Jatupornpipat, Marisa

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Jatupornpipat, Marisa
Alternative Name
Jatupornpipat, M.
Email
marisa.ja@kmitl.ac.th

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    The family 36 carbohydrate-binding module of Paenibacillus xylaniclasticus TW1 xylanase: Characterization and recognition in epidermal tissue of sweet potato roots
    (2025-07-01)
    Tangthirasunun, N.
    ;
    Sornyotha, S.
    ;
    Jatupornpipat, M.
    Paenibacillus xylaniclasticus TW1 was able to aerobically produce a multienzyme complex. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the crude enzyme preparation revealed at least 12 proteins that were bound to insoluble cellulose. Only the band representing cellulose-bound protein 12 (CBP12) from SDS-PAGE was identified as xylanase family 11 with a carbohydrate-binding module family 36 (CBM36) using matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry (MALDI-TOF/TOF MS). In this report, CBM36 of P. xylaniclasticus TW1 (PxTW1CBM36) was cloned, expressed, purified and studied for binding characteristic. The results found that PxTW1CBM36 displayed broad binding ability to polysaccharides which high affinity for xylan and insoluble cellulose. Interestingly, this is the first report indicated that CBM36 had an affinity for insoluble cellulose. Although the amino acid residues involved in PxTW1CBM36 binding were conserved, the binding capacity of PxTW1CBM36 do not perturb by the addition of ethylenediaminetetraacetic acid (EDTA). It is possible that PxTW1CBM36 had different binding mechanisms with other CBM36. In addition, the binding characteristic of CBM36 on polysaccharides embedded within plant cell walls was also elucidated. It displayed the strong recognition for ligands located in epidermal tissue of sweet potato roots. Therefore, this study might provide a new tool for targeting enzymes to surface of plant.
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    Optimization, isolation, identification and molecular mechanisms in B16F10 melanoma cells of a novel tyrosinase inhibitory peptide derived from split gill mushrooms
    (2024-10-01)
    Arnamwong, Sarinya
    ;
    Kuptawach, Kittisak
    ;
    Sangtanoo, Papassara
    ;
    Srimongkol, Piroonporn
    ;
    Saisavoey, Tanatorn
    Hyperpigmentation often arises from an imbalance in melanogenesis, primarily due to the overexpression of tyrosinase (TYR). While the inhibition of TYR presents a common approach to skin whitening, it can lead to undesirable side effects. Thus, there is growing interest in safe and natural alternatives for TYR inhibition. Bioactive compounds and peptides sourced from split gill mushrooms hold promise in this regard. This study aims to optimize the conditions for papain-mediated hydrolysis of split gill mushroom protein to inhibit TYR activity, utilizing response surface methodology (RSM) and central composite design (CCD). Optimal conditions were determined at a temperature of 46.70 °C, a hydrolysis time of 217.09 min, and an enzyme-to-substrate ratio (E/S) of 1.1%. Under these conditions, the resulting hydrolysates exhibited significant TYR inhibition, with an IC<inf>50</inf> value of 117.86 μg/mL and a degree of hydrolysis (DH) of 87.97%. Further purification via ultrafiltration and RP-HPLC yielded a peptide, Tyr-Ala-Ser-Ile-Leu-Leu (YASILL or YL-6), identified through LC-Q-TOF-MS/MS, which competitively inhibited TYR. YL-6 demonstrated an IC<inf>50</inf> value of 3.97 mM for mono-phenolase activity and 6.75 mM for di-phenolase activity. Molecular docking analysis revealed hydrogen bonds and hydrophobic interactions between TYR and YL-6. Treatment of B16F10 cells with YL-6 across concentrations ranging from 10-3000 μM showed no cytotoxic effects.The inhibition of melanin synthesis was investigated via qRT-PCR along with Western blot in MITF, TYR, TRP-1, and TRP-2. The results obtained in this research may prove significant in guiding the development of commercially viable cosmetic products to whiten the skin.
