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Effects of sorbitol addition on the action of free and immobilized hydrolytic enzymes in organic media

Triantafyllou, Angeliki Öste ; Wehtje, Ernst LU ; Adlercreutz, Patrick LU orcid and Mattiasson, Bo LU (1995) In Biotechnology and Bioengineering 45(5). p.406-414
Abstract

The effect of the addition of sorbitol on the activity and stability of enzymes was examined by monitoring transesterification reactions performed in organic media at various water activities (aw = 0.08 to 0.97). Lipases from Chromobacterium viscosum and Candida rugosa immobilized on celite, and chymotrypsin, free or immobilized on celite, were used. When the sorbitol‐containing enzymes were employed, higher reaction rates and less hydrolysis were observed. Immobilization of chymotrypsin resulted in high activity and operational stability, while the nonimmobilized enzyme was stable only in the presence of sorbitol. The activity of all preparations diminished after washing them with pyridine to remove sorbitol. Furthermore,... (More)

The effect of the addition of sorbitol on the activity and stability of enzymes was examined by monitoring transesterification reactions performed in organic media at various water activities (aw = 0.08 to 0.97). Lipases from Chromobacterium viscosum and Candida rugosa immobilized on celite, and chymotrypsin, free or immobilized on celite, were used. When the sorbitol‐containing enzymes were employed, higher reaction rates and less hydrolysis were observed. Immobilization of chymotrypsin resulted in high activity and operational stability, while the nonimmobilized enzyme was stable only in the presence of sorbitol. The activity of all preparations diminished after washing them with pyridine to remove sorbitol. Furthermore, severe stability problems occurred in the preparations lacking sorbitol. Sorbitol treatment, even after removal of the sorbitol itself, improved the activity of nonimmobilized chymotrypsin relative to the washed control. On the other hand, washing to remove sorbitol had a negative effect on the activity of both coimmobilized lipase and coimmobilized chymotrypsin. Addition of a substrate analogue, N‐acetyl‐L‐phenylalanine, to chymotrypsin yielded a preparation that exhibited higher activity than both the control and its sorbitol‐containing counterpart. Differential scanning calorimetry measurements revealed that the chymotrypsin–sorbitol complex was stable against thermal denaturation, undergoing transition at a high temperature (89°C). The transition temperatures of the substrate‐containing chymotrypsin and of the control were identical (72°C). © 1995 John Wiley & Sons, Inc.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
chymotrypsin, differential scanning calorimetry, ligands, lipase, organic media, sorbitol
in
Biotechnology and Bioengineering
volume
45
issue
5
pages
9 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:0029636230
ISSN
0006-3592
DOI
10.1002/bit.260450505
language
English
LU publication?
yes
id
bcd0ba55-3d78-4f9c-baeb-fbc24c34d493
date added to LUP
2019-06-22 09:07:50
date last changed
2021-01-03 04:55:45
@article{bcd0ba55-3d78-4f9c-baeb-fbc24c34d493,
  abstract     = {{<p>The effect of the addition of sorbitol on the activity and stability of enzymes was examined by monitoring transesterification reactions performed in organic media at various water activities (a<sub>w</sub> = 0.08 to 0.97). Lipases from Chromobacterium viscosum and Candida rugosa immobilized on celite, and chymotrypsin, free or immobilized on celite, were used. When the sorbitol‐containing enzymes were employed, higher reaction rates and less hydrolysis were observed. Immobilization of chymotrypsin resulted in high activity and operational stability, while the nonimmobilized enzyme was stable only in the presence of sorbitol. The activity of all preparations diminished after washing them with pyridine to remove sorbitol. Furthermore, severe stability problems occurred in the preparations lacking sorbitol. Sorbitol treatment, even after removal of the sorbitol itself, improved the activity of nonimmobilized chymotrypsin relative to the washed control. On the other hand, washing to remove sorbitol had a negative effect on the activity of both coimmobilized lipase and coimmobilized chymotrypsin. Addition of a substrate analogue, N‐acetyl‐L‐phenylalanine, to chymotrypsin yielded a preparation that exhibited higher activity than both the control and its sorbitol‐containing counterpart. Differential scanning calorimetry measurements revealed that the chymotrypsin–sorbitol complex was stable against thermal denaturation, undergoing transition at a high temperature (89°C). The transition temperatures of the substrate‐containing chymotrypsin and of the control were identical (72°C). © 1995 John Wiley &amp; Sons, Inc.</p>}},
  author       = {{Triantafyllou, Angeliki Öste and Wehtje, Ernst and Adlercreutz, Patrick and Mattiasson, Bo}},
  issn         = {{0006-3592}},
  keywords     = {{chymotrypsin; differential scanning calorimetry; ligands; lipase; organic media; sorbitol}},
  language     = {{eng}},
  month        = {{03}},
  number       = {{5}},
  pages        = {{406--414}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Biotechnology and Bioengineering}},
  title        = {{Effects of sorbitol addition on the action of free and immobilized hydrolytic enzymes in organic media}},
  url          = {{http://dx.doi.org/10.1002/bit.260450505}},
  doi          = {{10.1002/bit.260450505}},
  volume       = {{45}},
  year         = {{1995}},
}