Activity studies of immobilized subtilisin on functionalized pure cellulose-based membranes

J. Liu, J. Wang, Leonidas G Bachas, D. Bhattacharyya

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The activity of immobilized subtilisin BPN' on pure cellulose-based membrane support was investigated using site-directed and random immobilization approaches. The catalytic activity of site-directed immobilized subtilisin on pure cellulose fiber-based materials was found to be 81% of that in homogeneous solution, while that of randomly immobilized subtilisin was 27%. Pure cellulose membrane supports provided large surface areas for high enzyme loading without diffusional limitations. The activity of immobilized subtilisin on pure cellulose support was more than twice that on a modified polyether sulfone (MPS) membrane, which was attributed to the higher hydrophilicity of cellulose. Immobilized subtilisin maintained its initial activity for 14 days at 4°C and 7 days at 24°C. The immobilized enzyme could resist higher temperature and operate over a wider range of pH without loss of activity. This study showed that pure cellulose fiber-based membranes are well suited for enzyme immobilization and biocatalysis.

Original languageEnglish (US)
Pages (from-to)866-871
Number of pages6
JournalBiotechnology Progress
Volume17
Issue number5
DOIs
StatePublished - 2001
Externally publishedYes

Fingerprint

Subtilisin
subtilisin
Cellulose
cellulose
Membranes
cellulosic fibers
immobilized enzymes
Immobilization
Biocatalysis
Subtilisins
Immobilized Enzymes
catalytic activity
Enzymes
surface area
Hydrophobic and Hydrophilic Interactions
Catalytic Domain
enzymes
Temperature
temperature

ASJC Scopus subject areas

  • Food Science
  • Biotechnology
  • Microbiology

Cite this

Activity studies of immobilized subtilisin on functionalized pure cellulose-based membranes. / Liu, J.; Wang, J.; Bachas, Leonidas G; Bhattacharyya, D.

In: Biotechnology Progress, Vol. 17, No. 5, 2001, p. 866-871.

Research output: Contribution to journalArticle

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