Hydrolysis of starch particles using immobilized barley α-amylase
Barley α-amylase has been immobilized on silica particles with diameters between 0.5 and 10 μm using a covalent binding method. Immobilization procedures were adjusted to optimize enzyme activity. The effects of product inhibition, thermal stability and operational stability have been determined. Th...
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Veröffentlicht in: | Biochemical engineering journal 2003, Vol.13 (1), p.53-62 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | Barley α-amylase has been immobilized on silica particles with diameters between 0.5 and 10
μm using a covalent binding method. Immobilization procedures were adjusted to optimize enzyme activity. The effects of product inhibition, thermal stability and operational stability have been determined. The feasibility of using the immobilized enzyme to hydrolyze wheat starch particles at temperatures below the gelatinization temperature ( |
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ISSN: | 1369-703X 1873-295X |
DOI: | 10.1016/S1369-703X(02)00101-8 |