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Fred Naider - One of the best experts on this subject based on the ideXlab platform.

  • synthesis of the dodecapeptide α Mating Factor of saccharomyces cerevisiae
    International Journal of Peptide and Protein Research, 2009
    Co-Authors: S A Khan, Jeffrey M Becker, Glenn J Merkel, Fred Naider
    Abstract:

    The synthesis of His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr, the dodecapeptide alpha-Mating Factor from Saccharomyces cerevisiae, and its Ala2- and Cha2-(beta-cyclohexylalanine) analogs are reported. Peptides were synthesized in solution using a combination of mixed anhydride and 1-hydroxybenzotriazole accelerated active ester coupling procedures. Dilute methanesulfonic acid (0.1-0.2 M) in methylene chloride-formic acid solution was employed to specifically remove the tert.-butoxycarbonyl group in the presence of the benzyloxycarbonyl group. Free peptides were obtained using catalytic transfer hydrogenation with formic acid as the hydrogen donor followed by mild acidolysis with trifluoroacetic acid. The alpha-Factor and the Cha2-analog exhibited almost equal ability to cause "shmooing" of a-Mating types of S. cerevisiae whereas the Ala2-analog exhibited no activity in this assay. These results differ with structure-activity studies reported on the tridecapeptide alpha-Factor.

  • solution phase synthesis of saccharomyces cerevisiae a Mating Factor and its analogs
    International Journal of Peptide and Protein Research, 2009
    Co-Authors: Chubiao Xue, Jeffrey M Becker, Ariel Ewenson, Fred Naider
    Abstract:

    The solution phase synthesis of the Saccharomyces cerevisiae a-Mating Factor and nonfarnesylated and nonmethylated a-Factor analogs are reported. The a-Factor, a lipopeptide with the sequence Tyr-Ile-Ile-Lys-Gly-Val-Phe-Trp-Asp-Pro-Ala-Cys(S-Farnesyl)OCH3 was synthesized by the condensation of the amine terminal protected decapeptide with the carboxyl terminal farnesylated dipeptide using benzotriazol-l-yloxy-tris-(dimethylamino)-phosphonium hexafluorophosphate (BOP reagent) as the coupling agent. The synthesis of the decapeptide involved 5 + 5 fragment coupling with the BOP reagent and the successful application of 9-fluorenylmethyl ester(OFm) and 9-fluorenylmethoxycarbonyl(Fmoc) groups for the protection of Asp and Lys side chains and Tyr alpha-amine and of phenacyl esters (OPa) for alpha-carboxyl protection. The OFm and Fmoc groups tolerated repeated couplings and were completely stable to zinc powder in acetic acid, a condition under which the OPa group was removed. The synthesis of the nonfarnesylated alpha-Factor was accomplished by the coupling of the decapeptide with tetrapeptide (Ala-CysOCH3)2 followed by the deprotection of the OFm and Fmoc groups with piperidine and the cleavage of the disulfide bond with zinc powder in acetic acid. The nonmethylated a-Factor was prepared by 10 + 2 fragment coupling using OFm protection of the dipeptide carboxyl group followed by removal of all protecting groups with piperidine. Attempts to saponify a-Factor were not successful. The synthetic nonfarnesylated and nonmethylated a-Mating pheromones were 100-1000 times less active than the a-Factor, indicating that although the methyl ester and the farnesyl group are not essential for biological activity, they are necessary for high potency.

  • atr ftir study of the structure and orientation of transmembrane domains of the saccharomyces cerevisiae α Mating Factor receptor in phospholipids
    Biochemistry, 2001
    Co-Authors: Faxiang Ding, Jeffrey M Becker, Haibo Xie, Boris Arshava, Fred Naider
    Abstract:

    The structures of seven synthetic transmembrane domains (TMDs) of the α-Factor receptor (Ste2p) from Saccharomyces cerevisiae were studied in phospholipid multilayers by transmission Fourier transform infrared (FTIR) and attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopies. Peptide conformation assumed in multilayers depended on the method of sample preparation. Amide proton H/D exchange experiments showed that 60−80% of the NH bonds in these TMDs did not exchange with bulk water in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) multilayers. FTIR results showed that peptides corresponding to TMDs one, two, and seven were mostly α-helical in DMPC multilayers. Peptides corresponding to TMDs three and six assumed predominantly β-sheet structures, whereas those corresponding to TMDs four and five were a mixture of α-helices and β-sheets. ATR-FTIR showed that in DMPC the α-helices of TMDs two and five oriented with tilt angles of 34° and 32°, respectively, with respect to the mu...