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    Bee pollen peptides as potent tyrosinase inhibitors with anti-melanogenesis effects in murine b16f10 melanoma cells and zebrafish embryos
    (2024-12-01)
    Sangtanoo, Papassara
    ;
    Srimongkol, Piroonporn
    ;
    Saisavoey, Tanatorn
    ;
    Puthong, Songchan
    ;
    Buakeaw, Anumart
    One important functional food ingredient today, valued for its health properties and ability to prevent disease, is bee pollen, which comprises a combination of nectar, pollen from plants, and the secretions of bees. In this research, the tyrosinase (TYR) inhibiting abilities of the peptides derived from bee pollen protein hydrolysates are investigated. Various proteases were utilized to generate these peptides, followed by testing at different concentrations. Tyrosinase inhibition activity was detected in all cases, while the hydrolysate drawn from 5.0% w/v neutrase exhibited the best IC<inf>50</inf> value and was thus investigated further via ultrafiltration to separate the active fractions. The highest potential for tyrosinase inhibition was recorded for the fractions below 0.65 kDa. Subsequent purification steps via SEC and RP-HPLC led to the identification of the VDGYPAAGY (named VY-9) peptide via LC-Q-TOF-MS/MS in fraction F<inf>1–2</inf>, known for its non-toxic and hydrophobic characteristics albeit poor water solubility. The synthesized VY-9 peptide demonstrated competitive inhibition, with IC<inf>50</inf> values of 0.55 ± 0.03 µM for mono-phenolase and 2.54 ± 0.06 µM for di-phenolase activities, as confirmed by molecular docking analysis revealing dominant hydrogen bond interactions with TYR. Effective concentrations of 0.2–1.6 µM of VY-9 showed negligible cytotoxicity in B16F10 cells. Melanin synthesis suppression was examined via qRT-PCR, and western blot in MITF, TYR, TRP-1, and TRP-2. Cell death in zebrafish embryos was evaluated in vivo using a toxicity assay which revealed no significant influence from VY-9, while anti-melanogenic effects were observed when the concentration was 4 µM, suggesting bee pollen-derived peptides’ potential in cosmetic and pharmaceutical depigmentation applications.
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    Formulation Development of Serum Beads: Investigating the Influence of Sodium Alginate/Iota Carrageenan Ratio on Bead Characteristics
    (2024-05-01)
    Woraphokanunt, Yada
    ;
    Teeranachaideekul, Veerawat
    ;
    Rittiboon, Aree
    ;
    Jatupornpipat, Marisa
    Background and Objectives: To develop cosmetic products by using Ionic gelation techniques as the main technique in the production of serum beads. The purpose of this study is to develop the serum beads recipe by studying the ratio of various types of gelling agents for complete serum beads products. Methodology: Test the ratio of gelling agents in serums that create beads with ionic gelation techniques by Sodium Alginate and Iota-carrageenan which affect the appearance and beads texture after forming. Then compare the concentration of the gelling agent used in the suspension of serum beads that affects the ability to suspend serum beads. In this study, Carbopol® ultrez 20 was selected as the type of gelling agent. Main Results: The most suitable ratio for forming serum beads between Sodium Alginate and Iota-carrageenan is 0.20:0.30. Because the appearance of serum beads is spherical which can be pressed, cracked and spread on the surface easily-moderately, which is the most suitable characteristic for serum beads compared with the other ratios. When the serum beads were suspended inside the Carbopol® ultrez 20 gel at different concentrations and sensory tests, it was found that Carbopol® ultrez 20 at a concentration of 0.70 percent was the most favored. After storing in accelerated conditions to test the stability of the product, it was found that all concentrations of the gelling agent Carbopol® ultrez 20 could make the serum beads suspended and disperse inside the gel, but the viscosity was significantly reduced in each formulation. Conclusions: Conclusion: The ratio of Sodium Alginate and Iota-carrageenan affects the formation and hardness of beads. The most suitable ratio in this study is 0.20:0.30 and the gelling agent Carbopol® ultrez 20 at a concentration of 0. 70 percent is the most suitable choice for using as a suspension gel in the serum bead cosmetic formula. Because it is the most stable and has the least change when stored in accelerated condition for 8 weeks.