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 af dette arbejde

Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › 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.

Originalsprog	Engelsk
Tidsskrift	Progress in Biotechnology
Vol/bind	15
Nummer	C
Sider (fra-til)	147-150
Antal sider	4
ISSN	0921-0423
DOI	https://doi.org/10.1016/S0921-0423(98)80024-5
Status	Udgivet - 1 dec. 1998

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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",

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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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