  • probing the binding domain of the saccharomyces cerevisiae alpha Mating Factor receptor with rluorescent ligands
    Biochemistry, 2001
    Co-Authors: Faxiang Ding, Jeffrey M Becker, Byungkwon Lee, Melinda Hauser, Lesley Davenport, Fred Naider
    Abstract:

    Three analogues of the alpha-Mating Factor pheromone of Saccharomyces cerevisiae containing the 7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD) group were synthesized that had high binding affinity to the receptor and retained biological activity. The fluorescence emission maximum of the NBD group in [K7(NBD),Nle(12)]-alpha-Factor was blue shifted by 35 nm compared to buffer when the pheromone bound to its receptor. Fluorescence quenching experiments revealed that the NBD group in [K7(NBD),Nle(12)]-alpha-Factor bound to the receptor was shielded from collision with iodide anion when in aqueous buffer. In contrast, the emission maximum of NBD in [K7(ahNBD),Nle(12)]-alpha-Factor or [Orn7(NBD),Nle(12)]-alpha-Factor was not significantly shifted and iodide anion efficiently quenched the fluorescence of these derivatives when they were bound to receptor. The fluorescence investigation suggests that when the alpha-Factor is bound to its receptor, K7 resides in an environment that has both hydrophobic and hydrophilic groups within a few angstroms of each other.

  • studies on the yeast α Mating Factor a model for mammalian peptide hormones
    Biopolymers, 1992
    Co-Authors: Fred Naider, Chubiao Xue, John Gounarides, Effimia Bargiota, Jeffrey M Becker
    Abstract:

    Small peptides initiate sexual conjugation in the yeast Saccharomyces cerevisiae and this phenomenon is an ideal paradigm for studying the mode of action of mammalian peptide hormones. 1H-nmr spectroscopy was used to examine the conformation of linear and cyclic analogues of the alpha-Factor (WHWLQLKPGQPMY) in aqueous solution. In all cases peptides that exhibit nmr parameters expected for a type II beta-turn have higher biological activities than those that do not appear to assume this conformation. Based on a simple model for the interaction of the pheromone with its receptor, we prepared fragments of the alpha-Factor. Several of these fragments either antagonize or potentiate the activity of the alpha-Factor. The latter represent the first example of peptide fragments that synergize the activity of the parent pheromone.

Eugene Jeon - One of the best experts on this subject based on the ideXlab platform.

  • cellulosic alcoholic fermentation using recombinant saccharomyces cerevisiae engineered for the production of clostridium cellulovorans endoglucanase and saccharomycopsis fibuligeraβ glucosidase
    Fems Microbiology Letters, 2009
    Co-Authors: Eugene Jeon, Jeong Eun Hyeon, Byeoung Soo Park
    Abstract:

    In this study, Saccharomyces cerevisiae was engineered for simultaneous saccharification and fermentation of cellulose by the overexpression of the endoglucanase D (EngD) from Clostridium cellulovorans and the β-glucosidase (Bgl1) from Saccharomycopsis fibuligera. To promote secretion of the two enzymes, the genes were fused to the secretion signal of the S. cerevisiaeα Mating Factor gene. The recombinant developed yeast could produce ethanol through simultaneous production of sufficient extracellular endoglucanase and β-glucosidase. When direct ethanol fermentation from 20 g L−1β-glucan as a substrate was performed with our recombinant strains, the ethanol concentration reached 9.15 g L−1 after 50 h of fermentation. The conversion ratio of ethanol from β-glucan was 80.3% of the theoretical ethanol concentration produced from 20 g L−1β-glucan. In conclusion, we have demonstrated the construction of a yeast strain capable of conversion of a cellulosic substrate to ethanol, representing significant progress towards the realization of processing of cellulosic biomass in a consolidated bioprocessing configuration.

  • cellulosic alcoholic fermentation using recombinant saccharomyces cerevisiae engineered for the production of clostridium cellulovorans endoglucanase and saccharomycopsis fibuligeraβ glucosidase
    Fems Microbiology Letters, 2009
    Co-Authors: Eugene Jeon, Jeong Eun Hyeon, Byeoung Soo Park, Lee Sung Eun, Seung Woo Kim, Jinwon Lee, Sung Ok Han
    Abstract:

    In this study, Saccharomyces cerevisiae was engineered for simultaneous saccharification and fermentation of cellulose by the overexpression of the endoglucanase D (EngD) from Clostridium cellulovorans and the beta-glucosidase (Bgl1) from Saccharomycopsis fibuligera. To promote secretion of the two enzymes, the genes were fused to the secretion signal of the S. cerevisiaealpha Mating Factor gene. The recombinant developed yeast could produce ethanol through simultaneous production of sufficient extracellular endoglucanase and beta-glucosidase. When direct ethanol fermentation from 20 g L(-1)beta-glucan as a substrate was performed with our recombinant strains, the ethanol concentration reached 9.15 g L(-1) after 50 h of fermentation. The conversion ratio of ethanol from beta-glucan was 80.3% of the theoretical ethanol concentration produced from 20 g L(-1)beta-glucan. In conclusion, we have demonstrated the construction of a yeast strain capable of conversion of a cellulosic substrate to ethanol, representing significant progress towards the realization of processing of cellulosic biomass in a consolidated bioprocessing configuration.

