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Kazunobu Matsushita - One of the best experts on this subject based on the ideXlab platform.
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high temperature Sorbose fermentation with thermotolerant gluconobacter frateurii chm43 and its mutant strain adapted to higher temperature
Applied Microbiology and Biotechnology, 2012Co-Authors: Hiromi Hattori, Osao Adachi, Hirohide Toyama, Toshiharu Yakushi, Minenosuke Matsutani, Duantip Moonmangmee, Kazunobu MatsushitaAbstract:We succeeded in obtaining a strain adapted to higher temperature from a thermotolerant strain, Gluconobacter frateurii CHM43, for Sorbose fermentation. The adapted strain showed higher growth and l-Sorbose production than original CHM43 strain at higher temperature around 38.5–40 °C. It was also shown to be useful even with the fermentation without temperature control. To understand the Sorbose fermentation ability of the adapted strain at higher temperature, d-sorbitol-oxidizing respiratory chain was compared with the CHM43 strain and the adapted strain. We found that the activity of pyrroloquinoline quinone (PQQ)-dependent glycerol dehydrogenase (GLDH), which is a primary dehydrogenase of the respiratory chain and responsible for l-Sorbose production, was decreased when the temperature increased, but the decreased activity of GLDH was recovered by the addition of PQQ. Since the adapted strain was found to produce more PQQ than the CHM43 strain, it was suggested that the adapted strain keeps GLDH as holoenzyme with the increased PQQ production, and thus produces more l-Sorbose and grows better under higher temperature.
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purification crystallization and preliminary x ray analysis of l Sorbose reductase from gluconobacter frateurii complexed with l Sorbose or nadph
Acta Crystallographica Section F-structural Biology and Crystallization Communications, 2009Co-Authors: Keiko Kubota, Hirohide Toyama, Kazunobu Matsushita, Koji Nagata, Kenichi Miyazono, Masaru TanokuraAbstract:NADPH-dependent l-Sorbose reductase (SR) from Gluconobacter frateurii was expressed in Escherichia coli, purified and crystallized with l-Sorbose or NADPH using the sitting-drop vapour-diffusion method at 293 K. Crystals of the SR–l-Sorbose complex and the SR–NADPH complex were obtained using reservoir solutions containing PEG 2000 or PEG 400 as precipitants and diffracted X-rays to 2.38 and 1.90 A resolution, respectively. The crystal of the SR–l-Sorbose complex belonged to space group C2221, with unit-cell parameters a = 124.2, b = 124.1, c = 60.8 A. The crystal of the SR–NADPH complex belonged to space group P21, with unit-cell parameters a = 124.3, b = 61.0, c = 124.5 A, β = 89.99°. The crystals contained two and eight molecules, respectively, in the asymmetric unit.
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Purification, crystallization and preliminary X-ray analysis of L-Sorbose reductase from Gluconobacter frateurii complexed with L-Sorbose or NADPH.
Acta crystallographica. Section F Structural biology and crystallization communications, 2009Co-Authors: Keiko Kubota, Hirohide Toyama, Kazunobu Matsushita, Koji Nagata, Kenichi Miyazono, Masaru TanokuraAbstract:NADPH-dependent L-Sorbose reductase (SR) from Gluconobacter frateurii was expressed in Escherichia coli, purified and crystallized with L-Sorbose or NADPH using the sitting-drop vapour-diffusion method at 293 K. Crystals of the SR-L-Sorbose complex and the SR-NADPH complex were obtained using reservoir solutions containing PEG 2000 or PEG 400 as precipitants and diffracted X-rays to 2.38 and 1.90 A resolution, respectively. The crystal of the SR-L-Sorbose complex belonged to space group C222(1), with unit-cell parameters a = 124.2, b = 124.1, c = 60.8 A. The crystal of the SR-NADPH complex belonged to space group P2(1), with unit-cell parameters a = 124.3, b = 61.0, c = 124.5 A, beta = 89.99 degrees . The crystals contained two and eight molecules, respectively, in the asymmetric unit.
