Journal ArticleDOI
Hydrolysis of maltose and cornstrarch by glucoamylase immobilized in porous glass fibres and beads
TLDR
Glucoamylase (1,4 α-d glucan glucohydrolase, EC 3.2.3) was covalently immobilized on porous glass fibres and beads as discussed by the authors.About:
This article is published in Process Biochemistry.The article was published on 1992-05-01. It has received 6 citations till now. The article focuses on the topics: Dextrose equivalent & Immobilized enzyme.read more
Citations
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Journal ArticleDOI
Enzymatic conversions of starch.
Piotr Tomasik,Derek Horton +1 more
TL;DR: Methods for the enzymatic conversion of starch, involving hydrolases and nonhydrolyzing enzymes, as well as the role of microorganisms producing such enzymes, are surveyed, covering the period from the early 19th century up to 2009.
Journal ArticleDOI
Carrier free co-immobilization of glucoamylase and pullulanase as combi-cross linked enzyme aggregates (combi-CLEAs)
Sachin Talekar,Shashikant Desai,Meena M Pillai,Nupur Nagavekar,Sneha Ambarkar,Sharvari Surnis,Mayur R. Ladole,Shamraja S. Nadar,Mosin Mulla +8 more
TL;DR: The successful preparation of carrier free co-immobilized form of glucoamylase and pullulanase using combi-CLEAs method from commercial multi-enzyme preparation OPTIMAX® 7525 HP shows that co-IMobilization enhanced the thermal stability and storage stability.
Journal ArticleDOI
Structured fiber supports for gas phase biocatalysis
TL;DR: Under the conditions investigated, the immobilized enzyme showed a high thermostability and could be efficiently used to catalyze hydrolytic and transesterification reactions in continuous mode.
Journal ArticleDOI
Immobilization of glucoamylase onto novel porous polymer supports of vinylene carbonate and 2-hydroxyethyl methacrylate.
TL;DR: The immobilized glucoamylase still maintained about 84% of its initial activity, whereas the native enzyme only maintained about 58% of the initial activity after storage for 23 d, and the properties of porous polymer supports had an effect on the activity of the immobilized enzyme.
Journal ArticleDOI
Peptide generation from casein hydrolysis by immobilised porcine cathepsins
TL;DR: A porcine kidney enzyme extract containing high levels of cathepsins B and L activities has been successfully immobilised onto porous glass beads and showed improved stability when immobilised, exhibiting a half-life of 97.5 h at 30 °C vs 5.6 h for the free enzyme in solution.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Book ChapterDOI
Covalent coupling methods for inorganic support materials.
TL;DR: In this article, the covalent attachment of enzymes to organic supports is discussed, and derivatives of alkylamines and coupling techniques are described in the chapter, including aqueous and organic silanization.
Journal ArticleDOI
Pilot plant production of glucose with glucoamylase immobilized to porous silica.
TL;DR: The immobilized enzyme was immobilized to porous silica and its kinetics and stability were observed with acid‐ and α‐amylase‐hydrolyzed dextrin as feed and it was found to be extremely stable in both laboratory and pilot plant operations.
Journal ArticleDOI
Effect of pore diffusion limitation on dextrin hydrolysis by immobilized glucoamylase.
TL;DR: Data reported here and previously indicate that when dextrin is hydrolyzed in the presence of immobilized glucoamylase, use of a larger average molecular weight substrate leads to lower overall rates of hydrolysis, while the maltose concentration during the bulk of the reaction and the maximum glucose concentration are lower than when the soluble form of the enzyme is employed under the same conditions.
Related Papers (5)
Characterization of glucoamylase immobilized on magnetic poly(styrene) particles
Tahsin Bahar,Serdar S. Çelebi +1 more
Comparison between different inorganic supports for the immobilization of amyloglucosidase and α-amylase to be used in enzyme reactors in flow-injection systems: Part I. Hydrolysis of maltose, maltooligosaccharides and soluble starch
Jenny Emnéus,Lo Gorton +1 more