Screening of Potential Bioremediation Enzymes from Hot Spring Isolates and Characterization of Amylase Protein Sequences of Bacteria and Fungi: An In Silico Study

Abstract Survival and average body weight of Litopenaeus vannamei after application of Bacillus barbaricus SSB-119 in 111-day culture experiments was increased compared with the control pond shrimps. Application of SSB-119 was scheduled in three different phases, first 40 days (5 L/ha), second 40 da...

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Veröffentlicht in:Journal of hazardous, toxic and radioactive waste toxic and radioactive waste, 2020-10, Vol.24 (4)
Hauptverfasser: Raut, Sangeeta, Satpathy, Soumya, Sen, Sudip Kumar
Format: Artikel
Sprache:eng
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Zusammenfassung:Abstract Survival and average body weight of Litopenaeus vannamei after application of Bacillus barbaricus SSB-119 in 111-day culture experiments was increased compared with the control pond shrimps. Application of SSB-119 was scheduled in three different phases, first 40 days (5 L/ha), second 40 days (10 L/ha), and end of the experiment (15 L/ha). The average shrimp survival rate was notably poorer, 59.1% ± 1.5% and 66.8% ± 2.1% in the control ponds C-1 and C-2 (P < 0.001), respectively. Significant variances (P < 0.05) in the animals average weight between the experiment (35.21 g ± 0.1 g in T-1 and 34.26 g ± 0.1 g in T-2) and control (27.18 g ± 0.1 g in C-1 and 29.08 g ± 0.1 g in C-2) groups were seen in the statistical analysis. The amylase protein sequences of 84 microorganisms were obtained from the database of National Center for Biotechnology Information (NCBI). To reveal the evolutionary relationship between them, multiple sequence alignment and a phylogenetic tree were constructed. The functional motifs and domains of the protein sequences were also detected. Three motifs are present in each bacterial and fungal family. Bacterial motifs were of alpha-amylase protein and motifs from fungal protein sequences were of fungal lignin peroxidase protein sequence representing their role in the fundamental and catalytic attributes of lignin peroxidase.
ISSN:2153-5493
2153-5515
DOI:10.1061/(ASCE)HZ.2153-5515.0000524