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Improved activity retention of enzymes deposited on solid supports

Wehtje, Ernst LU ; Adlercreutz, Patrick LU orcid and Mattiasson, Bo LU (1993) In Biotechnology and Bioengineering 41(2). p.171-178
Abstract

Enzymes deposited on solid support usually show good stability when operated in organic solvents. Decreased stability of the enzyme preparations was noticed when low enzyme loadings were used (e.g., with Celite as support; less than 1 mg enzyme/g). It was possible to avoid the activity loss by the addition of an additive which protects the enzyme during the immobilization. Proteins (such as albumin, gelatin, and casein) and poly(ethylene glycol) were effective additives whereas amino acids, monomeric carbohydrates, and polysaccharides had no effect. The amount of additive needed for stabilization was shown to depend on the structure of the support, more additive being required for a support with high porosity. The stabilizing effect was... (More)

Enzymes deposited on solid support usually show good stability when operated in organic solvents. Decreased stability of the enzyme preparations was noticed when low enzyme loadings were used (e.g., with Celite as support; less than 1 mg enzyme/g). It was possible to avoid the activity loss by the addition of an additive which protects the enzyme during the immobilization. Proteins (such as albumin, gelatin, and casein) and poly(ethylene glycol) were effective additives whereas amino acids, monomeric carbohydrates, and polysaccharides had no effect. The amount of additive needed for stabilization was shown to depend on the structure of the support, more additive being required for a support with high porosity. The stabilizing effect was investigated in a series of glyceryl‐controlled‐pore glass (CPG) with varying specific surface areas (9.5–180 m2/g). The minimum addition of albumin, giving full stabilization, on the different supports correlated to a monolayer coverage of the surface, approximately 2–3 mg protein/m2. The effect of the additive was less pronounced when increasing amounts of enzyme were immobilized (5–40 mg enzyme/g Celite). The effect of the additives was studied using mandelonitrile lyase, but α‐chymotrypsin and lipase P were also shown to be stabilized. © 1993 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
additive, enzyme stabilization, immobilization, organic media, support material
in
Biotechnology and Bioengineering
volume
41
issue
2
pages
8 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:0027439598
ISSN
0006-3592
DOI
10.1002/bit.260410202
language
English
LU publication?
yes
id
8827a501-74a2-4503-b50a-6892f9941538
date added to LUP
2019-06-22 09:20:04
date last changed
2021-02-07 05:36:56
@article{8827a501-74a2-4503-b50a-6892f9941538,
  abstract     = {{<p>Enzymes deposited on solid support usually show good stability when operated in organic solvents. Decreased stability of the enzyme preparations was noticed when low enzyme loadings were used (e.g., with Celite as support; less than 1 mg enzyme/g). It was possible to avoid the activity loss by the addition of an additive which protects the enzyme during the immobilization. Proteins (such as albumin, gelatin, and casein) and poly(ethylene glycol) were effective additives whereas amino acids, monomeric carbohydrates, and polysaccharides had no effect. The amount of additive needed for stabilization was shown to depend on the structure of the support, more additive being required for a support with high porosity. The stabilizing effect was investigated in a series of glyceryl‐controlled‐pore glass (CPG) with varying specific surface areas (9.5–180 m<sup>2</sup>/g). The minimum addition of albumin, giving full stabilization, on the different supports correlated to a monolayer coverage of the surface, approximately 2–3 mg protein/m<sup>2</sup>. The effect of the additive was less pronounced when increasing amounts of enzyme were immobilized (5–40 mg enzyme/g Celite). The effect of the additives was studied using mandelonitrile lyase, but α‐chymotrypsin and lipase P were also shown to be stabilized. © 1993 John Wiley &amp; Sons, Inc.</p>}},
  author       = {{Wehtje, Ernst and Adlercreutz, Patrick and Mattiasson, Bo}},
  issn         = {{0006-3592}},
  keywords     = {{additive; enzyme stabilization; immobilization; organic media; support material}},
  language     = {{eng}},
  month        = {{01}},
  number       = {{2}},
  pages        = {{171--178}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Biotechnology and Bioengineering}},
  title        = {{Improved activity retention of enzymes deposited on solid supports}},
  url          = {{http://dx.doi.org/10.1002/bit.260410202}},
  doi          = {{10.1002/bit.260410202}},
  volume       = {{41}},
  year         = {{1993}},
}