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Enzymatic modification of natural an...
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Chakraborty, Soma.
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Enzymatic modification of natural and synthetic polymers using lipases and proteases.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Enzymatic modification of natural and synthetic polymers using lipases and proteases./
作者:
Chakraborty, Soma.
面頁冊數:
109 p.
附註:
Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4560.
Contained By:
Dissertation Abstracts International64-09B.
標題:
Engineering, Materials Science. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3104063
Enzymatic modification of natural and synthetic polymers using lipases and proteases.
Chakraborty, Soma.
Enzymatic modification of natural and synthetic polymers using lipases and proteases.
- 109 p.
Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4560.
Thesis (Ph.D.)--Polytechnic University, 2004.
Enzymatic modification of natural/synthetic polymers [starch nanoparticles, poly (n-alkyl acrylates) and poly(vinyl formamide)] was studied. Enzymes used for catalysis were lipases and proteases.Subjects--Topical Terms:
1017759
Engineering, Materials Science.
Enzymatic modification of natural and synthetic polymers using lipases and proteases.
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Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4560.
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Adviser: Richard A. Gross.
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Thesis (Ph.D.)--Polytechnic University, 2004.
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Enzymatic modification of natural/synthetic polymers [starch nanoparticles, poly (n-alkyl acrylates) and poly(vinyl formamide)] was studied. Enzymes used for catalysis were lipases and proteases.
520
$a
Starch nanoparticles (40nm diameter) were incorporated into AOT-coated reverse micelles. Reactions performed with the acylating agents vinyl stearate, ϵ-caprolactone and maleic anhydride in toluene in presence of Novozyme-435 at 40°C for 36h gave products with degrees of substitution of 0.8, 0.6 and 0.4 respectively. DEPT-135 NMR spectra revealed that the modification occurred regioselectively at the C-6 position of the glucose units. Infrared microspectroscopy showed that the surfactant coated starch nanoparticles diffuse into pores of Novozyme-435 beads, coming in close proximity with CALB to promote modification. The modified products retained nanoscale dimensions.
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Catalysis of amide bond formation between a low molar mass amine and ester side groups of poly(n-alkyl acrylates)[poly(ethyl acrylate), poly(methyl acrylate) and poly(butyl acrylate)] was also examined. The nucleophiles were mono and diamines. Among the poly(n-alkyl acrylates) and the lipases studied, poly(ethyl acrylate) was the preferred substrate and Novozyme-435 the most active lipase. Poly(ethyl acrylate) in 80% by-volume toluene was reacted with 1 equivalent per repeat unit of hexyl amine at 70°C in presence of Novozyme-435. The product contained 10.6 mol% amide groups. Attempts to increase the amidation beyond 10–11 mol% by increasing the reaction time or use of fresh enzyme were unsuccessful, showing that poly(ethylacrylate-co-10mol%hexylacrylamide) is a poor substrate for further acylation. When chiral amines ([R,S]-α-methyl benzylamine, [R,S]-β-methyl phenyl amine) were used as nucleophiles, Novozyme-435 enantioselectively catalyzed amidation of poly(ethyl acrylate).
520
$a
Poly(vinyl formamide), P(VfAm) by acid or base-catalyzed hydrolysis leads to poly(vinylamine), P(VAm), and corresponding copolymers. As an alternative to chemical hydrolysis a mild and selective enzymatic method was discovered. Fifteen proteases were evaluated for this transformation. Of these, PROT 7 was the most active. Within 24h PROT 7 gave products with 44% hydrolysis. Further hydrolysis was not observed by extending the reaction time because poly(vinylformamide-co-40%vinylamine) is a poor substrate for further hydrolysis. The sequence distribution of copolymers formed by chemical hydrolysis and enzymatic hydrolysis was compared. Chemical hydrolysis gave random copolymer. In contrast, PROT 7 gave block-like arrangement of VAm units.
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School code: 0179.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3104063
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