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l Sorbose reductase and its transcriptional regulator involved in l Sorbose utilization of gluconobacter frateurii
Journal of Bacteriology, 2007Co-Authors: Wichai Soemphol, Osao Adachi, Duangtip Moonmangmee, Hirohide Toyama, Kazunobu MatsushitaAbstract:Upstream of the gene for flavin adenine dinucleotide (FAD)-dependent d-sorbitol dehydrogenase (SLDH), sldSLC, a putative transcriptional regulator was found in Gluconobacter frateurii THD32 (NBRC 101656). In this study, the whole sboR gene and the adjacent gene, sboA, were cloned and analyzed. sboR mutation did not affect FAD-SLDH activity in the membrane fractions. The SboA enzyme expressed and purified from an Escherichia coli transformant showed NADPH-dependent l-Sorbose reductase (NADPH-SR) activity, and the enzyme was different from the NADPH-SR previously reported for Gluconobacter suboxydans IFO 3291 in molecular size and amino acid sequence. A mutant defective in sboA showed significantly reduced growth on l-Sorbose, indicating that the SboA enzyme is required for efficient growth on l-Sorbose. The sboR mutant grew on l-Sorbose even better than the wild-type strain did, and higher NADPH-SR activity was detected in cytoplasm fractions. Reverse transcription-PCR experiments indicated that sboRA comprises an operon. These data suggest that sboR is involved in the repression of sboA, but not in the induction of sldSLC, on d-sorbitol and that another activator is required for the induction of these genes by d-sorbitol or l-Sorbose.
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crystallization and properties of nadph dependent l Sorbose reductase from gluconobacter melanogenus ifo 3294
Bioscience Biotechnology and Biochemistry, 1999Co-Authors: Osao Adachi, Duangtip Moonmangmee, Emiko Shinagawa, Hirohide Toyama, Gunjana Theeragool, Napha Lotong, Kazunobu MatsushitaAbstract:NADPH-Dependent L-Sorbose reductase (SORD, synonimously NADP-dependent D-srobitol dehydrogenase) was purified and crystallized for the first time from the cytosolic fraction of Gluconobacter melanogenus IFO 3294. The enzyme catalyzed oxidoreduction between D-sorbitol and L-Sorbose in the presence of NADP or NADPH. Affinity chromatography by a Blue-dextran Sepharose 4B column was effective for purifying the enzyme giving about 770-fold purification with an overall yield of more than 50%. The crystalline enzyme showed a single sedimentation peak in analytical ultracentrifugation, giving an apparent sedimentation constant of 3.8 s. Gel filtration on a Sephadex G-75 column gave the molecular mass of 60 kDa to the enzyme, which dissociated into 30 kDa subunit on SDS-PAGE, indicating that the enzyme is composed of 2 identical subunits. Reduction of L-Sorbose to D-sorbitol predominated in the presence of NADPH with the optimum pH of 5.0-7.0. Oxidation of D-sorbitol to L-Sorbose was observed in the presence of NADP at the optimum pH of 7.0-9.0. The relative rate of L-Sorbose reduction was more than seven times higher to that of D-sorbitol oxidation. NAD and NADH were inert for both reactions. D-Fructose reduction in the presence of NADPH did not occur with SORD. Since the reaction rate in L-Sorbose reduction highly predominated over D-sorbitol oxidation over a wide pH range, the enzyme could be available for direct enzymatic measurement of L-Sorbose. Even in the presence of a large excess of D-glucose and other substances, oxidation of NADPH to NADP was highly specific and stoichiometric to the L-Sorbose reduced. Judging from the enzymatic properties, SORD would contribute to the intracellular assimilation of L-Sorbose incorporated from outside the cells where L-Sorbose is accumulated in huge amounts in the culture medium.
Hirohide Toyama - One of the best experts on this subject based on the ideXlab platform.
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high temperature Sorbose fermentation with thermotolerant gluconobacter frateurii chm43 and its mutant strain adapted to higher temperature
Applied Microbiology and Biotechnology, 2012Co-Authors: Hiromi Hattori, Osao Adachi, Hirohide Toyama, Toshiharu Yakushi, Minenosuke Matsutani, Duantip Moonmangmee, Kazunobu MatsushitaAbstract:We succeeded in obtaining a strain adapted to higher temperature from a thermotolerant strain, Gluconobacter frateurii CHM43, for Sorbose fermentation. The adapted strain showed higher growth and l-Sorbose production than original CHM43 strain at higher temperature around 38.5–40 °C. It was also shown to be useful even with the fermentation without temperature control. To understand the Sorbose fermentation ability of the adapted strain at higher temperature, d-sorbitol-oxidizing respiratory chain was compared with the CHM43 strain and the adapted strain. We found that the activity of pyrroloquinoline quinone (PQQ)-dependent glycerol dehydrogenase (GLDH), which is a primary dehydrogenase of the respiratory chain and responsible for l-Sorbose production, was decreased when the temperature increased, but the decreased activity of GLDH was recovered by the addition of PQQ. Since the adapted strain was found to produce more PQQ than the CHM43 strain, it was suggested that the adapted strain keeps GLDH as holoenzyme with the increased PQQ production, and thus produces more l-Sorbose and grows better under higher temperature.
