Related Experiment Video
Updated: Mar 7, 2026
13:30
A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
18.6K
β-Propeller phytases: Diversity, catalytic attributes, current developments and potential biotechnological
Vinod Kumar1, Ajar Nath Yadav1, Priyanka Verma2
1Department of Biotechnology, Akal College of Agriculture, Eternal University, Baru Sahib, Sirmour 173101, India.
International Journal of Biological Macromolecules
|February 9, 2017
Summary
This review covers β-Propeller phytase (BPPhy), a diverse microbial enzyme. Advances in BPPhy research enhance its applications in animal nutrition, human health, and environmental protection.
Area of Science:
- Biochemistry
- Enzymology
- Microbiology
Background:
- Phytases are enzymes that remove phosphates from phytic acid.
- β-Propeller phytase (BPPhy) is a unique class of microbial phytases, primarily from Bacillus species.
- BPPhy exhibits Ca2+-dependent activity, substrate specificity, neutral to alkaline pH optimum, and high thermostability.
Purpose of the Study:
- To review the sources, diversity, and biochemical properties of BPPhy.
- To discuss structural elucidation, catalytic improvements, and applications of BPPhy.
- To highlight recent advancements in cloning, expression, and genetic engineering of BPPhy.
Main Methods:
- Literature review of sequence and structure-based studies.
- Analysis of biochemical and catalytic properties.
- Examination of genetic engineering and expression approaches.
Main Results:
- BPPhy possesses unique attributes compared to other phytase classes.
- Recent genetic engineering has improved BPPhy's catalytic efficiency.
- BPPhy shows potential for diverse applications.
Conclusions:
- BPPhy is a versatile enzyme with significant potential for various industrial and environmental applications.
- Continued research in BPPhy can lead to further improvements and expanded utilization.
- BPPhy plays a crucial role in improving nutrition, health, and sustainability.
Related Concept Videos
01:59Plant Breeding and Biotechnology
22.0K
Crop cultivation has a long history in human civilization, with records showing the cultivation of cereal plants beginning at around 8000 BC. This early plant breeding was developed primarily to provide a steady supply of food.
22.0K
02:54Protein Kinases and Phosphatases
15.4K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.4K
01:09Recombinant DNA
104.4K
Overview
104.4K
01:19Allosteric Proteins-ATCase
6.8K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.8K
01:18Amino Acid Catabolism
1.5K
Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
1.5K
01:07Catalytically Perfect Enzymes
5.3K
The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Most enzymes...
Most enzymes...
5.3K