A differential scanning calorimetric study of chymotrypsin in the presence of added polymers
Otamiri, Marina ; Adlercreutz, Patrick LU
and Mattiasson, Bo
LU
(1994)
In Biotechnology and Bioengineering
44(1).
p.73-78
- Abstract
Scanning calorimetry measurements of different amounts of chymotrypsin in water alone gave a temperature of denaturation (Td) value of 54°C. However, when high‐molecular‐weight poly(ethylene glycol) was added to aqueous solutions of chymotrypsin, the thermostability of the enzyme was enhanced. For example, the addition of 20% (w/w) of poly(ethylene glycol) of molecular weight of 100,000 increased the Td/ value to 66°C. In toluene containing various amounts of added water, ethyl cellulose was used to improve the thermostability of chymotrypsin. For this system, a Td value of 82°C was obtained with a 20% (w/w/) concentration of ethyl cellulose and 2% (v/v) of added water. Polymers in these solvents... (More)
Scanning calorimetry measurements of different amounts of chymotrypsin in water alone gave a temperature of denaturation (Td) value of 54°C. However, when high‐molecular‐weight poly(ethylene glycol) was added to aqueous solutions of chymotrypsin, the thermostability of the enzyme was enhanced. For example, the addition of 20% (w/w) of poly(ethylene glycol) of molecular weight of 100,000 increased the Td/ value to 66°C. In toluene containing various amounts of added water, ethyl cellulose was used to improve the thermostability of chymotrypsin. For this system, a Td value of 82°C was obtained with a 20% (w/w/) concentration of ethyl cellulose and 2% (v/v) of added water. Polymers in these solvents interact with water, which could otherwise denature the enzyme; polymers also from complexes with enzyme molecules to produce a more stable structure. © 1994 John Wiley & Sons, Inc.
(Less)
- author
- Otamiri, Marina
; Adlercreutz, Patrick
LU
and Mattiasson, Bo
LU
- organization
- publishing date
- 1994-01-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- chymotrypsin, ethyl cellulose, poly(ethylene glycol), polymers
- in
- Biotechnology and Bioengineering
- volume
- 44
- issue
- 1
- pages
- 6 pages
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:0028765236
- ISSN
- 0006-3592
- DOI
- 10.1002/bit.260440111
- language
- English
- LU publication?
- yes
- id
- f226f50a-afc1-4baf-b3fa-f7730b910c79
- date added to LUP
- 2019-06-22 09:11:16
- date last changed
- 2021-01-03 04:25:41
@article{f226f50a-afc1-4baf-b3fa-f7730b910c79,
abstract = {{<p>Scanning calorimetry measurements of different amounts of chymotrypsin in water alone gave a temperature of denaturation (T<sub>d</sub>) value of 54°C. However, when high‐molecular‐weight poly(ethylene glycol) was added to aqueous solutions of chymotrypsin, the thermostability of the enzyme was enhanced. For example, the addition of 20% (w/w) of poly(ethylene glycol) of molecular weight of 100,000 increased the T<sub>d/</sub> value to 66°C. In toluene containing various amounts of added water, ethyl cellulose was used to improve the thermostability of chymotrypsin. For this system, a T<sub>d</sub> value of 82°C was obtained with a 20% (w/w/) concentration of ethyl cellulose and 2% (v/v) of added water. Polymers in these solvents interact with water, which could otherwise denature the enzyme; polymers also from complexes with enzyme molecules to produce a more stable structure. © 1994 John Wiley & Sons, Inc.</p>}},
author = {{Otamiri, Marina and Adlercreutz, Patrick and Mattiasson, Bo}},
issn = {{0006-3592}},
keywords = {{chymotrypsin; ethyl cellulose; poly(ethylene glycol); polymers}},
language = {{eng}},
month = {{01}},
number = {{1}},
pages = {{73--78}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Biotechnology and Bioengineering}},
title = {{A differential scanning calorimetric study of chymotrypsin in the presence of added polymers}},
url = {{http://dx.doi.org/10.1002/bit.260440111}},
doi = {{10.1002/bit.260440111}},
volume = {{44}},
year = {{1994}},
}