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the crystal structure of l Sorbose reductase from gluconobacter frateurii complexed with nadph and l Sorbose
Journal of Molecular Biology, 2011Co-Authors: Keiko Kubota, Hirohide Toyama, Koji Nagata, Masahiko Okai, Kenichi Miyazono, Wichai Soemphol, Jun Ohtsuka, Akihiro Yamamura, Natsaran SaichanaAbstract:Abstract l -Sorbose reductase from Gluconobacter frateurii (SR) is an NADPH-dependent oxidoreductase. SR preferentially catalyzes the reversible reaction between d -sorbitol and l -Sorbose with high substrate specificity. To elucidate the structural basis of the catalytic mechanism and the substrate specificity of SR, we have determined the structures of apo-SR, SR in complex with NADPH, and the inactive mutant (His116Leu) of SR in complex with NADPH and l -Sorbose at 2.83 A, 1.90 A, and 1.80 A resolutions, respectively. Our results show that SR belongs to the short-chain dehydrogenase/reductase (SDR) family and forms a tetrameric structure. Although His116 is not conserved among SDR family enzymes, the structures of SR have revealed that His116 is important for the stabilization of the proton relay system and for active-site conformation as a fourth catalytic residue. In the ternary complex structure, l -Sorbose is recognized by 11 hydrogen bonds. Site-directed mutagenesis of residues around the l -Sorbose-binding site has shown that the loss of almost full enzymatic activity was caused by not only the substitution of putative catalytic residues but also the substitution of the residue used for the recognition of the C4 hydroxyl groups of l -Sorbose (Glu154) and of the residues used for the construction of the substrate-binding pocket (Cys146 and Gly188). The recognition of the C4 hydroxyl group of l -Sorbose would be indispensable for the substrate specificity of SR, which recognizes only l -Sorbose and d -sorbitol but not other sugars. Our results indicated that these residues were crucial for the substrate recognition and specificity of SR.
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purification crystallization and preliminary x ray analysis of l Sorbose reductase from gluconobacter frateurii complexed with l Sorbose or nadph
Acta Crystallographica Section F-structural Biology and Crystallization Communications, 2009Co-Authors: Keiko Kubota, Hirohide Toyama, Kazunobu Matsushita, Koji Nagata, Kenichi Miyazono, Masaru TanokuraAbstract:NADPH-dependent l-Sorbose reductase (SR) from Gluconobacter frateurii was expressed in Escherichia coli, purified and crystallized with l-Sorbose or NADPH using the sitting-drop vapour-diffusion method at 293 K. Crystals of the SR–l-Sorbose complex and the SR–NADPH complex were obtained using reservoir solutions containing PEG 2000 or PEG 400 as precipitants and diffracted X-rays to 2.38 and 1.90 A resolution, respectively. The crystal of the SR–l-Sorbose complex belonged to space group C2221, with unit-cell parameters a = 124.2, b = 124.1, c = 60.8 A. The crystal of the SR–NADPH complex belonged to space group P21, with unit-cell parameters a = 124.3, b = 61.0, c = 124.5 A, β = 89.99°. The crystals contained two and eight molecules, respectively, in the asymmetric unit.
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Purification, crystallization and preliminary X-ray analysis of L-Sorbose reductase from Gluconobacter frateurii complexed with L-Sorbose or NADPH.
