A computational method for prediction of xylanase enzymes activity in strains of Bacillus subtilis based on pseudo amino acid composition features

Shohreh Ariaeenejad*, Maryam Mousivand, Parinaz Moradi Dezfouli, Maryam Hashemi, Kaveh Kavousi, Ghasem Hosseini Salekdeh

*Corresponding author for this work

Research output: Contribution to journalArticle

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Xylanases are hydrolytic enzymes which based on physicochemical properties, structure, mode of action and substrate specificities are classified into various glycoside hydrolase (GH) families. The purpose of this study is to show that the activity of the members of the xylanase family in the specified pH and temperature conditions can be computationally predicted. The proposed computational regression model was trained and tested with the Pseudo Amino Acid Composition (PseAAC) features extracted solely from the amino acid sequences of enzymes. The xylanases with experimentally determined activities were used as the training dataset to adjust the model parameters. To develop the model, 41 strains of Bacillus subtilis isolated from field soil were screened. From them, 28 strains with the highest halo diameter were selected for further studies. The performance of the model for prediction of xylanase activity was evaluated in three different temperature and pH conditions using stratified cross-validation and jackknife methods. The trained model can be used for determining the activity of newly found xylanases in the specified condition. Such computational models help to scale down the experimental costs and save time by identifying enzymes with appropriate activity for scientific and industrial usage. Our methodology for activity prediction of xylanase enzymes can be potentially applied to the members of the other enzyme families. The availability of sufficient experimental data in specified pH and temperature conditions is a prerequisite for training the learning model and to achieve high accuracy.

Original languageEnglish
Article numbere0205796
Pages (from-to)1-16
Number of pages16
JournalPLoS ONE
Issue number10
Publication statusPublished - 22 Oct 2018
Externally publishedYes


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