A simple entrapment of glucoamylase into LentiKats® as an efficient catalyst for maltodextrin hydrolysis
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Rebros, Martin
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Slovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, SlovakiaSlovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, Slovakia
Rebros, Martin
[1
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Rosenberg, Michal
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Slovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, SlovakiaSlovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, Slovakia
Rosenberg, Michal
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Mlichova, Zuzana
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Slovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, SlovakiaSlovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, Slovakia
Mlichova, Zuzana
[1
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Kristofikova, L'udmila
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Slovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, SlovakiaSlovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, Slovakia
Kristofikova, L'udmila
[1
]
Paluch, Miroslav
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Slovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, SlovakiaSlovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, Slovakia
Paluch, Miroslav
[1
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[1] Slovak Univ Technol Bratislava, Dept Biotechnol, Fac Chem & Food Technol, Bratislava 81237, Slovakia
The glucoamylase from Aspergillus niger was immobilized into a poly(vinylalcohol) hydrogel lens-shaped capsules LentiKats (R). Immobilization broadened the pH optimum of the enzyme. The K-M of glucoamylase increased after immobilization (approximately 1.5 times on maltose), which reflected the decrease in affinity of enzyme for its substrate. Immobilized enzyme retained excellent long-term operational stability for both, batch and continuous mode of hydrolysis. Specific enzymatic activity of the immobilized enzyme (0.67 g g(-1) h(-1)) was constant for 63 days of continuous operation at 45 degrees C. (c) 2006 Elsevier Inc. All rights reserved.
机构:Middle E Tech Univ, Dept Sci Biol, Biotechnol Res Unit, TR-06531 Ankara, Turkey
Arica, MY
Alaeddinoglu, NG
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机构:Middle E Tech Univ, Dept Sci Biol, Biotechnol Res Unit, TR-06531 Ankara, Turkey
Alaeddinoglu, NG
Hasirci, V
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Middle E Tech Univ, Dept Sci Biol, Biotechnol Res Unit, TR-06531 Ankara, TurkeyMiddle E Tech Univ, Dept Sci Biol, Biotechnol Res Unit, TR-06531 Ankara, Turkey
机构:Middle E Tech Univ, Dept Sci Biol, Biotechnol Res Unit, TR-06531 Ankara, Turkey
Arica, MY
Alaeddinoglu, NG
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机构:Middle E Tech Univ, Dept Sci Biol, Biotechnol Res Unit, TR-06531 Ankara, Turkey
Alaeddinoglu, NG
Hasirci, V
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Middle E Tech Univ, Dept Sci Biol, Biotechnol Res Unit, TR-06531 Ankara, TurkeyMiddle E Tech Univ, Dept Sci Biol, Biotechnol Res Unit, TR-06531 Ankara, Turkey