Acta crystallographica. Section F Structural biology and crystallization communications, 2009Co-Authors: Keiko Kubota, Hirohide Toyama, Kazunobu Matsushita, Koji Nagata, Kenichi Miyazono, Masaru TanokuraAbstract:NADPH-dependent L-Sorbose reductase (SR) from Gluconobacter frateurii was expressed in Escherichia coli, purified and crystallized with L-Sorbose or NADPH using the sitting-drop vapour-diffusion method at 293 K. Crystals of the SR-L-Sorbose complex and the SR-NADPH complex were obtained using reservoir solutions containing PEG 2000 or PEG 400 as precipitants and diffracted X-rays to 2.38 and 1.90 A resolution, respectively. The crystal of the SR-L-Sorbose complex belonged to space group C222(1), with unit-cell parameters a = 124.2, b = 124.1, c = 60.8 A. The crystal of the SR-NADPH complex belonged to space group P2(1), with unit-cell parameters a = 124.3, b = 61.0, c = 124.5 A, beta = 89.99 degrees . The crystals contained two and eight molecules, respectively, in the asymmetric unit.
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l Sorbose reductase and its transcriptional regulator involved in l Sorbose utilization of gluconobacter frateurii
Journal of Bacteriology, 2007Co-Authors: Wichai Soemphol, Osao Adachi, Duangtip Moonmangmee, Hirohide Toyama, Kazunobu MatsushitaAbstract:Upstream of the gene for flavin adenine dinucleotide (FAD)-dependent d-sorbitol dehydrogenase (SLDH), sldSLC, a putative transcriptional regulator was found in Gluconobacter frateurii THD32 (NBRC 101656). In this study, the whole sboR gene and the adjacent gene, sboA, were cloned and analyzed. sboR mutation did not affect FAD-SLDH activity in the membrane fractions. The SboA enzyme expressed and purified from an Escherichia coli transformant showed NADPH-dependent l-Sorbose reductase (NADPH-SR) activity, and the enzyme was different from the NADPH-SR previously reported for Gluconobacter suboxydans IFO 3291 in molecular size and amino acid sequence. A mutant defective in sboA showed significantly reduced growth on l-Sorbose, indicating that the SboA enzyme is required for efficient growth on l-Sorbose. The sboR mutant grew on l-Sorbose even better than the wild-type strain did, and higher NADPH-SR activity was detected in cytoplasm fractions. Reverse transcription-PCR experiments indicated that sboRA comprises an operon. These data suggest that sboR is involved in the repression of sboA, but not in the induction of sldSLC, on d-sorbitol and that another activator is required for the induction of these genes by d-sorbitol or l-Sorbose.
Jun-ichi Okumura - One of the best experts on this subject based on the ideXlab platform.
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Effect of Dietary Sorbose on Lipid Metabolism in Male and Female Broilers
Poultry Science, 2019Co-Authors: Mitsuhiro Furuse, Toshio Shimizu, Toshiya Ishii, Syuichi Miyagawa, Jiro Nakagawa, Tohru Watanabe, Jun-ichi OkumuraAbstract:Abstract Male and female broilers were given diets (6 males and 6 females per diet) containing varying percentages of Sorbose (0, 3, 6, and 9%) and fed for ad libitum access from 28 to 56 days of age. Body weight gain and feed intake were decreased with increasing dietary Sorbose, particularly in male birds fed diets containing 9% Sorbose, although feed efficiency and N retention rate were not influenced by dietary treatments. Absolute and relative abdominal fat weights were higher in females than in males and decreased with the increasing levels of dietary Sorbose in both sexes. Fat content in the pectoral muscle also decreased as dietary Sorbose increased. Dietary Sorbose did not have significant effects on serum glucose, triglyceride, total cholesterol, low density lipoprotein, very low density lipoprotein, and chylomicron levels in either male or female birds. The ME values of diets decreased as dietary Sorbose increased. Palmitic acid content of abdominal fat was significantly lower in birds fed the 9% Sorbose diet than in birds fed the control diet. The reverse was true for linoleic acid content. It was concluded that dietary Sorbose can be used as a potential regulator of lipid deposition in broilers.
