2014
DOI: 10.1515/ijcre-2013-0145
|View full text |Cite
|
Sign up to set email alerts
|

α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite

Abstract: The α-amylase from Aspergillus oryzae was immobilized covalently onto expanded perlite (EP) and modified EP by treatment with TiO2 (EP-TiO2), dye HE3B (EP-HE3B) polyethylene terephthalate (PET)-hydrazide (EP-PET) and magnetite (EP-magnetite). The modified EP was characterized using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The supports were functionalized with aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA). The optimum pH for free and immobilized α-amyla… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2

Citation Types

0
2
0

Year Published

2017
2017
2017
2017

Publication Types

Select...
1

Relationship

0
1

Authors

Journals

citations
Cited by 1 publication
(2 citation statements)
references
References 24 publications
0
2
0
Order By: Relevance
“…The unit of catalytic activity katal (kat) was taken as the amount of enzyme that liberates 1 mol of maltose per second (Rodriguez et al, 2014). As the reaction progressed, we measured the amount of maltose produced by assay of the DNS.…”
Section: A-amylasementioning
confidence: 99%
See 1 more Smart Citation
“…The unit of catalytic activity katal (kat) was taken as the amount of enzyme that liberates 1 mol of maltose per second (Rodriguez et al, 2014). As the reaction progressed, we measured the amount of maltose produced by assay of the DNS.…”
Section: A-amylasementioning
confidence: 99%
“…As the reaction progressed, we measured the amount of maltose produced by assay of the DNS. The unit of catalytic activity katal (kat) was taken as the amount of enzyme that liberates 1 mol of maltose per second (Rodriguez et al, 2014).…”
Section: A-amylasementioning
confidence: 99%