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Catalytic characterization of phytase (myo-inositolhexakisphosphate phosphohydrolase) from Aspergillus niger van Teighem: Glycosylation pattern, kinetics and molecular properties

Paper ID Volume ID Publish Year Pages File Format Full-Text
18493 42725 2006 5 PDF Available
Title
Catalytic characterization of phytase (myo-inositolhexakisphosphate phosphohydrolase) from Aspergillus niger van Teighem: Glycosylation pattern, kinetics and molecular properties
Abstract

A phytase with a high specific activity from Aspergillus niger van Teighem was purified to near homogeneity and characterized in terms of different catalytic properties. The N-terminal sequence of purified phytase was determined to be FYYGAALPQS. The purified phytase was a glycosylated protein as judged by positive PAS staining with pI of 3.8 as estimated by two-dimensional gel electrophoresis. The kinetic studies revealed that the enzyme was competitively inhibited by myo-inositolhexasulphate (MIHS), a structural analogue of phytic acid, with apparent Ki of 0.05 mM. The Km of the phytase increased from 0.625 to 1.898 mM in the presence MIHS with 50% inhibition of phytase activity at 100 μM MIHS. The enzyme was significantly inhibited by inorganic phosphorus in uncompetitive manner (Ki = 0.16 mM) with 50% inhibition of phytase activity at 0.2 mM Pi. This phytase protein was approx. three-fold more sensitive to MIHS inhibition than inorganic phosphorus.

Keywords
Aspergillus niger; Phytases; Acid-phosphatases; Inositolhexaphosphate phosphohydrolases; Catalytic properties; Myo-inositolhexasulphate
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Catalytic characterization of phytase (myo-inositolhexakisphosphate phosphohydrolase) from Aspergillus niger van Teighem: Glycosylation pattern, kinetics and molecular properties
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 4, 2 August 2006, Pages 596–600
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
Online Support
Any Questions? feel free to contact us