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Lower fat deposition and energy utilization of growing rats fed diets containing Sorbose
Comparative Biochemistry and Physiology Part A: Physiology, 2003Co-Authors: Mitsuhiro Furuse, Yoshinaga Tamura, Satoshi Matsuda, Toshio Shimizu, Jun-ichi OkumuraAbstract:1. Growing rats were fed diets containing graded levels (0, 100, 200 and 300 g/kg diet) of Sorbose for 6 weeks. Protein, fat and energy deposition were determined by carcass analysis. 2. The values for growth, serum insulin level, digestible energy (DE), metabolizable energy (ME) and fat and energy deposition declined with the increment of dietary Sorbose. 3. The efficiency of protein utilization (protein retained/protein consumed) was hardly affected by dietary Sorbose. The DE and ME of Sorbose per se was calculated as 14.09 and 12.35 kJ/g respectively. The efficiency of energy utilization (energy retained/ME intake) decreased with the increase of dietary Sorbose, although Sorbose had an ME. 4. The relative weights of gastro-intestinal tract and liver were positively associated with dietary Sorbose level, although the reverse was true for the amount of stomach content, being heavier with higher dietary Sorbose. 5. It is suggested that dietary Sorbose, as a sweetener as well as a bulky agent, seems to be a suitable sugar for the obese and diabetic with special reference to lower body fat and energy deposition without reducing protein utilization.
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Dietary Sorbose Ameliorates Obesity and Hyperglycemia in Gold Thioglucose-Injected Obese Mice
Journal of Applied Animal Research, 2002Co-Authors: Kazumi Kita, Y. Kitayama, K. Nagao, J. Hwangbo, Mitsuhiro Furuse, Jun-ichi OkumuraAbstract:Abstract Kita, K., Kitayama, Y., Nagao, K., Hwangbo, J., Furuse, M. and Okumura, J. 2002. Dietary Sorbose ameliorates obesity and hyperglycemia in gold thioglucose-injected obese mice. J. Appl. Anim. Res., 21: 25–32. The influence of dietary Sorbose on hyperphagia, hyperglycemia and hyperinsulinemia in gold thioglucose (GTG)–injected obese mice was examined. Body weight of GTG–injected obese mice was decreased by feeding a Sorbose diet. When GTG–injected obese mice were given the diet containing Sorbose, food intake was significantly lower than that of intact normal mice given a sucrose diet. The reduction in body weight of GTG–injected obese mice given dietary Sorbose may be due to the decrease in food intake. Blood glucose concentration in GTG–injected obese mice was decreased by feeding the Sorbose diet to the level of intact normal mice given sucrose. Feeding the Sorbose diet lowered plasma insulin concentration compared to the sucrose group. It is concluded that feeding Sorbose ameliorates hyperphagi...
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Influence of dietary Sorbose on diabetes in nonobese diabetic mice
Comparative Biochemistry and Physiology Part A: Physiology, 1994Co-Authors: Mitsuhiro Furuse, Chiharu Kimura, Hisahide Takahashi, Jun-ichi OkumuraAbstract:Abstract The effect of dietary Sorbose on diabetes after the incidence of the syndrome in the nonobese diabetic mouse was investigated in the animals from 8 to 14 weeks of age. When sucrose (200g/kg diet) in a control diet was replaced by Sorbose, the body weight and the blood glucose concentration were significantly reduced, but the serum insulin concentration was unchanged. The urinary glucose concentration was the same for both sucrose and Sorbose diets. It is suggested that after the incidence of diabetes, dietary Sorbose could not improve urinary excretion of glucose, even though Sorbose could reduce the blood glucose concentration.
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dietary Sorbose prevents and improves hyperglycemia in genetically diabetic mice
Journal of Nutrition, 1993Co-Authors: Mitsuhiro Furuse, Chiharu Kimura, Hisahide Takahashi, Remedios T Mabayo, Jun-ichi OkumuraAbstract:: The effect of dietary Sorbose on the prevention (Experiment 1) and amelioration (Experiment 2) of diabetes was investigated in the genetically diabetic mouse [C57BL/KsJ (db/db)] for 6 wk. When sucrose (200 g/kg diet) in a control diet was replaced by Sorbose, the blood glucose concentration was dramatically lower, but the serum insulin concentrations did not differ. When mice were fed the diets before the onset of diabetic symptoms, glucose excretion in urine was prevented in the mice fed the Sorbose diet, but mice fed the control diet excreted glucose in the urine, and the concentration increased with age. When dietary treatment began after the development of diabetic symptoms, dietary Sorbose greatly reduced the incidence of hyperglycemia and lowered urinary glucose excretion, compared with mice fed the sucrose-containing diet. These results suggest that dietary Sorbose might be useful in patients with, or at risk of developing, noninsulin-dependent diabetes, both before and after exhibiting the syndrome.
