# In silico analysis of insect-associated bacterial phytases reveals optimal biochemical properties and function in poultry gut condition

## TL;DR

Researchers analyzed insect gut bacteria to find phytases that could improve poultry nutrition and found promising candidates with good biochemical properties.

## Contribution

A homology search and in silico analysis identified insect-associated bacterial phytases with optimal properties for poultry gut conditions.

## Key findings

- Twenty-six phytases from insect-associated bacteria were identified and predicted to be stable and positively charged in poultry gut conditions.
- The histidine acid phosphatase from Tatumella sp. JGM130 showed the best structural quality and forms homo-tetramers.
- Molecular docking confirmed phytate binding at the catalytic motif of histidine acid phosphatases.

## Abstract

Insect guts may harbor phytase-producing bacteria applicable in poultry nutrition, but only Serratia sp. TN49 and its histidine acid phytase (AEQ29498.1) have been studied for this purpose. Therefore, AEQ29498.1 was used as a query to conduct a homology search for insect-associated bacterial phytases, followed by prediction of their structure and function. This in silico analysis of phytase may lead to the isolation of native phytase-producing bacteria from insect guts, potentially facilitating the production of desirable phytases for use in feed additives.

Twenty-six phytases from bacteria associated with the guts of black soldier fly larvae, fruit flies, and honey bees were identified. The mature chains of these phytases, except for the 4-phytase of Bartocella apis PEB0150, were predicted to carry a positive charge under the acidic conditions of the poultry upper gastrointestinal tract. They are stable (instability indices <40) and belong to histidine acid phosphatase family, which has been proven to be an effective poultry feed additive. The three-dimensional structure of the mature histidine-type phosphatase of Tatumella sp. JGM130 demonstrated the best quality and was found to be a homo-tetrameric protein. Molecular docking confirmed phytate binding at the catalytic motif of the histidine acid phosphatase family, RHGVRPP/AP/Q and HD.