2012
DOI: 10.3390/ijms130911870
|View full text |Cite
|
Sign up to set email alerts
|

Polystyrene Attached Pt(IV)–Azomethine, Synthesis and Immobilization of Glucose Oxidase Enzyme

Abstract: Modified polystyrene with Pt(IV)–azomethine (APS–Sch–Pt) was synthesized by means of condensation and demonstrated to be a promising enzyme support by studying the enzymatic properties of glucose oxidase enzyme (GOx) immobilized on it. The characteristics of the immobilized glucose oxidase (APS–Sch–Pt–GOx) enzyme showed two optimum pH values that were pH = 4.0 and pH = 7. The insertion of stable Pt(IV)–azomethine spacers between the polystyrene backbone and the immobilized GOx, (APS–Sch–Pt–GOx), increases the … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

0
8
0

Year Published

2014
2014
2022
2022

Publication Types

Select...
7

Relationship

2
5

Authors

Journals

citations
Cited by 18 publications
(8 citation statements)
references
References 18 publications
0
8
0
Order By: Relevance
“…However, after an additional ∼300 min, the YOYO-1 fluorescence behaviour dramatically changed: immediately after the light exposure, isolated, strong diffraction-limited signals appeared indicating the potential of this preparation method for SMLM (Figure 3C ). At pH 4, GOX activity is still at ∼40% of its value at neutral pH ( 51 ), therefore GOX will keep the oxygen concentration low in a sealed sample in acidic pH. When GOX was replaced with pyranose oxidase (PO), whose product of oxygen scavenging does not have an effect on pH of the buffer ( 49 ) (Figure 3A ), the YOYO-1 signal intensity remained constant over time (Figure 3B ) and no single molecule signals could be observed (data not shown).…”
Section: Resultsmentioning
confidence: 99%
“…However, after an additional ∼300 min, the YOYO-1 fluorescence behaviour dramatically changed: immediately after the light exposure, isolated, strong diffraction-limited signals appeared indicating the potential of this preparation method for SMLM (Figure 3C ). At pH 4, GOX activity is still at ∼40% of its value at neutral pH ( 51 ), therefore GOX will keep the oxygen concentration low in a sealed sample in acidic pH. When GOX was replaced with pyranose oxidase (PO), whose product of oxygen scavenging does not have an effect on pH of the buffer ( 49 ) (Figure 3A ), the YOYO-1 signal intensity remained constant over time (Figure 3B ) and no single molecule signals could be observed (data not shown).…”
Section: Resultsmentioning
confidence: 99%
“…The optimum pH values are given in Table . The pH is a significant parameter capable of altering enzymatic activities in aqueous solution . The maximum activity was obtained at pH 5.0, for the free enzyme.…”
Section: Resultsmentioning
confidence: 99%
“…Covalent bonding is a preferred immobilization method because of its potential advantages such as increased enzyme activity and preservation of its structure . In GOx, the hydroxyl groups are connected by hydrogen bonds/or coordination covalent bonds to polymeric support by acting as good chelating agents …”
Section: Introductionmentioning
confidence: 99%
“…The elemental analyses can be considered compatible with the chemical formulas of the compounds [23,24]. The weight average molecular weight (Mw) was suggested from element analyses.…”
Section: Characterization Of Support Nanospherementioning
confidence: 99%