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

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Properties of PEG-modified microbial proteases. Activity and stability studies. / Fatum, T. M.; Olsen, A. Agerlin; Fuglsang, C. C. et al.

In: Progress in Biotechnology, Vol. 15, No. C, 01.12.1998, p. 147-150.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Fatum, TM, Olsen, AA, Fuglsang, CC & Otzen, D 1998, 'Properties of PEG-modified microbial proteases. Activity and stability studies', Progress in Biotechnology, vol. 15, no. C, pp. 147-150. https://doi.org/10.1016/S0921-0423(98)80024-5

APA

Fatum, T. M., Olsen, A. A., Fuglsang, C. C., & Otzen, D. (1998). Properties of PEG-modified microbial proteases. Activity and stability studies. Progress in Biotechnology, 15(C), 147-150. https://doi.org/10.1016/S0921-0423(98)80024-5

CBE

MLA

Vancouver

Fatum TM, Olsen AA, Fuglsang CC, Otzen D. Properties of PEG-modified microbial proteases. Activity and stability studies. Progress in Biotechnology. 1998 Dec 1;15(C):147-150. doi: 10.1016/S0921-0423(98)80024-5

Author

Fatum, T. M. ; Olsen, A. Agerlin ; Fuglsang, C. C. et al. / Properties of PEG-modified microbial proteases. Activity and stability studies. In: Progress in Biotechnology. 1998 ; Vol. 15, No. C. pp. 147-150.

Bibtex

@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",
month = dec,
day = "1",
doi = "10.1016/S0921-0423(98)80024-5",
language = "English",
volume = "15",
pages = "147--150",
journal = "Progress in Biotechnology",
issn = "0921-0423",
publisher = "Elsevier",
number = "C",

}

RIS

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

VL - 15

SP - 147

EP - 150

JO - Progress in Biotechnology

JF - Progress in Biotechnology

SN - 0921-0423

IS - C

ER -