Philippine Journal of Science
152 (1): 109-124, February 2023
ISSN 0031 – 7683
Date Received: 22 Jul 2022

Alkalihalobacillus lehensis M136, a Novel Alkaliphilic,
Cyclodextrin Glucanotransferase (CGTase)-producing
Isolate from Manleluag Hyperalkaline
Spring in Pangasinan, Philippines

Eula Francia M. Bosito1,2*, Andrew D. Montecillo1, Rose Ann G. Franco1,4, Noel G. Sabino1,
Aryana Lee G. Bertuso1,3, Bernadette C. Mendoza1, and Nacita B. Lantican1*

1Institute of Biological Sciences, University of the Philippines Los Baños,
College, Laguna 4031, Philippines
2National Institute of Molecular Biology and Biotechnology,
University of the Philippines Los Baños, College, Laguna 4031, Philippines
3Institute of Biology, University of the Philippines Diliman,
Diliman, Quezon City 1101, Philippines
4Centre for Biomedical Technologies, School of Mechanical, Medical, and Process Engineering,
Faculty of Engineering, Queensland University of Technology (QUT), Brisbane 4000 Australia

*Corresponding author:
embosito@up.edu.ph; nblantican@up.edu.ph

[Download]
Bosito EF et al. 2023. Alkalihalobacillus lehensis M136, a Novel Alkaliphilic, Cyclodextrin
Glucanotransferase (CGTase)-producing Isolate from Manleluag Hyperalkaline
Spring in Pangasinan, Philippines. Philipp J Sci 152(1): 109–124.
https://doi.org/10.56899/152.01.08

 

 

ABSTRACT

A cyclodextrin glucanotransferase (CGTase)-producing bacterium was isolated from Manleluag hyperalkaline spring, Pangasinan, the first to be reported from a hyperalkaline environment in the Philippines. The isolate, M136, had the highest CGTase enzyme activity (46.01 U/mL) out of the forty-one similar bacterial isolates and exceeds the CGTase activity of the reference strain, Paenibacillus sp. JCM 9143. Using whole genome analysis, M136 was identified as Alkalihalobacillus lehensis. The CGTase enzyme produced by Alkalihalobacillus lehensis M136 was partially purified with 73.97% recovery and post-purification activity of 49.52 U/mL. The enzyme has an estimated molecular weight of 78.64 kDa and an isoelectric point of 4.72. Enzyme characterization revealed that it was stable at 30–80 °C (optimal activity at 70 °C), pH 4.0–10.0 (optimal activity at pH 6.0), and in the presence of different metal ions and reagents such as zinc, calcium, magnesium, and manganese, ethylenediaminetetraacetic acid, iodoacetic acid, sodium dodecyl sulfate, and phenylmethylsulfonyl fluoride.