Hint yağı bitkisi (Ricinus communis L.) tohum yağından enzimatik yöntemle risinoleik asit üretimi
Küçük Resim Yok
Tarih
2004
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Trakya Üniversitesi
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
ÖZET Hint yağı; Euphorbiaceae familyasının Ricinnus communis türü olan hint yağı bitkisi tohumlarından elde edilen doğal bir yağdır. Hint yağırım trigliseridleri içinde, gliserol yaklaşık olarak % 90 oranında risinoleik asit ile esterleşmiştir. Bu çalışmanın amacı; Hint yağından doğal katalizörler olan spesifik enzimlerle hidroliz yoluyla, sağlığa zararlı atık içermeyecek şekilde, risinoleik asidin elde edilmesidir. Hint yağından enzimatik hidroliz yoluyla risinoleik asit üretimi için reaksiyon koşullan, hayvansal sığır pankreatik lipazı, mikrobiyal Candida rugosa lipazı ve bitkisel hint yağı lipazı biyokatalizör olarak kullanılarak belirlendi. Bu üç serbest enzimle titrasyon metoduyla hint yağının hidroliz denemeleri yapıldı ve yüzey aktif maddenin enzim cinsine bağlı olarak hidrolize etkisi gösterildi. Ayrıca, hint yağının bazik hidrolizi de gerçekleştirilerek enzimatik hidroliz sonuçlarıyla karşılaştırıldı. Risinoleik asidin daha ekonomik olarak elde edilmesi amacıyla enzimler inorganik inert bir destek olan Celit'e immobilize edildi. Her immobilizasyondan sonra Lowry metoduyla protein tayinleri yapıldı ve immobilizasyon yüzdeleri sırasıyla % 95.4, 95.3, 94.1 olarak belirlendi, immobilize enzimlerle hint yağının hidroliz reaksiyonları katalizlendi ve sonuçlar immobilize ve serbest enzimlerle karşılaştırıldı. Denemeler sonucunda en aktif olan immobilize sığır pankreatik lipazı için katalitik karakterizasyon çalışmaları gerçekleştirildi. Deneysel çalışmalar; sıcaklık, pH, reaksiyon zamanı ve enzim substrat oram değiştirilerek gerçekleştirildi. Maksimum aktivite pH: 8'de, 50 °C sıcaklıkta, 10 mg enzim içeren destek ile, 15 dk. reaksiyon süresinde gözlendi. Aynı immobilize enzimle hint yağı substraüna karşı hidrolizin kinetik sabitleri Km: 6.49 10"5 M, Vmax: 17.4 olarak hesaplandı.
II SUMMARY Castor oil is a natural oil which is derived from the bean of the castor oil plant, Ricinnus communis of the family Euphorbiaceae. hi the triglycerides of castor oil, glycerol is esterified at approximately the 90 % level by ricinoleic acid. The aim of this study is to obtain ricinoleic acid from castor oil with the spesific enyzmes, which is natural catalysts, by hydrolysis reactions that is not included the waste for human healthy. Reaction conditions for the obtain of ricinoleic acid with enzyme-catalyzed hydrolysis of c astor o il u sing b ovine p ancreatic 1 ipase d erived from animals ( PL), microbial Candida rugosa (CR) and castor bean lipase derived from Castor bean seeds (CBL) as biocatalysts have been determined. The hydrolysis of castor oil were carried out with these three free enyzmes by titration method and investigated the effect of surface active reagent on hydrolysis according to enyzme types. Furthermore, the alkaline based hydrolysis of castor oil were determined with NaOH solution and compared with results of enzyme-catalyzed hydrolysis. The free enzymes (PL, CR, CBL) were immobilized on Celit as a stable inorganic support in order to produce ricinoleic acid more economically. Following each immobilization, the protein assay was determined and the percentage immobilization for PL, CR and CBL were determinated as 95.4, 95.3 and 94.1 %, respectively. The hydrolysis reaction of castor oil was catalyzed with immobilized enzymes and the results were compared with each other and free forms. The catalytic characterization assays of immobilized pancreatic lipase that is found as the most effective lipase, was performed. The experimental studies were performed in which various temperature, pH, reaction time and the ratio of enzyme to substrates. The maximum activity was obtained at pH 8, 50 °C with support that contained 10 mg of immobilized enzyme-protein for 15 minutes. The kinetic constants; Km and Vmax values were calculated as 6.49 10"5M and 17.4, respectively, using castor oil as a substrate by immobilized porcine pancreatic lipase in immobilized conditions.
II SUMMARY Castor oil is a natural oil which is derived from the bean of the castor oil plant, Ricinnus communis of the family Euphorbiaceae. hi the triglycerides of castor oil, glycerol is esterified at approximately the 90 % level by ricinoleic acid. The aim of this study is to obtain ricinoleic acid from castor oil with the spesific enyzmes, which is natural catalysts, by hydrolysis reactions that is not included the waste for human healthy. Reaction conditions for the obtain of ricinoleic acid with enzyme-catalyzed hydrolysis of c astor o il u sing b ovine p ancreatic 1 ipase d erived from animals ( PL), microbial Candida rugosa (CR) and castor bean lipase derived from Castor bean seeds (CBL) as biocatalysts have been determined. The hydrolysis of castor oil were carried out with these three free enyzmes by titration method and investigated the effect of surface active reagent on hydrolysis according to enyzme types. Furthermore, the alkaline based hydrolysis of castor oil were determined with NaOH solution and compared with results of enzyme-catalyzed hydrolysis. The free enzymes (PL, CR, CBL) were immobilized on Celit as a stable inorganic support in order to produce ricinoleic acid more economically. Following each immobilization, the protein assay was determined and the percentage immobilization for PL, CR and CBL were determinated as 95.4, 95.3 and 94.1 %, respectively. The hydrolysis reaction of castor oil was catalyzed with immobilized enzymes and the results were compared with each other and free forms. The catalytic characterization assays of immobilized pancreatic lipase that is found as the most effective lipase, was performed. The experimental studies were performed in which various temperature, pH, reaction time and the ratio of enzyme to substrates. The maximum activity was obtained at pH 8, 50 °C with support that contained 10 mg of immobilized enzyme-protein for 15 minutes. The kinetic constants; Km and Vmax values were calculated as 6.49 10"5M and 17.4, respectively, using castor oil as a substrate by immobilized porcine pancreatic lipase in immobilized conditions.
Açıklama
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Yüksek Lisans
Yüksek Lisans
Anahtar Kelimeler
Kimya, Chemistry
