetic diastereoisomeric amphiphiles, d- and l-2-(2,3,4,5,6-pentahydroxy-hexanoylamino)-propyl]-carbamoyl-propionylamino)-pentanedioic acid didodecyl ester (d- and l-BIG2C12CA); d- and l-2-(2,3,4,5,6-pentahydroxy-hexanoylamino)-pentanedioic acid didodecyl ester (d- and l-2C12GE). Enzyme activities of the modified lipase in the transesterification in organic solvent were evaluated. Both pairs of the diastereoisomeric amphiphiles showed enhanced enzyme activity in the transacetylation between racemic sulcatol and isopropenyl acetate in diisopropyl ether, catalyzed by the PCL-co-lyophilizate, by 19–48 fold when compared to the native lipase lyophilized from buffer alone independent of the stereochemistry of the amphiphiles, while in the case of the CRL-co-lyophilizate only the l-BIG2C12CA showed enhanced enzyme activity in the transbutyrylation between racemic solketal and vinyl butyrate in cyclohexane as high as 68–78 fold. 相似文献
15.
Kimitoshi Fukunaga Yurie Mine Ken-ichi Samejima Makoto Yoshimoto Katsumi Nakao Yoshiaki Sugimura 《Biotechnology letters》2002,24(14):1157-1160
Modified Candida rugosa lipase was co-lyophilized with two gemini-type amphiphiles, l- and d-2-(3-bis-[3-(2,3,4,5,6-pentahydroxy-hexanoylamino)-propyl]-carbamoyl -propionylamino)-pentanedioic acid didodecyl ester or dodecanoic acid 2-[(3-bis-[3-(2,3,4,5,6-pentahydroxy-hexanoylamino)-propyl]-carbamoyl -propionyl)-(2-dodecanoyloxy-ethyl)-amino]-ethyl ester. Enzymatic activities of the modified lipases in the transesterification between racemic 2,2-dimethyl-1,3-dioxolane-4-methanol and vinyl butyrate in cyclohexane were enhanced as much as by 37-78, 1.5–5- and 41–83-fold of magnitude relative to that of native enzyme, respectively. The lack of significant enhancement of the enzymatic activity, only in the case of the d-isomeric amphiphile-modified lipase, was considered from the topological view of the amphiphile. 相似文献
16.
H.W. Yu H. Chen X. Wang Y.Y. Yang C.B. Ching 《Journal of Molecular Catalysis .B, Enzymatic》2006,43(1-4):124
Aggregation agent type and concentration, lipase and glutaraldehyde concentration, and pH are able to affect the formation of cross-linked lipase. The carrier-free immobilized Candida rugosa lipase with a particle size of 40–50 μm showed higher activity than that of the lipase with other particle sizes. The carrier-free immobilized C. rugosa lipase can keep 86% original lipase activity (0.018 g g−1 min−1). The enantioselectivity of the carrier-free immobilized lipase (23.3) was about 1.8 times as much as that of the native lipase (13.0) in kinetic resolution of ibuprofen racemic mixture. 相似文献
17.
Enhanced activity and enantioselectivity of Candida rugosa lipase immobilized on macroporous adsorptive resins for ibuprofen resolution 总被引:2,自引:0,他引:2
The lipase from Candida rugosa was immobilized on three commercially available macroporous adsorptive resins for kinetic resolution of ibuprofen. One resin, CRB02, increased the enzyme activity by 50% to 0.027 g g(-1) min(-1). The deactivation constant (0.19 h(-1)) of the immobilized enzyme was half of that of the native enzyme and the enantioselectivity (E = 29.2) of the immobilized lipase was 2.2 times as much as that of the native lipase for the kinetic resolution of ibuprofen with 1-propanol in isooctane at 30 degrees C. 相似文献
18.
The derivatives of polyethylene glycol (PEG) were prepared by reacting PEG with propylene oxide to enhance its hydrophobicity and introduce a branched structure. The PEG derivatives were activated with cyanuric chloride and used to modify the lipase fromCandida rugosa. The maximum specific activity of lipase modified with the PEG derivatives was about 2-fold of that modified with PEG for the esterification of oleic acid and lauryl alcohol in hexane. 相似文献
19.
Kato M Fuchimoto J Tanino T Kondo A Fukuda H Ueda M 《Applied microbiology and biotechnology》2007,75(3):549-555
To prepare a whole-cell biocatalyst of a stable lipase at a low price, mutated Candida antarctica lipase B (mCALB) constructed on the basis of the primary sequences of CALBs from C. antarctica CBS 6678 strain and from C. antarctica LF 058 strain was displayed on a yeast cell surface by α-agglutinin as the anchor protein for easy handling and stability
of the enzyme. When mCALB was displayed on the yeast cell surface, it showed a preference for short chain fatty acids, an
advantage for producing flavors; although when Rhizopus oryzae lipase (ROL) was displayed, the substrate specificity was for middle chain lengths. When the thermal stability of mCALB on
the cell surface was compared with that of ROL on a cell surface, T
1/2, the temperature required to give a residual activity of 50% for heat treatment of 30 min, was 60°C for mCALB and 44°C for
ROL indicating that mCALB displayed on cell surface has a higher thermal stability. Furthermore, the activity of the displayed
mCALB against p-nitrophenyl butyrate was 25-fold higher than that of soluble CALB, as reported previously. These findings suggest that mCALB-displaying
yeast is more practical for industrial use as the whole-cell biocatalyst. 相似文献
20.
Nemanja Mileti Zorica Vukovi Aleksandra Nastasovi Katja Loos 《Journal of Molecular Catalysis .B, Enzymatic》2009,56(4):196-201
Crosslinked macroporous hydrophilic poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate)s [abbreviated poly(GMA-co-EGDMA)] with identical chemical structure (60% of glycidyl methacrylate) but with varied average pore sizes (from 30 to 560 nm), specific surface areas (from 13.2 to 106.0 m2/g), specific volumes (from 0.755 to 1.191 cm3/g) and particle sizes (less than 100–650 μm) were synthesized via suspension polymerization. The influence of the resin properties on the loading of Candida antarctica lipase B (Cal-B) during immobilization and on the hydrolytic (hydrolysis of para-nitrophenyl acetate) and synthetic (ring-opening polymerization of -caprolactone) activity of the immobilized Cal-B were studied. Immobilization of Cal-B was performed at different temperatures and pH values. Cal-B immobilized at 30 °C and pH 6.8 was leading to increased activities. By decreasing the resin diameter: (i) the amount of Cal-B adsorbed onto the resin decreases, (ii) the conversion of para-nitrophenyl acetate increases (hydrolytic activity) and (iii) the conversion of -caprolactone and the molecular weight of the synthesized poly--caprolactone increases (synthetic activity). Varying the porosity parameters results in different hydrolytic and synthetic activities. Pore sizes of all synthesized resins (from 30 to 560 nm) are big enough to overcome diffusion limitations. Therefore increasing the pore size of the resins resulted in a large increase in the hydrolytic and synthetic activity. Increasing the specific surface area resulted in an increase of activities, as the result of alleviated substrate approach to the immobilized enzyme zones. The obtained results were compared to results from dried Cal-B powder and Novozyme 435. Resin with particle size less than 100 μm and pore size 48 nm had much higher hydrolytic activity than both dried Cal-B powder and Novozyme 435. Nearly similar trends were observed for the synthetic activity.Via the DMSO leaching technique we could show that about 80% of Cal-B was covalently attached to the macroporous resin. 相似文献