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 language | English |
|---|---|
| Pages (from-to) | 151-159 |
| Number of pages | 9 |
| Journal | Biotechnology and Bioengineering |
| Volume | 84 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2003 Oct 20 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology
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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 journal › Article
TY - JOUR
T1 - Binding and reversibility of Thermobifida fusca Cel5A, Cel6B, and Cel48A and their respective catalytic domains to bacterial microcrystalline cellulose
AU - Jung, Hyungil
AU - Wilson, David B.
AU - Walker, Larry P.
PY - 2003/10/20
Y1 - 2003/10/20
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0141504945&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0141504945&partnerID=8YFLogxK
U2 - 10.1002/bit.10743
DO - 10.1002/bit.10743
M3 - Article
C2 - 12966571
AN - SCOPUS:0141504945
VL - 84
SP - 151
EP - 159
JO - Biotechnology and Bioengineering
JF - Biotechnology and Bioengineering
SN - 0006-3592
IS - 2
ER -