Lewatit partikülüne üreaz enziminin immobilizasyonu
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Dosyalar
Tarih
2017
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Batman Üniversitesi
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Ticari olarak alınan Lewatit VP OC 1600 partiküllerine üreaz enzimi immobilizasyon tekniği uygulanılarak
partiküle immobilize edildi. Enzim immobilizasyonlarında araştırma parametrelerinden biri olan enzimin tekrar
kullanılabilirliği immobilze olan partikülün kullanılması ve sonuçların alınması enzimin ticari alınan lewatit
partiküller üzerine immobilize olduğunu gösterdi. Lewatit VP OC 1600, metakrilik esterlere dayanılarak küresel
boncuk biçiminde macropor içeren ve divinilbenzen (DVB) ile çapraz bağlanmış polimerdir. Lewatit VP OC
1600’ün maksimum üreaz immobilize etme kapasitesi 480 mg.g -1
‘dir. Serbest ve immobilize olan enzimler, 7.5 ve
6.5 gibi farklı optimum pH'lar sergiledi. İmmobilize olan enzimin optimum sıcaklığı 60 oC'e kayarken, serbest
enzim 50 oC olarak belirlendi. İmmobilize olan enzim ile serbest enzim yüksek sıcaklıklara maruz bırakıldığında
tutuklanan enzim serbest enzime göre sıcaklığa daha fazla direnç gösterdiği tespit edildi. Tutuklanan ve serbest
enzimin kinetik parametreleri belirlendi. Buna göre, serbest enzimin substrata ilgisinin tutuklanan enzimin
substrata olan ilgisinden düşük olduğu gözlemlendi. Tutuklanan enzimin, termostabilitesi, tekrar kullanılabilirliği
ve depolama parametrelerinin serbest enzime kıyasla daha yüksek bir etkinlik gösterdiği tespit edildi.
Urease enzyme was intended to comercially obtained Lewatit VP OC 1600 particles by available immobilization technique. Resusability is the one of research parameters in enzym immobilization. Reusability of out enzyme and results showed that enzyme succesfully immobilized to lewatit particles. Lewatit VP OC 1600 is a macroporous, DVB(divinylbenzene) -crosslinked polymer in spherical bead form, based on methacrylic esters. The maximum urease arrest capacity of Lewatit VP OC 1600 was 480 mg.g-1 . Free and arrested enzymes exhibited different optimum pH’s such as 7.5 and 6.5. Optimum temperature of the arrested enzyme shifted to 60 oC, while free enzyme was detected as the its 50 oC. When the arrested enzyme and the free enzyme were exposed to high temperatures, it was found that the arrested enzyme showed more resistance to temperature than the free enzyme. In determining the kinetic parameters of free and arrested enzymes, we observed that the interest of free enzyme to substrat is lower than interest of arrested enzyme to substrat. The arrested enzyme was defined to have a higher activity according to thermostability, reusability and storage parameters than free enzyme.
Urease enzyme was intended to comercially obtained Lewatit VP OC 1600 particles by available immobilization technique. Resusability is the one of research parameters in enzym immobilization. Reusability of out enzyme and results showed that enzyme succesfully immobilized to lewatit particles. Lewatit VP OC 1600 is a macroporous, DVB(divinylbenzene) -crosslinked polymer in spherical bead form, based on methacrylic esters. The maximum urease arrest capacity of Lewatit VP OC 1600 was 480 mg.g-1 . Free and arrested enzymes exhibited different optimum pH’s such as 7.5 and 6.5. Optimum temperature of the arrested enzyme shifted to 60 oC, while free enzyme was detected as the its 50 oC. When the arrested enzyme and the free enzyme were exposed to high temperatures, it was found that the arrested enzyme showed more resistance to temperature than the free enzyme. In determining the kinetic parameters of free and arrested enzymes, we observed that the interest of free enzyme to substrat is lower than interest of arrested enzyme to substrat. The arrested enzyme was defined to have a higher activity according to thermostability, reusability and storage parameters than free enzyme.
Açıklama
Anahtar Kelimeler
Enzim, Üreaz, İmmobilizasyon, Enzymes, Urease, Immobilization
Kaynak
WoS Q Değeri
Scopus Q Değeri
Cilt
7
Sayı
2/2
Künye
Çınar, E., Ercan, S., Güleşçi, N. (2017). Lewatit partikülüne üreaz enziminin immobilizasyonu. Batman Üniversitesi Yaşam Bilimleri Dergisi, 7 (2/2), 124-136.
