Properties of PEG-modified microbial proteases. Activity and stability studies

T. M. Fatum; A. Agerlin Olsen; C. C. Fuglsang; D. Otzen

doi:10.1016/S0921-0423(98)80024-5

Properties of PEG-modified microbial proteases. Activity and stability studies

T. M. Fatum^*, A. Agerlin Olsen, C. C. Fuglsang, D. Otzen

^*Corresponding author for this work

Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Abstract

Attachment of PEG to enzymes has been reported to prevent (auto)proteolysis¹, increase solu-bility and activity in organic solvents and to shield the enzyme from recognition by the immune system². We now report results of activity and stability studies of PEG modified subtilisins.

Original language	English
Journal	Progress in Biotechnology
Volume	15
Issue	C
Pages (from-to)	147-150
Number of pages	4
ISSN	0921-0423
DOIs	https://doi.org/10.1016/S0921-0423(98)80024-5
Publication status	Published - 1 Dec 1998

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@article{b719d66a215f4c239585805247fb70a4,

title = "Properties of PEG-modified microbial proteases. Activity and stability studies",

abstract = "Attachment of PEG to enzymes has been reported to prevent (auto)proteolysis1, increase solu-bility and activity in organic solvents and to shield the enzyme from recognition by the immune system2. We now report results of activity and stability studies of PEG modified subtilisins.",

author = "Fatum, {T. M.} and Olsen, {A. Agerlin} and Fuglsang, {C. C.} and D. Otzen",

year = "1998",

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doi = "10.1016/S0921-0423(98)80024-5",

language = "English",

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pages = "147--150",

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TY - JOUR

T1 - Properties of PEG-modified microbial proteases. Activity and stability studies

AU - Fatum, T. M.

AU - Olsen, A. Agerlin

AU - Fuglsang, C. C.

AU - Otzen, D.

PY - 1998/12/1

Y1 - 1998/12/1

N2 - Attachment of PEG to enzymes has been reported to prevent (auto)proteolysis1, increase solu-bility and activity in organic solvents and to shield the enzyme from recognition by the immune system2. We now report results of activity and stability studies of PEG modified subtilisins.

AB - Attachment of PEG to enzymes has been reported to prevent (auto)proteolysis1, increase solu-bility and activity in organic solvents and to shield the enzyme from recognition by the immune system2. We now report results of activity and stability studies of PEG modified subtilisins.

UR - http://www.scopus.com/inward/record.url?scp=77957142439&partnerID=8YFLogxK

U2 - 10.1016/S0921-0423(98)80024-5

DO - 10.1016/S0921-0423(98)80024-5

M3 - Journal article

AN - SCOPUS:77957142439

SN - 0921-0423

VL - 15

SP - 147

EP - 150

JO - Progress in Biotechnology

JF - Progress in Biotechnology

IS - C

ER -

Properties of PEG-modified microbial proteases. Activity and stability studies

Abstract

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