KMITL

Permanent URI for this communityhttps://dspace.kmitl.ac.th/handle/kmitl/1

Browse

Search Results

Now showing 1 - 5 of 5
  • Some of the metrics are blocked by your 
    Item type:Publication,
    Sulphation and hydrolysis improvements of bioactivities, and immuno-modulatory properties of edible amanita hemibapha subspecies javanica (Corner and bas) mucilage polysaccharide as a potential in personalized functional foods
    (2021-10-01)
    Surayot, Utoomporn
    ;
    Wangtueai, Sutee
    ;
    You, Sangguan
    ;
    Techapun, Charin
    ;
    Phimolsiripol, Yuthana
    In this study, the mucilage polysaccharide (MP) from Amanita hemibapha subspecies javanica was prepared by hot water extraction and ethanol precipitation and then fractionated using anion-exchange chromatography equipped with a DEAE Sepharose fast flow column. The most immune-enhancing polysaccharide fraction 2 (MPF2) was subjected to a structural modification such as hydrolysis or over-sulphation. The sulphate and molecular weight (Mw) of over-sulphated (OS1-3) and hydrolysed (HS1-3) derivatives of MPF2 differed between 9.85% and 14.2% and 32.8 and 88.1 × 10<sup>3</sup> g/mol, respectively. Further, the immune-enhancing properties of MPF2 and its derivatives were tested on RAW264.7 and NK cells through various in vitro assays. Interestingly, a low molecular weight of HS1-3 significantly increased the nitric oxide (NO) production (p < 0.05) more than MPF2, indicating that Mw is a major factor in RAW264.7 cell stimulation. In addition, RAW264.7 cells produced various cytokines by up-regulating mRNA expression levels and the activation of nuclear factor kappa-B (NF-κB) and mitogen-activated protein kinase (MAPK) pathways. On the other hand, OS1-3-treated natural killer (NK) cells induced cytotoxicity in HepG2 cells through the expression of IFN-γ, Grandzyme-B, perforin, NKp30, and FasL. These results demonstrated that sulphate derivatives play an important role in NK cell activation. Further, this study also explores how polysaccharide binds to RAW264.7 and NK cells. MPF2 and HS3 may activate RAW264.7 cells via binding to TLR4 receptors, and OS2 could be activated through the CR3 signalling pathways.
      1
  • Some of the metrics are blocked by your 
    Item type:Publication,
    Extraction, structural characterisation, and immunomodulatory properties of edible amanita hemibapha subspecies javanica (Corner and bas) mucilage polysaccharide as a potential of functional food
    (2021-08-01)
    Surayot, Utoomporn
    ;
    Wangtueai, Sutee
    ;
    You, Sangguan
    ;
    Palanisamy, Subramnaian
    ;
    Krusong, Warawut
    This research aimed to extract mucilage polysaccharides (MP) from Amanita hemibapha subspecies javanica (Corner and Bas), and further fractionate them using anion-exchange chromatography, yielding two fractions (MPF1 and MPF2). The crude extract, and fractions mainly consisted of carbohydrates (83.5–93.2%) with minor amounts of proteins (5.40–7.20%), and sulphates (1.40–9.30%). Determination of the monosaccharide composition revealed that glucose was the major unit, followed by galactose, mannose, rhamnose, and arabinose. The average molecular weight (MW) of the crude extract and fractions was in the range 104.0–479.4 × 10<sup>3</sup> g/mol. Interestingly, the crude extract, and fractions did not cause any toxic effect in RAW264.7 cells. However, they stimulated the RAW264.7 cells to release nitric oxide and cytokines through the activation of nuclear factor-kappa B (NF-κB), and mitogen-activated protein kinase (MAPK) pathways via cell surface TLR4. Structural analysis of the most immunestimulating extract fraction, MPF2, revealed that the main backbone consisted of α-D-(1→6)-glucopyranoside. These results suggest that the MPs derived from A. hemibapha subspecies javanica (Corner and Bas) are potent in enhancing immunity; hence, they can be used as a functional ingredient in food products.
      1
  • Some of the metrics are blocked by your 
    Item type:Publication,
    Kinetic parameters of Candida tropicalis TISTR 5306 for ethanol production process using an optimal enzymatic digestion strategy of assorted grade longan solid waste powder
    (2019-11-01)
    Wattanapanom, Saengkae
    ;
    Muenseema, Jidapa
    ;
    Techapun, Charin
    ;
    Jantanasakulwong, Kittisak
    ;
