Immobilized lipase on macroporous polystyrene modified by PAMAM-dendrimer and their enzymatic hydrolysis

Hou, Chen; Zhu, Hao; Wu, Duoming; Li, Yijing; Hou, Ke; Jiang, Yu; Li, Yanfeng

doi:10.1016/j.procbio.2013.10.019

Cited by 32 publications

(16 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The first stage is between 20 and 200°C, and the second from around 800°C. The first stage corresponds to the loss of water adsorbed on the surface of the materials, while the second stage corresponds to the thermal decomposition of lipase that was adsorbed on the silica surface [37,38].…”

Section: Tg Analysismentioning

confidence: 99%

Immobilization of Amano Lipase A onto Stöber silica surface: process characterization and kinetic studies

Zdarta

Sałek

Kołodziejczak-Radzimska

et al. 2014

Open Chemistry

View full text Add to dashboard Cite

The immobilization of Amano Lipase A fromAspergillus niger by adsorption onto Stöber silica matrix obtained by sol-gel method was studied. The effectiveness of the enzyme immobilization and thus the usefulness of the method was demonstrated by a number of physicochemical analysis techniques including Fourier Transform Infrared Spectroscopy (FT-IR), elemental analysis (EA), thermogravimetric analysis (TG), porous structure of the support and the products after immobilization from the enzyme solution with various concentration at different times. The analysis of the process' kinetics allowed the determination of the sorption parameters of the support and optimization of the process. The optimum initial concentration of the enzyme solution was found to be 5 mg mL -1 , while the optimum time of the immobilization was 120 minutes. These values of the variable parameters of the process were obtained by as ensuring the immobilization of the largest possible amount of the biocatalyst at the most economically beneficial aspects of the process.

show abstract

Section: Tg Analysismentioning

confidence: 99%

Immobilization of Amano Lipase A onto Stöber silica surface: process characterization and kinetic studies

Zdarta

Sałek

Kołodziejczak-Radzimska

et al. 2014

Open Chemistry

View full text Add to dashboard Cite

show abstract

“…The adsorption of lipase into supports requires adequate interactions, most commonly hydrophobic and in some cases ionic interactions, between these components[ 19 ]. Consequently, a variety of hydrophobic supports, such as polypropylene-based supports[ 20 ] and styrene-divinylbencene resin, have been introduced as carrier candidates for lipase immobilization[ 18 ]. Novozyme 435 (Novozymes, Denmark), frequently used in food and pharmaceutical industries, is a commercial lipase preparation of Candida antarctica lipase immobilized with Lewatit, a methacrylate-styrenedivinylbenzene resin carrier.…”

Section: Introductionmentioning

confidence: 99%

Immobilization, Regiospecificity Characterization and Application of Aspergillus oryzae Lipase in the Enzymatic Synthesis of the Structured Lipid 1,3-Dioleoyl-2-Palmitoylglycerol

Cai

Zhao

et al. 2015

PLoS ONE

View full text Add to dashboard Cite

The enzymatic synthesis of 1,3-dioleoyl-2-palmitoylglycerol (OPO), one of the main components of human milk fats, has been hindered by the relatively high cost of sn-1,3-specific lipases and the deficiency in biocatalyst stability. The sn-1,3-specific lipase from Aspergillus oryzae (AOL) is highly and efficiently immobilized with the polystyrene-based hydrophobic resin D3520, with a significant 49.54-fold increase in specific lipase activity compared with the AOL powder in catalyzing the synthesis of OPO through the acidolysis between palm stearin and oleic acid (OA). The optimal immobilization conditions were investigated, including time course, initial protein concentration and solution pH. The sn-1,3 specificity of lipases under different immobilization conditions was evaluated and identified as positively associated with the lipase activity, and the pH of the immobilization solution influenced the regiospecificity and synthetic activity of these lipases. Immobilized AOL D3520, as the biocatalyst, was used for the enzymatic synthesis of the structured lipid OPO through the acidolysis between palm stearin and OA. The following conditions were optimized for the synthesis of structured lipid OPO: 65 °C temperature; 1:8 substrate molar ratio between palm stearin and OA; 8% (w/w) enzyme load; 3.5% water content of the immobilized lipase; and 1 h reaction time. Under these conditions, highly efficient C52 production (45.65%) was achieved, with a tripalmitin content of 2.75% and a sn-2 palmitic acid (PA) proportion of 55.08% in the system.

show abstract

“…Poly(hydroxymethyl methacrylate), mp(HEMA-GMA), ferrogel was grafted with polyaniline, PANI, to create a functional surface for interaction with biological macromolecules, and glucoamylase was immobilized on the PANI grafted ferrogel [14]. Polyamidoamine dendrimers modified macroporous polystyrene supports were synthesized and the porcine pancreas lipase was covalently immobilized on it [15]. Poly(methacrylic acid) was grafted on the poly(ethylene terephthalate) and poly(acylonitrile) fabrics, and used for thrombin immobilization [2].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Mucor miehei esterase on core-shell magnetic beads via adsorption and covalent binding: Application in esters synthesis

Bayramoğlu

Arıca

2014

Fibers Polym

View full text Add to dashboard Cite

In this work, poly(hydroxyethyl methacrylate/glycidylmethacrylate), p(HPMA-GMA), magnetic beads were prepared via suspension polymerization, and grafted with poly(methacrylic acid), p(MMAc) via redox polymerization. Esterase from M. miehei was immobilized onto core-shell magnetic beads with two different methods (i.e., adsorption and covalent binding). For adsorption, the effects of pH and initial esterase concentration on the immobilization efficiency via adsorption have been studied. The maximum adsorption capacity of the magnetic beads for esterase was found to be 27.6 mg/g magnetic beads at pH 7.0. The covalent immobilization of esterase via carbodiimide coupling on mp(HEMA-GMA)-gp(MAAc) beads was found to be the more effective than the direct immobilization of the enzyme on the mp(HEMA-GMA) beads. The covalently immobilized esterase on the mp(HEMA-GMA)-g-p(MAAc) beads exhibited higher activity compared to the adsorbed esterase on the same magnetic beads. Tributyrin hydrolysis properties of the free and both immobilized esterase preparations were determined under different experimental conditions. The operational, thermal and storage stabilities of the immobilized esterase preparations were increased compared with the free esterase. Finally, esterification reactions have been performed to produce citronellyl-esters (namely: acetate, butyrate and propionate) in n-hexane medium using covalently immobilized esterase. The immobilized esterase was effectively reused in successive batch runs in n-hexane medium for citronellyl-butyrate synthesis, and only 23 % activity was lost after 6 cycles.

show abstract

Immobilized lipase on macroporous polystyrene modified by PAMAM-dendrimer and their enzymatic hydrolysis

Cited by 32 publications

References 43 publications

Immobilization of Amano Lipase A onto Stöber silica surface: process characterization and kinetic studies

Immobilization of Amano Lipase A onto Stöber silica surface: process characterization and kinetic studies

Immobilization, Regiospecificity Characterization and Application of Aspergillus oryzae Lipase in the Enzymatic Synthesis of the Structured Lipid 1,3-Dioleoyl-2-Palmitoylglycerol

Immobilization of Mucor miehei esterase on core-shell magnetic beads via adsorption and covalent binding: Application in esters synthesis

Contact Info

Product

Resources

About