CaltechAUTHORS
  A Caltech Library Service

Recent Advances in Directed Phytase Evolution and Rational Phytase Engineering

Shivange, Amol V. and Schwaneberg, Ulrich (2017) Recent Advances in Directed Phytase Evolution and Rational Phytase Engineering. In: Directed Enzyme Evolution: Advances and Applications. Springer , Cham, Switzerland, pp. 145-172. ISBN 978-3-319-50411-7. http://resolver.caltech.edu/CaltechAUTHORS:20170711-133839640

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:20170711-133839640

Abstract

Phytases are hydrolytic enzymes that initiate stepwise removal of phosphate from phytate. Phytate is the major phosphorous storage compound in cereal gains, oilseeds, and legumes and is indigestible by monogastric animals such as poultry and swine. Supplementation of phytase in animal feed proved to improve animal nutrition and decrease phosphorous pollution. Several phytases were discovered in the last century, and today a highly competitive market situation emerged the demands for phytases that are redesigned to excellently match industrial demands. Phytase engineering by directed evolution and rational design has offered a robust approach to tailor-made phytases with high specific activity, broad thermal and pH profile, and protease resistance. In this chapter, we summarized challenges and successful approaches employed in phytase engineering. Factors influencing phytase thermostability, pH stability, pH optima, and protease resistance have been discussed with respect to structural perspective and potential molecular mechanism for improvement. Importance of cooperative substitutions and a way to identify these interactions are discussed. Recent development in screening technology and molecular insights in combining key beneficial substitutions are detailed. In addition, strategies and approaches for rapid and efficient evolution of phytases and to understand structure function relationships on a molecular level have been proposed.


Item Type:Book Section
Related URLs:
URLURL TypeDescription
https://doi.org/10.1007/978-3-319-50413-1_6DOIArticle
Additional Information:© 2017 Springer International Publishing AG. First Online: 15 February 2017.
Record Number:CaltechAUTHORS:20170711-133839640
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20170711-133839640
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:78954
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:11 Jul 2017 20:50
Last Modified:10 Sep 2018 14:58

Repository Staff Only: item control page