fusion protein designed for noncovalent immobilization: stability, enzymatic activity, and use in an enzyme reactor
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Veröffentlicht in: | Nature biotechnology 1996-04, Vol.14 (4), p.481-484 |
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container_issue | 4 |
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container_title | Nature biotechnology |
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creator | Stempfer, G Holl-Neugebauer, B Kopetzki, E Rudolph, R |
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doi_str_mv | 10.1038/nbt0496-481 |
format | Article |
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Psychology</subject><subject>hexa-arginine peptides</subject><subject>immobilization</subject><subject>Immobilization of enzymes and other molecules</subject><subject>Immobilization techniques</subject><subject>immobilized enzymes</subject><subject>maltose</subject><subject>Methods. Procedures. 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Psychology</topic><topic>hexa-arginine peptides</topic><topic>immobilization</topic><topic>Immobilization of enzymes and other molecules</topic><topic>Immobilization techniques</topic><topic>immobilized enzymes</topic><topic>maltose</topic><topic>Methods. Procedures. 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ispartof | Nature biotechnology, 1996-04, Vol.14 (4), p.481-484 |
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source | SpringerLink; Springer Nature - Connect here FIRST to enable access |
subjects | adsorption alpha-galactosidase Biological and medical sciences bioreactors Biotechnology chemical structure enzyme activity Fundamental and applied biological sciences. Psychology hexa-arginine peptides immobilization Immobilization of enzymes and other molecules Immobilization techniques immobilized enzymes maltose Methods. Procedures. Technologies oligopeptides recombinant proteins Saccharomyces cerevisiae stability |
title | fusion protein designed for noncovalent immobilization: stability, enzymatic activity, and use in an enzyme reactor |
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