Abstract:
:The immobilization of F(0)F(1)-ATPase in uniform orientation is reported. The biotinylated and histidine-tagged subunits of the bacterial F(0)F(1)-ATPase complex were used for immobilization of the complex on artificial semi-permeable membranes resulting in 88+/-7.8 and 72+/-5.2% coupling of the enzymes. The immobilized enzymes retained over 90% activity. The immobilized ATPase/synthase was used for generation of ATP from ADP and P(i) at the expense of electrochemical potential energy. The re-usability, ratio of amount of enzyme immobilized to enzymic activity conferred on the membranes, ATP synthesized by assembled system and suitability of ATP generated for use in coupled enzymic reactions were determined.
journal_name
Biotechnol Appl Biochemjournal_title
Biotechnology and applied biochemistryauthors
Bhattacharya S,Schiavone M,Nayak A,Bhattacharya SKdoi
10.1042/BA20030132subject
Has Abstractpub_date
2004-06-01 00:00:00pages
293-301issue
Pt 3eissn
0885-4513issn
1470-8744pii
BA20030132journal_volume
39pub_type
杂志文章abstract::The optimum temperature and initial medium pH for amylase production by Bacillus sp. TS-23 were 55 degrees C and 8.5 respectively. Maximum amylase activity was obtained in a medium containing peptone and soluble starch as nitrogen and carbon sources. Activity staining revealed that two amylases with molecular masses o...
journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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abstract::Two different enzymes that metabolize lactate in the presence of oxygen, either to acetate plus CO2 (lactate 2-mono-oxygenase; Lmox) or to pyruvate plus H2O2 (lactate oxidase; Lox) were encapsulated in human and murine red blood cells (RBCs). Lmox shows a low affinity for lactate (Km 22 mM) and thus works at a low rat...
journal_title:Biotechnology and applied biochemistry
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doi:
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
pub_type: 杂志文章
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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