Microbial phytases are enzymes that break down phytic acid, an anti-nutritional compound found in plant-based foods. These enzymes which are derived from bacteria and fungi have diverse properties and can function under different pH and temperature conditions. Their ability to convert phytic acid into inositol and inorganic phosphate makes them valuable in food processing. The application of microbial phytases in the food industry has several advantages. Firstly, adding them to animal feedstuff improves phosphorus availability, leading to improved nutrient utilization and growth in animals. This also reduces environmental pollution by phosphorus from animal waste. Secondly, microbial phytases enhance mineral bioavailability and nutrient assimilation in plant-based food products, counteracting the negative effects of phytic acid on human health. They can also improve the taste and functional properties of food and release bioactive compounds that have beneficial health effects. To effectively use microbial phytases in the food industry, factors like enzyme production, purification, and immobilization techniques are important. Genetic engineering and protein engineering have enabled the development of phytases with improved properties such as enhanced stability, substrate specificity, and resistance to degradation. This review provides an overview of the properties and function of phytases, the microbial strains that produce them, and their industrial applications, focusing on new approaches.
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Recent advances in phytase thermostability engineering towards potential application in the food and feed sectors.
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Integrated Bioprocess Laboratory, Department of Biotechnology, School of Bioengineering, SRM Institute of Science and Technology, Kattankulathur, Chennai, 603203 India.
Article Synopsis
- This review highlights recent advancements in engineering thermostable phytase through genetic modification and immobilization techniques over the last seven years.
- Genetic modifications have improved the enzyme's thermostability and functionality, while immobilization methods have helped retain 50-60% of its activity at temperatures above 50°C.
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