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Piyanun Harnpicharnchai,Janthima Jaresitthikunchai,Mintra Seesang,Sasitorn Jindamorakot,Sutipa Tanapongpipat,Supawadee Ingsriswang 한국미생물·생명공학회 2020 한국미생물·생명공학회지 Vol.48 No.2
Various microorganisms play important roles in food fermentation, food spoilage, and agriculture. In this study, the biotype of 54 yeast and bacterial strains having high potential for utilization in food and agriculture, including Candida spp., Lactobacillus spp., and Acetobacter spp., were characterized by matrixassisted laser desorption/ionization time-of flight mass spectrometry (MALDI-TOF MS). This characterization using a fast and robust method provides much-needed information on the selected microorganisms and will facilitate effective usage of these strains in various applications. Importantly, the unique protein profile of each microbial species obtained from this study was used to create a database of fingerprints from these species. The database was validated using microbial strains of the same species by comparing the mass spectra with the created database through pattern matching. The created reference database provides crucial information and is useful for further utilization of a large number of valuable microorganisms relevant to food and agriculture.
( Asano Krisana ),( Sriprang Rutchadaporn ),( Gobsuk Jarupan ),( Eurwilaichitr Lily ),( Tanapongpipat Sutipa ),( Kirtikara Kanyawim ) 생화학분자생물학회 2005 BMB Reports Vol.38 No.1
During the screening of xylanolytic enzymes from locally isolated fungi, one strain BCC14405, exhibited high enzyme activity with thermostability. This fugal strain was identified as Aspergillus cf. niger based on its morphological characteristics and internal transcribed spacer (ITS) sequences. An enzyme with xylanolytic activity from BCC14405 was later purified and characterized. It was found to have a molecular mass of ca. 21 kDa, an optimal pH of 5.0, and an optimal temperature of 55℃. When tested using xylan from birchwood, it showed K_(m) and V_(max) values of 8.9 mg/ml and 11,100 U/mg, respectively. The enzyme was inhibited by CuSO₄, EDTA, and by FeSO₄. The homology of the 20-residue N-terminal protein sequence showed that the enzyme was an endo-1,4-β-xylanase. The full-length gene encoding endo-1,4-β-xylanase from BCC14405 was obtained by PCR amplification of its cDNA. The gene contained an open reading frame of 678 bp, encoding a 225 amino acid protein, which was identical to the endo-1,4-a^-xylanase B previously identified in A. niger.
Harnpicharnchai, Piyanun,Jaresitthikunchai, Janthima,Seesang, Mintra,Jindamorakot, Sasitorn,Tanapongpipat, Sutipa,Ingsriswang, Supawadee The Korean Society for Microbiology and Biotechnol 2020 한국미생물·생명공학회지 Vol.48 No.2
Various microorganisms play important roles in food fermentation, food spoilage, and agriculture. In this study, the biotype of 54 yeast and bacterial strains having high potential for utilization in food and agriculture, including Candida spp., Lactobacillus spp., and Acetobacter spp., were characterized by matrix-assisted laser desorption/ionization time-of flight mass spectrometry (MALDI-TOF MS). This characterization using a fast and robust method provides much-needed information on the selected microorganisms and will facilitate effective usage of these strains in various applications. Importantly, the unique protein profile of each microbial species obtained from this study was used to create a database of fingerprints from these species. The database was validated using microbial strains of the same species by comparing the mass spectra with the created database through pattern matching. The created reference database provides crucial information and is useful for further utilization of a large number of valuable microorganisms relevant to food and agriculture.
Thermostable Xylanase from Marasmius sp.: Purification and Characterization
Ratanachomsri, Ukrit,Sriprang, Rutchadaporn,Sornlek, Warasirin,Buaban, Benchaporn,Champreda, Verawat,Tanapongpipat, Sutipa,Eurwilaichitr, Lily Korean Society for Biochemistry and Molecular Biol 2006 Journal of biochemistry and molecular biology Vol.39 No.1
We have screened 766 strains of fungi from the BIOTEC Culture Collection (BCC) for xylanases working in extreme pH and/or high temperature conditions, the so-called extreme xylanases. From a total number of 32 strains producing extreme xylanases, the strain BCC7928, identified by using the internal transcribed spacer (ITS) sequence of rRNA to be a Marasmius sp., was chosen for further characterization because of its high xylanolytic activity at temperature as high as $90^{\circ}C$. The crude enzyme possessed high thermostability and pH stability. Purification of this xylanase was carried out using an anion exchanger followed by hydrophobic interaction chromatography, yielding the enzyme with >90% homogeneity. The molecular mass of the enzyme was approximately 40 kDa. The purified enzyme retained broad working pH range of 4-8 and optimal temperature of $90^{\circ}C$. When using xylan from birchwood as substrate, it exhibits $K_m$ and $V_{max}$ values of $2.6{\pm}0.6\;mg/ml$ and $428{\pm}26\;U/mg$, respectively. The enzyme rapidly hydrolysed xylans from birchwood, beechwood, and exhibited lower activity on xylan from wheatbran, or celluloses from carboxymethylcellulose and Avicel. The purified enzyme was highly stable at temperature ranges from 50 to $70^{\circ}C$. It retained 84% of its maximal activity after incubation in standard buffer containing 1% xylan substrate at $70^{\circ}C$ for 3 h. This thermostable xylanase should therefore be useful for several industrial applications, such as agricultural, food and biofuel.
