Maneeruttanarungroj, Cherdsak

Preferred name

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School of Science

cherdsak.ma@kmitl.ac.th

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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⁻1 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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Purification and Identification of Antimicrobial Protein from the Green Alga Tetraspora Sp. CU2551
(2026-02-01)
Klinsanit, Tanaporn
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Tonawut, Yothawut
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Laokua, Natwikar
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Pansomsuay, Rawirat
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Khetkorn, Wanthanee
Antimicrobial resistance (AMR) is an escalating global health threat, necessitating the discovery of novel antimicrobial agents. Algae-derived proteins and peptides have gained increasing attention for their bioactive potential; however, standardized protocols for investigating antimicrobial peptides (AMPs) in green algae, particularly Tetraspora sp. CU2551, remain limited. This protocol describes a step-by-step workflow for the isolation, purification, and characterization of antimicrobial intact proteins from the green alga Tetraspora sp. CU2551. The procedure integrates optimized protein extraction, chromatographic fractionation, electrophoretic separation, antimicrobial activity screening, and protein identification. Protein extraction conditions are first optimized to reduce background inhibitory effects originating from buffer components. When the identity of the active peptide is unknown, a pull-down assay is applied to assess protein binding across different ion-exchange resins and to guide the selection of an appropriate purification matrix. DEAE-Sepharose ion-exchange chromatography is a suitable method for enriching antimicrobial protein fractions. All fractions are systematically evaluated for antimicrobial activity and analyzed by SDS-PAGE. The protein band corresponding to the highest antimicrobial activity, along with a distinct electrophoretic profile, is excised and subjected to LC-MS/MALDI-TOF analysis for protein identification. The workflow is further complemented by in silico analyses to predict antimicrobial peptide-related properties using publicly available bioinformatic tools. This protocol provides a versatile framework for antimicrobial protein discovery and can be readily adapted to other algal species and related biotechnological applications.
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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-1 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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Optimal conditions for maximized H2 yield from a new green algal strain Chlorella sp. KLSc61
(2022-08-01)
Laokua, Natwikar
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Rittiyan, Nutnicha
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Kornrawudaphikasama, Yosita
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Klinsalee, Rachaneekorn
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Tonawut, Yothawut
Hydrogen produced from microalgae is attracting the attention of scientists as a potential new ‘Bio-Circular-Green’ energy source. We screened a selection of naturally occurring algal strains for H<inf>2</inf> yield as a basis for high yield development. The best strain was a new strain of biohydrogen-producing green algae from a fresh water source at King Mongkut's Institute of Technology Ladkrabang, Thailand. Using morphological and 18S rDNA sequencing analyses, this alga was identified and classified as Chlorella sp. KLSc61. When adapted cells in TAP-K medium (with starting pH at 9.0) containing 25 mM ethanol, with 54 μmol photons m−2 s−1 light, and incubated at 35 °C, Chlorella sp. KLSc61 showed a maximum H<inf>2</inf> yield of 9,804 ± 469.5 μmol H<inf>2</inf> mg−1 Chl at day 7. Under these conditions, the cells produced ~ 12.2 times more H<inf>2</inf> gas than without optimization (753.0 μmol H<inf>2</inf> mg−1Chl). Our optimized system also produced H<inf>2</inf> at a rate 11–570 times greater than previously reported microalgae. Thus Chlorella sp. KLSc61 could be a viable strain for biohydrogen production as a clean future energy source.
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Proteomic insights into high biohydrogen production by Chlorella sp. KLSc61 under potassium deprivation: upregulation of carbohydrate synthesis proteins
(2025-12-01)
Laokua, Natwikar
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Dejtisakdi, Wipawee
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Maneeruttanarungroj, Cherdsak
Microalgae produce hydrogen by utilizing light energy to split water molecules and this produced hydrogen is considered as a promising alternative energy resource. This study investigated the proteomic response of the microalga, Chlorella sp. KLSc61 under an optimal condition for increasing hydrogen production. Chlorella KLSc61 cells were cultured in potassium deprivation medium (TAP-K medium) with an initial pH of 9.0 and added 25 mM ethanol, they were cultivated and exposed to the light intensity of 54 μmol photons m−2 s−1 at 35 °C. By day 7, under this growth condition, Chlorella cells produced a maximum H<inf>2</inf> yield of 19,600 ± 0.3 mmol H<inf>2</inf> mg−1 chlorophyll, which was 2.5 times greater than that under normal TAP condition. Under an increase of hydrogen production, Chlorella KLSc61 cells were both round- and oval-shaped with an average cell diameter of 10.0 ± 0.5 μm, along with variations of chloroplast distribution within the cytoplasm, whereas Chlorella cells in normal TAP medium showed only round shape with an average cell diameter of 5.0 ± 0.5 μm. Proteins from cells grown under normal and high hydrogen conditions were subjected to proteomic analysis, with the results presented as a cluster heat map of proteomics profiles from five different conditions. A total of 736 protein expression patterns were classified into six different expressed protein groups, which included both up- and down-regulated proteins. Carbohydrate synthesis proteins, including starch synthase, glucose-6-phosphate isomerase, glycerol-3-phosphate dehydrogenase, phosphoglucomutase, and UDP-glucuronate decarboxylase, were abundant during the high H<inf>2</inf> production. These findings allow us to take the next step of those protein overexpression into Chlorella KLSc61 cells to enhance in vivo hydrogen production and this strain could be used as a hydrogen production platform.

Maneeruttanarungroj, Cherdsak

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