Sonuç olarak, elde edilen immobilize BLP’nin endüstriyel amaçlar için kullanılabileceği söylenebilir.Īnahtar Kelimeler: Eupergit CM Immobilizasyon Inek sütü Proteaz: Protein Protein alerjisi IntroductionĬow’s milk protein (CMP) allergy is the immunological reactions that occur in the body against cow’s milk proteins. Sütün pH’sı 6.89’dan 6.53’e düşerken, renginde biraz açılma oldu fakat kokusunda ve tadında herhangi bir değişiklik olmadı. İmmobilize enzim kullanılarak süt proteinleri iki saat içinde tamamen hidrolize edildi. İmmobilize enzim, tekrarlanan yirmi kullanım sırasında ve yirmi gün saklama süresinde başlangıç aktivitesini kaybetmedi. Serbest ve immobilize enzim için K m değerleri sırasıyla 26.53 ve 37.59 g/L iken, V max değerleri sırasıyla 2.84 ve 3.31 g L-Tirozin/L Optimum pH (7–8) ve optimum sıcaklık (70☌) immobilizasyon sonrasında değişmemiştir. İmmobilizasyon % 100 immobilizasyon verimi ve % 107.7 aktivite verimi ile sonuçlandı.
Proteinler ve L-tirozin, UV/VIS spektrofotometre ile tayin edildi. İmmobilizasyon için optimum koşullar, şartlar ayrı ayrı değiştirilerek belirlendi. İmmobilize enzimler, tekrarlanan reaksiyonlarda kullanılamadığı ve kullanım şartlarında kararlı olmadığı ve endüstriyel sürekli süreçler için uygun olmadığından, bu çalışma, BLP’nin Eupergit CM’ye kovalent immobilizasyonunu amaçlamıştır. ConclusionĬonsequently, it can be said that the immobilized BLP obtained can be used for industrial purposes. The pH of the milk dropped from 6.89 to 6.53, the color was clearer but there was no change in the smell or the taste. The milk proteins were hydrolyzed in 2 h by using immobilized enzyme. The immobilized enzyme has not lost its initial activity during the repeated 20 uses and 20 days of storage.
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The K m values for free and immobilized enzyme were 26.53 and 37.59 g/L, while the V max values were 2.84 and 3.31 g L-Tyrosine/L The optimum pH (7–8) and the optimum temperature (70☌) have not changed after immobilization. The immobilization resulted in 100% immobilization and 107.7% activity yields. The proteins and L-tyrosine were determined by UV/VIS spectrophotometer. Optimum conditions for immobilization were determined by changing the conditions individually.
IgY and IgG activities were reduced significantly at pH 10.Since the soluble enzymes can not be used in repeated reactions and are not stable in operational conditions and not suitable for continuous processes, this study aimed the covalent immobilization of Bacillus licheniformis protease ( BLP) onto Eupergit CM. Treatment with pepsin significantly reduced IgY and IgG whereas trypsin slightly reduced IgY activities and has no effect on IgG activities.
IgY and IgG activities were significantly reduced at 80✬ and completely destroyed at 90✬. The activities of treated IgY and IgG were tested by enzyme linked immunosorbent assay (ELISA). Commercial antitetanus IgG was used as control. 120).The purified IgY was then treated at different levels of temperatures and pH as well as proteolytic enzymes. IgY was purified by ammonium sulfat precipitation and gel filtration chromatography (Sephadex G. Serum samples were collected 4 weeks following the last immunization. Antitetanus IgY was produced by immunization of chickens with tetanus toxoid, three times weekly at gradual doses of 100, 200, and 300 Lf, respectively. A study was carried out to find out an alternative method of producing antitetanus antibody (IgY) in chicken and to evaluate its activity at different levels of pH, temperatures and proteolytic enzymes.
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