Kouji Miyazaki - One of the best experts on this subject based on the ideXlab platform.
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prebiotic potential of l Sorbose and xylitol in promoting the growth and metabolic activity of specific butyrate producing bacteria in human fecal culture
FEMS Microbiology Ecology, 2017Co-Authors: Tadashi Sato, Shiro Kusuhara, Wakae Yokoi, Kouji MiyazakiAbstract:Dietary low-digestible carbohydrates (LDCs) affect gut microbial metabolism, including the production of short-chain fatty acids. The ability of various LDCs to promote butyrate production was evaluated in in vitro human fecal cultures. Fecal suspensions from five healthy males were anaerobically incubated with various LDCs. L-Sorbose and xylitol markedly promoted butyrate formation in cultures. Bacterial 16S rRNA gene–based denaturing gradient gel electrophoresis analyses of these fecal cultures revealed a marked increase in the abundance of bacteria closely related to the species Anaerostipes hadrus or Anaerostipes caccae , or both, during enhanced butyrate formation from L-Sorbose or xylitol. By using an agar plate culture, two strains of A. hadrus that produced butyrate from each substrate were isolated from the feces of two donors. Furthermore, of 12 species of representative colonic butyrate producers, only A. hadrus and A. caccae demonstrated augmented butyrate production from L-Sorbose or xylitol. These findings suggest that L-Sorbose and xylitol cause prebiotic stimulation of the growth and metabolic activity of Anaerostipes spp. in the human colon.
Yasushi Morikawa - One of the best experts on this subject based on the ideXlab platform.
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Xylanase Induction by L-Sorbose in a Fungus, Trichoderma reesei PC-3-7.
Bioscience Biotechnology and Biochemistry, 2014Co-Authors: Jianping Xu, Masahiro Nogawa, Hirofumi Okada, Yasushi MorikawaAbstract:Xylanase induction by L-Sorbose was studied in a resting cell system of a filamentous fungus, Trichoderma reesei PC-3-7, a hypercellulolytic mutant, and compared with that by other inducers. L-Sorbose induced xylanase activity as well as cellulase. It induced a higher level of xylanase activity than sophorose and xylose did. Three main xylanases, xylanase I (Xyn I), xylanase II (Xyn II), and a non-specific endoglucanase I (EG I), were separated using cation-exchange chromatography, and their activity were measured. Xyn II was induced in about the same proportion (60-80% of the total xylanase activity) by all inducers used. On the other hand, Xyn I was apparently induced by L-Sorbose, xylose, and xylooligosaccharides, but only a little by sophorose. Northern blot analysis showed that L-Sorbose induced Xyn I and Xyn II at the transcriptional level, and more xyn1 mRNA was transcribed after L-Sorbose addition than after sophorose. These results suggested that the expressions of both Xyn I and Xyn II are regulated, at least in part, in a different manner. Furthermore, the Xyn I induction by L-Sorbose indicated that an unknown common regulatory mechanism may exist between Xyn I and cellulase inductions.
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l Sorbose induces cellulase gene transcription in the cellulolytic fungus trichoderma reesei
Current Genetics, 2001Co-Authors: Masahiro Nogawa, Hirofumi Okada, Masahiro Goto, Yasushi MorikawaAbstract:l-Sorbose has previously been assumed to stimulate cellulase formation in an indirect manner, different from that of sophorose in Trichoderma reesei. Through Northern blot analysis however, l-Sorbose was found to regulate coordinately six cellulase genes (including egl3, whose behavior has not been studied so far) at transcriptional level, as is the case with sophorose in T. reesei strains PC-3-7 and QM9414. Dot blot analysis showed that the proportions of each cellulase mRNA to cbh1 mRNA, the largest amount of mRNA transcribed in T. reesei, did not change when l-Sorbose or sophorose was used as an inducer in the PC-3-7 and QM9414 strains. cbh2 and egl1 mRNAs were about 45–60% and 20–30% of the cbh1 transcript, whereas small amounts of mRNA, 1–2% of cbh1, were observed on other endoglucanase genes. Furthermore, the PC-3-7 strain showed an enhanced level of cellulase gene transcription, about two- and four- to six-fold higher than that of the QM9414 strain with sophorose and l-Sorbose, respectively.