Theppanya Charoenrat,Kanyalak Sangprapai,Peerada Promdonkoy,Kanokarn Kocharin,Sutipa Tanapongpipat,Niran Roongsawang 한국생물공학회 2015 Biotechnology and Bioprocess Engineering Vol.20 No.2
Control of the methanol supply during the production stage is a crucial parameter for maintaining cell growth and enhancing recombinant protein production by Pichia pastoris. In this study, optimization of the initial specific methanol supply rate was explored for high cell density fed-batch cultivation of recombinant fungal β- glucosidase in a slow methanol utilization strain (MutS), P. pastoris KM71. By varying the methanol feed rates for initiating the induction at a cell concentration of 60 g/L, the optimum initial specific methanol supply rate was determined to be 30.34 ± 0.34 mg/g·h. A methanol feed rate was proposed according to this optimum parameter and applied for the production of recombinant β-glucosidase at the higher cell concentrations of 80 and 100 g/L. The highest recombinant β-glucosidase activity obtained was 2851.7 ± 14.6 U/mL, which was four times higher than that obtained with the reference condition (40 g/L initial cell concentration). The success of this approach suggests that the strategy of optimizing the initial specific methanol supply rate could be adopted and applied for the production of other recombinant proteins in P. pastoris employing a methanol inducible system.
Krisana, Asano,Rutchadaporng, Sriprang,Jarupan, Gobsuk,Lily, Eurwilaichitr,Sutipa, Tanapongpipat,Kanyawim, Kirtikara Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.1
During the screening of xylanolytic enzymes from locally isolated fungi, one strain BCC14405, exhibited high enzyme activity with thermostability. This fugal strain was identified as Aspergillus cf. niger based on its morphological characteristics and internal transcribed spacer (ITS) sequences. An enzyme with xylanolytic activity from BCC14405 was later purified and characterized. It was found to have a molecular mass of ca. 21 kDa, an optimal pH of 5.0, and an optimal temperature of $55^{\circ}C$. When tested using xylan from birchwood, it showed $K_m$ and $V_{max}$ values of 8.9 mg/ml and 11,100 U/mg, respectively. The enzyme was inhibited by $CuSO_4$, EDTA, and by $FeSO_4$. The homology of the 20-residue N-terminal protein sequence showed that the enzyme was an endo-1,4-$\beta$-xylanase. The full-length gene encoding endo-1,4-$\beta$-xylanase from BCC14405 was obtained by PCR amplification of its cDNA. The gene contained an open reading frame of 678 bp, encoding a 225 amino acid protein, which was identical to the endo-1,4-$\^{a}$-xylanase B previously identified in A. niger.
Development of a Novel D-Lactic Acid Production Platform Based on Lactobacillus saerimneri TBRC 5746
Sansatchanon Kitisak,Sudying Pipat,Promdonkoy Peerada,Kingcha Yutthana,Visessanguan Wonnop,Tanapongpipat Sutipa,Runguphan Weerawat,Kocharin Kanokarn 한국미생물학회 2023 The journal of microbiology Vol.61 No.9
D-Lactic acid is a chiral, three-carbon organic acid, that bolsters the thermostability of polylactic acid. In this study, we developed a microbial production platform for the high-titer production of D-lactic acid. We screened 600 isolates of lactic acid bacteria (LAB) and identified twelve strains that exclusively produced D-lactic acid in high titers. Of these strains, Lactobacillus saerimneri TBRC 5746 was selected for further development because of its homofermentative metabolism. We investigated the effects of high temperature and the use of cheap, renewable carbon sources on lactic acid production and observed a titer of 99.4 g/L and a yield of 0.90 g/g glucose (90% of the theoretical yield). However, we also observed L-lactic acid production, which reduced the product’s optical purity. We then used CRISPR/dCas9-assisted transcriptional repression to repress the two Lldh genes in the genome of L. saerimneri TBRC 5746, resulting in a 38% increase in D-lactic acid production and an improvement in optical purity. This is the first demonstration of CRISPR/dCas9-assisted transcriptional repression in this microbial host and represents progress toward efficient microbial production of D-lactic acid.