کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6578446 | 1422927 | 2018 | 53 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Enhancing enzyme activity and enantioselectivity of Burkholderia cepacia lipase via immobilization on melamine-glutaraldehyde dendrimer modified magnetic nanoparticles
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کلمات کلیدی
VSMBioimprintingPPLEESBclHRPPCL(3-aminopropyl) triethoxysilane - (3-آمینوپروپیل) تری ات اسی سیلان1-Phenylethanol - 1-فینیل اتانولBurkholderia cepacia lipase - Burkholderia cepacia لیپازMNPs - MNP هاPseudomonas cepacia lipase - Pseudomonas cepacia لیپازImmobilization - ایمن سازیTem - این استDendrimer - دندریمرFT-IR - طیف سنجی مادون قرمز تبدیل فوریهFourier transform infrared spectroscopy - طیف سنجی مادون قرمز تبدیل فوریه یا طیف سنجی FTIRPorcine pancreas lipase - لیپاز پانکراس گوشتیSaturation magnetization - مغناطیس اشباعAPTES - مناسبVibrating sample magnetometer - مگنتومتر نمونه ارتعاشیTransmission electron microscope - میکروسکوپ الکترونی انتقالMagnetic nanoparticles - نانوذرات مغناطیسیChiral resolution - وضوح کریلPAMAM - پامامHorseradish peroxidase - پراکسیداز هوررادیشPolyamidoamine - پلی آمیدآمینCalb - کالباسCandida antarctica lipase B - کاندیدا آنتارکتازی لیپاز B
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
مهندسی شیمی (عمومی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Enhancing enzyme activity and enantioselectivity of Burkholderia cepacia lipase via immobilization on melamine-glutaraldehyde dendrimer modified magnetic nanoparticles Enhancing enzyme activity and enantioselectivity of Burkholderia cepacia lipase via immobilization on melamine-glutaraldehyde dendrimer modified magnetic nanoparticles](/preview/png/6578446.png)
چکیده انگلیسی
Burkholderia cepacia lipase (BCL) was a potential catalyst in chiral resolution. Immobilization can be used to increase the enzyme activity and operational stability. In this work, novel melamine-glutaraldehyde dendrimer-like polymers were firstly grafted on the aminated magnetic nanoparticles to increase protein binding sites for the lipase to be immobilized. The dendrimer-polymer-modified nanoparticles could obviously protect the conformation of lipase and increase the contact chance between substrates and catalyzed center of lipase. The standard esterification reaction between lauric acid and 1-dodecanol was used to test the lipases activities. The activity of the obtained immobilized lipase was 58.0-fold than BCL powder, and 3.0-fold than the immobilized lipase without modified polymers. Then, the immobilized lipase was used to catalyze the chiral resolution reaction between 1-phenylethanol and vinyl acetate. Different organic solvents were selected for chiral resolution reaction. It was found out that hexane and heptane were the best reaction media. Thermal stability and organic solvent tolerance of the immobilized lipase were greatly improved than those of the lipase powder. The most significant discovery was the improvement in enzyme activity by bioimprinting. It could greatly shorten the reaction time from 3â¯h to 20â¯min. The conversion and substrate enantiomeric excess (ees) reached 49.7% and 98.8% in 20â¯min, respectively. The immobilized lipase could be recycled for 8 times without obvious loss in activity. The study provides a good strategy for preparation of efficient biocatalyst, showing great potential for future industrial application.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chemical Engineering Journal - Volume 351, 1 November 2018, Pages 258-268
Journal: Chemical Engineering Journal - Volume 351, 1 November 2018, Pages 258-268
نویسندگان
Kai Li, Jianhua Wang, Yaojia He, Guli Cui, Miaad Adnan Abdulrazaq, Yunjun Yan,