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All Journal Journal of Tropical Life Science : International Journal of Theoretical, Experimental, and Applied Life Sciences
Samsulrizal, Nurul HIdayah
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Agriculture, Biological Sciences & Forestry Environmental Science

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Identification and characterization of a 2,2-dichloropropionic acid (2,2-DCP) degrading alkalotorelant bacterium strain BHS1 isolated from Blue Lake, Turkey Abdul Wahhab, Batool Hazim; Khairul Anuar, Nurul Fatin Syamimi; Abdul Wahab, Roswanira; Al Nimer, Marwan S.M.; Samsulrizal, Nurul HIdayah; Abdul Hamid, Azzmer Azzar; Edbeib, Mohamed Faraj; Kaya, Yilmaz; Huyop, Fahrul
Journal of Tropical Life Science Vol 10, No 3 (2020)
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/jtls.10.03.08

Abstract

An acid, 2,2-dichloropropionic acid (2,2-DCP) is an active ingredient in herbicide (Dalapon®). Using 2,2-DCP as a model substrate, an alkalotolerant bacterium was successfully isolated from the Blue Lake, Turkey. This bacterium is a potential bioremediation agent of recalcitrant xenobiotic halogenated compounds. This study aimed to prove the efficacy of the alkalotolerance Bacillus megaterium BHS1 in degrading 2,2-DCP as the sole source of carbon. Biolog GEN III system and 16S rRNA analysis were used for the identification of the bacterium. It was discovered that the strain BHS1 is Bacillus megaterium, and the bacterium that was observed to thrive in alkaline conditions (pH 7.0−14.0), supplemented with varying concentrations of 2,2-DCP (from 20 to 60 mM). Growth of strain BHS1 was exceptional in 40 mM of 2,2-DCP at pH 9, corresponding to a cell doubling time of 17.7 hour, whereas was fully inhibited at 50 mM 2,2-DCP. Since halogenated pollutants can make their way into highly alkaline environments, therefore, identifying threshold levels of strain BHS1 with respect to alkaline-tolerance and maximum level of 2,2-DCP may prove pertinent. This is to ensure that an optimal environment is created for the bacteria to degrade 2,2-DCP-contaminated water. In addition, this is the first study exploring a Bacillus species isolated from an alkaline environment adept in utilizing 2,2-DCP as a sole source of carbon. Hence, the ability of this strain to degrade other types of haloalkanoic acids constitutes a worthy future study.
In silico Characterization of UGT74G1 Protein in Stevia rebaudiana Bertoni Accession MS007 Khan, Afiqah Rahmatullah; Mokhtar, Nor Iwani; Zainuddin, Zarina; Samsulrizal, Nurul Hidayah
Journal of Tropical Life Science Vol 11, No 3 (2021)
Publisher : Journal of Tropical Life Science

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Abstract

Stevia rebaudiana is being promoted as an alternative sweetener in particular for diabetic and obese patients due to its low-calorie property. The steady demand in the market for high-quality stevia extracts presents a challenge for enhanced production of steviol glycosides that are safe for human consumption. This study characterized the structure and content of gene involved in the production of UGT74G1 protein for S. rebaudiana accession MS007 through in silico analysis using transcriptome dataset of stevia MS007.  Homologous search using BLASTp show high similarity to Q6VAA6 RecName: Full=UDP-glycosyltransferase 74G1 (S. rebaudiana) as the top hit sequences. InterPro family and domain protein motif search revealed the presence and entry of IPR002213 and IPR035595. The construction of the phylogenetic tree was done by selecting 19 out of 102 protein sequences from BLASTp. The phylogenetic analysis showed the same protein family which is Asteraceae. ProtParam Ex-Pasy, PSIPRED and Phyre2 computed the primary, secondary, and tertiary structures for UGT74G1 protein. The UGT74G1 predicted tertiary structure scored 100.0% confidence by the single highest scoring template and coverage of 96%. The model has dimensions (Å) of X: 57.609, Y: 70.386, and Z: 58.351. Outcomes of this research will help to enhance the understanding of UDP-glycosyltransferase 74G1 (S. rebaudiana MS007) characteristic and enhance target identification processes to improve understanding of protein-protein interaction in S. rebaudiana MS007.
Co-Authors Abdul Hamid, Azzmer Azzar Abdul Wahab, Roswanira Abdul Wahhab, Batool Hazim Al Nimer, Marwan S.M. Edbeib, Mohamed Faraj Huyop, Fahrul Kaya, Yilmaz Khairul Anuar, Nurul Fatin Syamimi Khan, Afiqah Rahmatullah Mokhtar, Nor Iwani Zainuddin, Zarina