Bovine Serum Albümin (bsa)’in Adsorpsiyon Kinetiğine Ko-solventlerin Etkisi
Bovine Serum Albümin (bsa)’in Adsorpsiyon Kinetiğine Ko-solventlerin Etkisi
Dosyalar
Tarih
Yazarlar
Güzey, Demet
Süreli Yayın başlığı
Süreli Yayın ISSN
Cilt Başlığı
Yayınevi
Fen Bilimleri Enstitüsü
Institute of Science and Technology
Institute of Science and Technology
Özet
Ko-solventlerin (glukoz, fructoz ve sucroz) %0 ile 40 arasında değişen derişimlerde bovine serum albumin (BSA)’in hava-çözelti arayüzeyinde 20oC sıcaklıktaki adsorpsiyon kinetiğine etkisi incelenmiştir. Zamana bağlı yüzey gerilimindeki değişim damla şekli analizi tensiometresi kulanılanarak ölçülmüştür. Ward and Tordai’nin genel adsorpsiyon modelinin proteinin adsorpsiyonun baslangıç kısmına uygulanmasıyla elde edilen difüzyon katsayıları % 40 sukroz varlığında saf su çözeltisindeki değerinden yaklaşık 1000 kat az olarak bulunmustur. % 10 un altındaki sukroz derişimlerinde adsorpsiyon hızındaki bağıl azalışın yüksek derişimlerdekine kıyasla belirgin derecede fazla olduğu bulunmuştur. Sonuçlar çözelti vizkozitesindeki artış nedeniyle protein moleküllerinin hareketliliğinin azalması ve şeker molekülleri ile protein moleküllerinin seçici etkileşimine bağlı olarak tartışılmaktadır. Şeker moleküllerinin protein molekülerinin yüzeyinden seçici olarak uzaklaştırılmaları ile BSA moleküllerinin stabilizasyonunun sağlandığı ve bu nedenle BSA’nin hava-çözelti arayüzeyine difüzyonun azaldığı düşünülmektedir.
The influence of co-solvents glucose, sucrose and fructose at concentrations ranging from 0 to 40 wt% on the adsorption kinetics of bovine serum albumin (BSA) at air-aqueous solution interfaces at 20oC was measured. The change in surface tension with time was recorded using drop shape analysis tensiometer. Diffusion coefficients were calculated from the initial period of protein adsorption using the short term solution of the general adsorption model by Ward and Tordai. Diffusion coefficients calculated for BSA in the presence of 40 wt% sucrose were nearly three orders of magnitude smaller than values obtained for BSA dissolved in pure water. The relative decrease of the adsorption rate was significantly higher at sugar concentrations lower than 10 wt%. Results were attributed to an increase in solution viscosity reducing the molecular mobility of the protein molecules and preferential interactions of sugars with the protein surface, which contributes to a stabilization of the native non-absorbed state of BSA.
The influence of co-solvents glucose, sucrose and fructose at concentrations ranging from 0 to 40 wt% on the adsorption kinetics of bovine serum albumin (BSA) at air-aqueous solution interfaces at 20oC was measured. The change in surface tension with time was recorded using drop shape analysis tensiometer. Diffusion coefficients were calculated from the initial period of protein adsorption using the short term solution of the general adsorption model by Ward and Tordai. Diffusion coefficients calculated for BSA in the presence of 40 wt% sucrose were nearly three orders of magnitude smaller than values obtained for BSA dissolved in pure water. The relative decrease of the adsorption rate was significantly higher at sugar concentrations lower than 10 wt%. Results were attributed to an increase in solution viscosity reducing the molecular mobility of the protein molecules and preferential interactions of sugars with the protein surface, which contributes to a stabilization of the native non-absorbed state of BSA.
Açıklama
Tez (Yüksek Lisans) -- İstanbul Teknik Üniversitesi, Fen Bilimleri Enstitüsü, 2002
Thesis (M.Sc.) -- İstanbul Technical University, Institute of Science and Technology, 2002
Thesis (M.Sc.) -- İstanbul Technical University, Institute of Science and Technology, 2002
Anahtar kelimeler
BSA,
şekerler,
adsorpsiyon,
fonksiyonel özellikler,
seçici etkileşim,
BSA, sugars, adsorption, functionality, preferential interaction