A novel protein tyrosine phosphatase like phytase from Lactobacillus fermentum NKN51: Cloning, characterization and application in mineral release for food technology applications

A novel protein tyrosine phosphatase like phytase from Lactobacillus fermentum NKN51: Cloning,... Bioresource Technology 249 (2018) 1000–1008 Contents lists available at ScienceDirect Bioresource Technology journal homepage: www.elsevier.com/locate/biortech A novel protein tyrosine phosphatase like phytase from Lactobacillus fermentum NKN51: Cloning, characterization and application in mineral release for food technology applications a,1 a,1 a b a, Rekha Sharma , Piyush Kumar , Vandana Kaushal , Rahul Das , Naveen Kumar Navani Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India Department of Biological Sciences, Indian Institute of Science Education and Research, Kolkata 741246, India GR APHICAL A BSTRACT ARTICLE I NFO ABSTRACT Keywords: A novel protein tyrosine phosphatase like phytase (PTPLP), designated as PhyLf from probiotic bacterium Protein tyrosine phosphatase like phytase Lactobacillus fermentum NKN51 was identified, cloned, expressed and characterized. The recombinant PhyLf Lactobacillus fermentum NKN51 showed specific activity of 174.5 U/mg. PhyLf exhibited strict specificity towards phytate and optimum tem- Dephytinization perature at 60 °C, pH 5.0 and ionic strength of 100 mM. K and K of PhyLf for phytate were 0.773 mM and m cat Gastrointestinal conditions −1 84.31 s , respectively. PhyLf exhibited high resistance against oxidative inactivation. PhyLf shares no Bioaccessibility homology, sans the active site with reported PTLPs, warranting classification as a new subclass. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Bioresource Technology Elsevier

A novel protein tyrosine phosphatase like phytase from Lactobacillus fermentum NKN51: Cloning, characterization and application in mineral release for food technology applications

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Publisher
Elsevier
Copyright
Copyright © 2017 Elsevier Ltd
ISSN
0960-8524
D.O.I.
10.1016/j.biortech.2017.10.106
Publisher site
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Abstract

Bioresource Technology 249 (2018) 1000–1008 Contents lists available at ScienceDirect Bioresource Technology journal homepage: www.elsevier.com/locate/biortech A novel protein tyrosine phosphatase like phytase from Lactobacillus fermentum NKN51: Cloning, characterization and application in mineral release for food technology applications a,1 a,1 a b a, Rekha Sharma , Piyush Kumar , Vandana Kaushal , Rahul Das , Naveen Kumar Navani Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India Department of Biological Sciences, Indian Institute of Science Education and Research, Kolkata 741246, India GR APHICAL A BSTRACT ARTICLE I NFO ABSTRACT Keywords: A novel protein tyrosine phosphatase like phytase (PTPLP), designated as PhyLf from probiotic bacterium Protein tyrosine phosphatase like phytase Lactobacillus fermentum NKN51 was identified, cloned, expressed and characterized. The recombinant PhyLf Lactobacillus fermentum NKN51 showed specific activity of 174.5 U/mg. PhyLf exhibited strict specificity towards phytate and optimum tem- Dephytinization perature at 60 °C, pH 5.0 and ionic strength of 100 mM. K and K of PhyLf for phytate were 0.773 mM and m cat Gastrointestinal conditions −1 84.31 s , respectively. PhyLf exhibited high resistance against oxidative inactivation. PhyLf shares no Bioaccessibility homology, sans the active site with reported PTLPs, warranting classification as a new subclass.

Journal

Bioresource TechnologyElsevier

Published: Feb 1, 2018

References

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