東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Enzyme immobilization into polymers ...

Drevon, Geraldine F.

Linked to FindBook

Google Book

Amazon

博客來

Enzyme immobilization into polymers and coatings.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Enzyme immobilization into polymers and coatings./
Author:	Drevon, Geraldine F.
Description:	245 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-05, Section: B, page: 2504.
Contained By:	Dissertation Abstracts International65-05B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3133179
ISBN:	9780496804191

Enzyme immobilization into polymers and coatings.
Drevon, Geraldine F.

Enzyme immobilization into polymers and coatings. - 245 p.

Source: Dissertation Abstracts International, Volume: 65-05, Section: B, page: 2504.

Thesis (Ph.D.)--University of Pittsburgh, 2002.

In this study, we have developed strategies to immobilize enzymes into various polymer and coatings. Three categories of bioplastic matrices were investigated. The first type of bioplastics was prepared by irreversibly incorporating di-isopropylfluorophosphatase (DFPase) into polyurethane (PU) foams. The resulting bioplastic retained up to 67% of the activity for native enzyme. The thermostability of DFPase was highly affected by the immobilization process. Unlike native enzyme, immobilized DFPase had biphasic deactivation kinetics. Our data demonstrated that the initial rapid deactivation of immobilized DFPase lead to the formation of a hyper-stable and still active form of enzyme. Spectroscopic studies enabled a structural analysis of the hyper-stable intermediate.

ISBN: 9780496804191Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Enzyme immobilization into polymers and coatings.
LDR:02910nam 2200289 4500 001 1403441
005 20111118095921.5
008 130515s2002 ||||||||||||||||| ||eng d
020 $a 9780496804191
035 $a (UMI)AAI3133179
035 $a AAI3133179
040 $a UMI $c UMI
100 1 $a Drevon, Geraldine F. $3 1682700
245 1 0 $a Enzyme immobilization into polymers and coatings.
300 $a 245 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-05, Section: B, page: 2504.
502 $a Thesis (Ph.D.)--University of Pittsburgh, 2002.
520 $a In this study, we have developed strategies to immobilize enzymes into various polymer and coatings. Three categories of bioplastic matrices were investigated. The first type of bioplastics was prepared by irreversibly incorporating di-isopropylfluorophosphatase (DFPase) into polyurethane (PU) foams. The resulting bioplastic retained up to 67% of the activity for native enzyme. The thermostability of DFPase was highly affected by the immobilization process. Unlike native enzyme, immobilized DFPase had biphasic deactivation kinetics. Our data demonstrated that the initial rapid deactivation of immobilized DFPase lead to the formation of a hyper-stable and still active form of enzyme. Spectroscopic studies enabled a structural analysis of the hyper-stable intermediate.
520 $a Biopolymers were also prepared via atom transfer radical polymerization (ATRP) using acrylic and sulfonate-derived monomers. ATRP ensured the covalent and multi-point immobilization of enzyme within polymer matrices. However, this approach was only partially successful, as no activity retention was obtained after polymerization.
520 $a Enzyme-containing PU- and Michael adduct (MA)-based coatings correspond to the last category of bioplastics that was investigated. DFPase was irreversibly incorporated into PU coatings. The distribution of immobilized DFPase as well as activity retention were homogeneous within the coating. The resulting enzyme-containing coating (ECC) film hydrolyzed DFP in buffered media at high rates retaining approximately 39% intrinsic activity. DFPase-ECC had a biphasic deactivation profile similar to that of bioplastic foams. The synthesis of enzyme-containing MA coatings was performed in a two-step process using carbonic anhydrase (CA, E.C. 4.2.1.1). CA was first covalently immobilized into NVF-based water-soluble polymer (EP). The resulting EP was further entrapped into the matrix of MA coating. The so-formed ECC's exhibited approximately 7% apparent activity. CA-ECC showed good stability under ambient conditions and retained 55% activity after 90 days of storage.
590 $a School code: 0178.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Chemistry, Polymer. $3 1018428
650 4 $a Engineering, Chemical. $3 1018531
690 $a 0487
690 $a 0495
690 $a 0542
710 2 $a University of Pittsburgh. $3 958527
773 0 $t Dissertation Abstracts International $g 65-05B.
790 $a 0178
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3133179