Maneeruttanarungroj, Cherdsak

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Ethanol-enhanced biohydrogen production and metabolomic response in the green microalga Micractinium sp. KLSc62
(2025-02-17)
Klinsalee, Rachaneekorn
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Laokua, Natwikar
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Rittiyan, Nutnicha
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Kornrawudaphikasama, Yosita
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Tonawut, Yothawut
Hydrogen (H<inf>2</inf>) is recognized as a viable clean energy option due to its high energy density and minimal environmental impact. Green microalgae have garnered attention as a potential source of hydrogen production because of their ability to produce photosynthetic hydrogen and their environmental benefits. In a recent study, thirteen species of microalgae were screened for their growth potential and hydrogen production when supplemented with ethanol. Among the species evaluated, Micractinium sp. KLSc62 (initially named as G4) yielded the highest hydrogen production rate of 6090.5 ± 28.6 μmol mg⁻<sup>1</sup> Chl with the supplementation of 30 mM ethanol over a 7-day period. Further analysis revealed that ethanol was utilized during H<inf>2</inf> production process, leading to the formation of acetaldehyde as an intermediate before acetate was produced. Metabolic profiling identified 44 metabolites that were up- or down-regulated, categorized into four distinct groups. These findings highlight the potential of Micractinium sp. KLSc62 as an alternative energy producer and a promising candidate for future metabolite production in various chemical applications, emphasizing its utility as a cellular factory.
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In silico encrypted peptide from green alga Tetraspora sp. CU2551 showed high antimicrobial activities
(2024-03-01)
Tonawut, Yothawut
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Rittiyan, Nutnicha
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Kornrawudaphikasama, Yosita
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Klinsalee, Rachaneekorn
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Laokua, Natwikar
The green alga Tetraspora sp. CU2551 has been previously identified as a biohydrogen producer for an alternative option for sustainable energy production development. Its biomass still contains a source of valuable biomolecules, especially proteins. Crude algal protein showed significant antimicrobial activity against Gram-positive bacteria (Bacillus subtilis TISTR 1248 and Staphylococcus aureus TISTR 746) and Gram-negative bacteria (Escherichia coli TISTR 074 and Pseudomonas aeruginosa TISTR 2370), representing a clear zone of 19.0 ± 0.1, 18.3 ± 0.5, 17.7 ± 0.5, and 19.0 ± 0.5, respectively. Further investigation revealed that encrypted peptides from pepsin-hydrolyzed crude proteins increased the inhibition activity against these bacteria by 3.4–10.5 %. The hydrolyzed peptides were fractionated using a Sephadex G-25 column, and peptides in fraction 17 showed the highest antimicrobial activity. Through peptide identification using LC-MS and prediction of obtained peptide primary sequences with four bioinformatic tools (DBAASP, AMPDiscover, iAMPpred, and AMPscanner), five peptides were selected and synthesized for activity evaluation. The PT11 peptide (RYGAAMAVGIACA) demonstrated the highest antimicrobial activity among the five peptides tested and compared favorably to previously reported algal encrypted peptides. The findings of this research demonstrate that the encrypted PT11 peptide derived from Tetraspora sp. CU2551 has promising potential as an antimicrobial agent. Additionally, we suggest that PT11 might be used for other things besides this, like animal feed.
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Hydrochloric acid producing higher purity of glucosamine than sulfuric acid: A comparison study with different detection approaches
(2024-06-01)
Kornrawudaphikasama, Yosita
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Laokua, Natwikar
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Rittiyan, Nutnicha
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Klinsalee, Rachaneekorn
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Tonawut, Yothawut
In this study, HCl and H<inf>2</inf>SO<inf>4</inf> were used to compare the best conditions for producing glucosamine from the dry chitin of shrimp shells. The results showed that for HCl hydrolysis, the most favored conditions were 12 M, 80 °C, 2 hours, and a chitin-to-acid volume ratio of 1:20, whereas, for H<inf>2</inf>SO<inf>4</inf> hydrolysis, the most favored conditions were 6 M, 90 °C, 5 hours, and a chitin to acid volume ratio of 1:20. HCl produced pured glucosamine with a higher yield than H<inf>2</inf>SO<inf>4</inf>. Additionally, our findings indicated that glucosamine could be detected using a UV detector with a weak signal, whereas we recommended using an RI detector for a comparably stronger signal. Our production maximum yield of 283.9 ± 13.8 mg Gln g<sup>-1</sup> chitin from HCl hydrolysis was comparable to that of other studies, with a comparison between using HCl and H<inf>2</inf>SO<inf>4</inf> being highlighted.
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Purification, characterization, and structural insights of Exo-1,4-β-D-glucosaminidase from Amycolatopsis sp. KLSc63: predictive modeling with glucosamine and N-acetyl glucosamine dimers
(2026-12-01)
Kornrawudaphikasama, Yosita
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Maneeruttanarungroj, Cherdsak
Chitin, a long-chain polysaccharide, is a major component in the exoskeletons of arthropods and the cell walls of fungi. Its derivative, chitosan, is widely used in various fields due to its solubility and versatility. This study focuses on the purification and biochemical characterization of exo-1,4-β-D-glucosaminidase from Amycolatopsis sp. KLSc63, an enzyme crucial for the degradation of chitin and chitosan. The enzyme was purified using anion exchange chromatography and characterized for its activity on colloidal chitin and chitosan solutions. Optimal activity was observed at pH 5.0 and temperatures of 40–45 °C for colloidal chitin and pH 4.0–6.0 at 55 °C for chitosan solution. The enzyme’s molecular weight was approximately 94 kDa. Various metal ions and surfactants significantly influenced enzyme activity, with Mn²⁺ at 1 mM concentration notably enhancing both activities. Structural modeling and docking studies confirmed the enzyme’s substrate specificity and binding interactions. These findings highlight the potential applications of exo-1,4-β-D-glucosaminidase in industrial processes, waste management, and the production of bioactive compounds.

Maneeruttanarungroj, Cherdsak

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