Covalent immobilization of an alkaline protease from Bacillus licheniformis
Yükleniyor...
Tarih
Aralık, 2018
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
DeGruyter
Erişim Hakkı
info:eu-repo/semantics/restrictedAccess
Attribution-NonCommercial-NoDerivs 3.0 United States
Attribution-NonCommercial-NoDerivs 3.0 United States
Özet
Objective: 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.
Methods: Optimum conditions for immobilization were determined by changing the conditions individually. The proteins and L-tyrosine were determined by UV/VIS spectrophotometer.
Results: The immobilization resulted in 100% immobilization and 107.7% activity yields. The optimum pH (7–8) and the optimum temperature (70°C) have not changed after immobilization. The Km values for free and immobilized enzyme were 26.53 and 37.59 g/L, while the Vmax values were 2.84 and 3.31 g L-Tyrosine/L · min, respectively. The immobilized enzyme has not lost its initial activity during the repeated 20 uses and 20 days of storage. The milk proteins were hydrolyzed in 2 h by using immobilized enzyme. 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.
Conclusion: Consequently, it can be said that the immobilized BLP obtained can be used for industrial purposes.
Açıklama
Anahtar Kelimeler
Cow’s milk; Eupergit CM; Immobilization; Protease; Protein; Protein allergy.
Kaynak
Turkish Journal of Biochemistry
WoS Q Değeri
Q4
Scopus Q Değeri
Q3
Cilt
43
Sayı
6
