Stabilization of papain by modification with chitosan

Küçük Resim Yok

Tarih

2002

Dergi Başlığı

Dergi ISSN

Cilt Başlığı

Yayıncı

Erişim Hakkı

info:eu-repo/semantics/openAccess

Özet

Papain (EC 3.4.22.2) was immobilized on chitosan by adsorption and subsequent cross-linking with glutaraldehyde. The immobilized papain displayed a lower specific activity than did the native enzyme. The thermal stability of the immobilized papain, relative to that of the free enzyme, was markedly increased. The storage stability of the conjugated enzyme was enhanced such that more than 85% of the initial activity remained after a month storage at 45°C. The optimum pH of immobilized papain was shifted to the acidic region and enzyme stability was increased at pH levels below 3.5.
Papain (EC 3.4.22.2) was immobilized on chitosan by adsorption and subsequent cross-linking with glutaraldehyde. The immobilized papain displayed a lower specific activity than did the native enzyme. The thermal stability of the immobilized papain, relative to that of the free enzyme, was markedly increased. The storage stability of the conjugated enzyme was enhanced such that more than 85% of the initial activity remained after a month storage at 45°C. The optimum pH of immobilized papain was shifted to the acidic region and enzyme stability was increased at pH levels below 3.5.

Açıklama

Anahtar Kelimeler

Mühendislik, Kimya

Kaynak

Turkish Journal of Chemistry

WoS Q Değeri

Scopus Q Değeri

Cilt

26

Sayı

3

Künye