Binding and reversibility of Thermobifida fusca Cel5A, Cel6B, and Cel48A and their respective catalytic domains to bacterial microcrystalline cellulose

Hyungil Jung, David B. Wilson, Larry P. Walker

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

The binding and reversibility of Thermobifida fusca intact Ce15A, Ce15B, and Ce148A and their corresponding catalytic domains (CDs) to bacterial microcrystalline cellulose (BMCC) were studied at 5°C. The binding of the intact cellulases and of corresponding CDs to BMCC was irreversible in all regions: Langmuir binding (region I), interstice penetration (region II), and interstice saturation (region III). The three cellulose binding domains (CBMs) bind reversibly in "region I" although their respective CDs do not. The irreversible binding of these enzymes in the Langmuir region does not satisfy the Langmuir assumption; however, the overall fit of the Interstice Saturation model, which includes binding in MBCC interstices as well as on the freely accessible surface (Jung et al., 2002a) is good. The main limitation of the model is that it does not explicitly address a mechanism for forming the enzyme-substrate complex within the active site of the CDs.

Original languageEnglish
Pages (from-to)151-159
Number of pages9
JournalBiotechnology and Bioengineering
Volume84
Issue number2
DOIs
Publication statusPublished - 2003 Oct 20

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Cellulose
Catalytic Domain
Cellulases
Enzymes
Substrates
microcrystalline cellulose

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this

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Binding and reversibility of Thermobifida fusca Cel5A, Cel6B, and Cel48A and their respective catalytic domains to bacterial microcrystalline cellulose. / Jung, Hyungil; Wilson, David B.; Walker, Larry P.

In: Biotechnology and Bioengineering, Vol. 84, No. 2, 20.10.2003, p. 151-159.

Research output: Contribution to journalArticle

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