    The optimal enzymatic digestion strategy for assorted grade whole fruit longan solid waste powder (WF–LSWP) to release the highest level of fermentable sugars for subsequent production of ethanol using Candida tropicalis TISTR 5306 has been reported for the first time in this study with several important fermentation kinetic parameters. WF–LSWP contained relatively low lignin content (5.79 ± 0.43 %(w/w)) with the presence of relatively high starch and pectin contents of 27.9 ± 0.86% (w/w) and 2.07 ± 0.16% (w/w), respectively. Pretreatment by alkali and saturated steam before enzymatic digestion step did not result in the improvement of overall sugars being released. The implementation of commercial enzyme mixture (amylase, glucoamylase, cellulase, and xylanase) for one step enzymatic digestion at 50°C for 48 h resulted in the statistical significantly highest (p ≤ 0.05) specific overall sugars productivity of (141 ± 1.4) × 10<sup>–4</sup> g total sugars/g WF–LSWP/digestion step/h. Cultivation of C. tropicalis TISTR 5306 in digested and concentrated WF–LSWP extract at concentration level of 90 g/l during 0 – 12 h resulted in the following statistical significantly highest (p ≤ 0.05) kinetic parameters; specific growth rate (m) of 0.097 ± 0.001 h<sup>–1</sup> and specific ethanol production rate (q<inf>P</inf>) of 0.221 ± 0.010 gP/gX/h. Dried biomass yield (Y<inf>X/S</inf>) and ethanol yield (Y<inf>P/S</inf>) based on utilized sugars of 90 g/l WF–LSWP extract at 0.180 ± 0.018 gX/gS and 0.411 ± 0.044 gP/gS, respectively, were statistical significantly highest (p ≤ 0.05) in comparison with those of 16 and 45 g/l WF–LSWP extracts.
  • Some of the metrics are blocked by your 
    Item type:Publication,
    Development of mathematical model for pyruvate decarboxylase deactivation kinetics by benzaldehyde with inorganic phosphate activation effect
    (2018-05-01)
    Khemacheewakul, Julaluk
    ;
    Techapun, Charin
    ;
    Kuntiya, Ampin
    ;
    ;
    Chaiyaso, Thanongsak
    The effect of phosphate concentrations at 20, 250, 500, and 1,000 mM on phenylacetylcarbinol (PAC) production, pyruvate decarboxylase (PDC) deactivation kinetics, and combination of phosphate activation effect in a mathematical model were evaluated in a biotransformation system using whole cells of Candida tropicalis TISTR 5350. This is the first report of phosphate activation effect on pyruvate decarboxylase deactivation model. The highest PAC concentration (28.6 ± 2.3 mM), average instantaneous PAC formation rate (0.57 ± 0.01 mM/min), PAC yields (0.95 ± 0.08 on benzaldehyde and 0.71 ± 0.06 on pyruvate) were achieved in 1,000 mM phosphate buffer. PDC volumetric activity of 0.52 ± 0.07 U carboligase/ml at the reaction time of 180 min was obtained. The mathematical model describing deactivation kinetics of whole cells PDC by benzaldehyde with activation effect for phosphate buffer concentration level predicted individual experimental data for all four levels of phosphate buffer relatively well with corresponding residual sum of square (RSS), mean square (MS), and correlation coefficient (R<sup>2</sup>) range of 213-1,100, 5.32-27.5, and 0.96-0.99. The activation effect of 1,000 mM phosphate buffer was evident with an average enzyme activation rate constant due to buffering species concentration level (K<inf>a</inf>) of 1.34 × 10<sup>-2</sup> % min<sup>-1</sup> which was higher than 20 mM phosphate buffer (1.48 × 10<sup>-6</sup> % min<sup>-1</sup>) by more than 9,050 times.
  • Some of the metrics are blocked by your 
    Item type:Publication,
    Partial purification and comparison of precipitation techniques of pyruvate decarboxylase enzyme
    (2017-01-01)
    Tangtua, Julaluk
    ;
    Techapun, Charin
    ;
    Pratanaphon, Ronachai
    ;
    Kuntiya, Ampin
    ;
    The intracellular pyruvate decarboxylase enzyme (PDC, EC 4.1.1.1) extract from Candida tropicalis TISTR 5350 was compared by two different purification methods using ammonium sulphate and acetone precipitation. The total volumetric PDC activity and percentage recovery (yield) of precipitated PDC based on 50% (v/v) cold acetone were significantly higher (1.13 ± 0.02 U/ml and 98.27 ± 2.98 %, respectively) than any other concentration levels of acetone used. Furthermore, all concentration levels of cold acetone also yielded a much higher specific PDC activity than the precipitate obtained using the 40 to 60% (w/v) ammonium sulphate saturation (0.75 ± 0.08 U/mg protein). The precipitated enzyme in buffer solutions from the 50% (v/v) acetone was subsequently freeze dried. Freeze drying of the precipitated PDC by cold acetone resulted in the specific PDC activity of 1.57 ± 0.02 U/mg protein and differed statistically (p ≤ 0.05) from the crude enzyme extract (control).
      1