  • production of cellulosic ethanol in saccharomyces cerevisiae heterologous expressing clostridium thermocellum endoglucanase and saccharomycopsis fibuligera β glucosidase genes
    Molecules and Cells, 2009
    Co-Authors: Eugene Jeon, Jeong Eun Hyeon, Kwang Ho Song
    Abstract:

    Heterologous secretory expression of endoglucanase E (Clostridium thermocellum) and β-glucosidase 1 (Saccharomycopsis fibuligera) was achieved in Saccharomyces cerevisiae fermentation cultures as an α-Mating Factor signal peptide fusion, based on the native enzyme coding sequence. Ethanol production depends on simultaneous saccharification of cellulose to glucose and fermentation of glucose to ethanol by a recombinant yeast strain as a microbial biocatalyst. Recombinant yeast strain expressing endoglucanase and β-glucosidase was able to produce ethanol from β-glucan, CMC and acid swollen cellulose. This indicates that the resultant yeast strain of this study acts efficiently as a whole cell biocatalyst.

F.r Cross - One of the best experts on this subject based on the ideXlab platform.

  • The Mating Factor response pathway regulates transcription of TEC1, a gene involved in pseudohyphal differentiation of Saccharomyces cerevisiae
    FEBS letters, 1998
    Co-Authors: L.j.w.m. Oehlen, F.r Cross
    Abstract:

    The transcription Factor Tec1 is involved in pseudohyphal differentiation and agar-invasive growth of Saccharomyces cerevisiae cells. The sole element in the TEC1 promoter that has thus far been shown to control Tec1 function is the filament response element. We find that the TEC1 promoter also contains several pheromone response element sequences which are likely to be functional: TEC1 transcription is induced by Mating Factor, cell cycle regulated and dependent on the Ste4, Ste18 and Ste5 components of the Mating Factor signal transduction pathway. Using alleles of the transcription Factor Ste12 that are defective in DNA binding, transcriptional induction or cooperativity with other transcription Factors, we find little correlation between TEC1 transcript levels and agar-invasive growth.

  • cyclin specific start events and the g1 phase specificity of arrest by Mating Factor in budding yeast
    Molecular Genetics and Genomics, 1998
    Co-Authors: L.j.w.m. Oehlen, D I Jeoung, F.r Cross
    Abstract:

    The START cell cycle transition in the budding yeast Saccharomyces cerevisiae is catalyzed by the Cdc28 cyclin-dependent kinase associated with Cln-type cyclins. Since ectopic expression of the B-type cyclin CLB5 can efficiently rescue the inviability that results from CLN depletion, we tested the specificity of the CLN and CLB classes of cyclins for promoting START-associated events. Several aspects of the regulation of the Mating Factor response were compared for cells in which START activity was provided by either Cln-cyclins or Clb5. Unlike Cln1 and Cln2, high level expression of Clb5 was unable to repress the activity of the Mating Factor response pathway at START. Downregulation of Far1 protein at START is normal in cln−GAL1::CLB5 cells. Even though the Clb5-Cdc28 kinase activity in cln−GAL1::CLB5 cells is not downregulated in response to Mating Factor, cells arrest in the first cycle after addition of Mating Factor with a similar sensitivity as wild-type cells. However, whereas wild-type cells treated with Mating Factor arrest specifically in G1 phase as unbudded cells with unreplicated DNA (pre-START), most cln−GAL1::CLB5 cells arrest as budded post-START cells with replicated DNA. Our findings demonstrate the ability of post-START cells to arrest in response to Mating Factor and provide novel evidence for mechanisms that contribute to restrict Mating Factor-induced arrest in wild-type cells to the G1 phase of the cell cycle.

  • g1 cyclins cln1 and cln2 repress the Mating Factor response pathway at start in the yeast cell cycle
    Genes & Development, 1994
    Co-Authors: L.j.w.m. Oehlen, F.r Cross
    Abstract:

    Transcriptional induction by the Mating pheromone ,,-Factor was monitored at different stages of the yeast cell cycle. G2/M-phase and pre-Start cells showed strong FUS1 mRNA induction, whereas in post-Start cells the signaling was reduced significantly. This reduction in signaling activity in post-Start cells was correlated with the presence of CLN1 or CLN2 transcripts and was not observed in synchronized cells lacking functional CLN1 and CLN2 genes. Activation of the Cln-Cdc28p kinase by overexpression of CLN2 from the GALl promoter strongly reduced FUS1 mRNA induction. CLN1 overexpression had a similar effect when the FAR1 gene, encoding a negative regulator of CLN1/2 function, was deleted. This reduction of pheromone signaling was specific for CLN1 and CLN2, as it was not observed when CLN3 was overexpressed. Inactivation of the Cln-Cdc28p kinase complex by thermal inactivation of temperature-sensitive Cdc28p prevented repression of FUS1 signaling. CLN2 overexpression suppressed the constitutive signaling and division-arrest phenotypes of cells with a disrupted gpal gene, indicating that the site of action for repression is downstream of the c~-subunit (Gpalp) of the heterotrimeric G protein. The repression at Start of pheromone signaling by Clnl-Cdc28p or Cln2-Cdc28p kinase complexes may contribute to the acquisition of pheromone resistance as cells execute Start.

Jeffrey M Becker - One of the best experts on this subject based on the ideXlab platform.

  • synthesis of the dodecapeptide α Mating Factor of saccharomyces cerevisiae
    International Journal of Peptide and Protein Research, 2009
    Co-Authors: S A Khan, Jeffrey M Becker, Glenn J Merkel, Fred Naider
    Abstract:

    The synthesis of His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr, the dodecapeptide alpha-Mating Factor from Saccharomyces cerevisiae, and its Ala2- and Cha2-(beta-cyclohexylalanine) analogs are reported. Peptides were synthesized in solution using a combination of mixed anhydride and 1-hydroxybenzotriazole accelerated active ester coupling procedures. Dilute methanesulfonic acid (0.1-0.2 M) in methylene chloride-formic acid solution was employed to specifically remove the tert.-butoxycarbonyl group in the presence of the benzyloxycarbonyl group. Free peptides were obtained using catalytic transfer hydrogenation with formic acid as the hydrogen donor followed by mild acidolysis with trifluoroacetic acid. The alpha-Factor and the Cha2-analog exhibited almost equal ability to cause "shmooing" of a-Mating types of S. cerevisiae whereas the Ala2-analog exhibited no activity in this assay. These results differ with structure-activity studies reported on the tridecapeptide alpha-Factor.

  • solution phase synthesis of saccharomyces cerevisiae a Mating Factor and its analogs
    International Journal of Peptide and Protein Research, 2009
    Co-Authors: Chubiao Xue, Jeffrey M Becker, Ariel Ewenson, Fred Naider
    Abstract:

    The solution phase synthesis of the Saccharomyces cerevisiae a-Mating Factor and nonfarnesylated and nonmethylated a-Factor analogs are reported. The a-Factor, a lipopeptide with the sequence Tyr-Ile-Ile-Lys-Gly-Val-Phe-Trp-Asp-Pro-Ala-Cys(S-Farnesyl)OCH3 was synthesized by the condensation of the amine terminal protected decapeptide with the carboxyl terminal farnesylated dipeptide using benzotriazol-l-yloxy-tris-(dimethylamino)-phosphonium hexafluorophosphate (BOP reagent) as the coupling agent. The synthesis of the decapeptide involved 5 + 5 fragment coupling with the BOP reagent and the successful application of 9-fluorenylmethyl ester(OFm) and 9-fluorenylmethoxycarbonyl(Fmoc) groups for the protection of Asp and Lys side chains and Tyr alpha-amine and of phenacyl esters (OPa) for alpha-carboxyl protection. The OFm and Fmoc groups tolerated repeated couplings and were completely stable to zinc powder in acetic acid, a condition under which the OPa group was removed. The synthesis of the nonfarnesylated alpha-Factor was accomplished by the coupling of the decapeptide with tetrapeptide (Ala-CysOCH3)2 followed by the deprotection of the OFm and Fmoc groups with piperidine and the cleavage of the disulfide bond with zinc powder in acetic acid. The nonmethylated a-Factor was prepared by 10 + 2 fragment coupling using OFm protection of the dipeptide carboxyl group followed by removal of all protecting groups with piperidine. Attempts to saponify a-Factor were not successful. The synthetic nonfarnesylated and nonmethylated a-Mating pheromones were 100-1000 times less active than the a-Factor, indicating that although the methyl ester and the farnesyl group are not essential for biological activity, they are necessary for high potency.

  • atr ftir study of the structure and orientation of transmembrane domains of the saccharomyces cerevisiae α Mating Factor receptor in phospholipids
    Biochemistry, 2001
    Co-Authors: Faxiang Ding, Jeffrey M Becker, Haibo Xie, Boris Arshava, Fred Naider
    Abstract:

    The structures of seven synthetic transmembrane domains (TMDs) of the α-Factor receptor (Ste2p) from Saccharomyces cerevisiae were studied in phospholipid multilayers by transmission Fourier transform infrared (FTIR) and attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopies. Peptide conformation assumed in multilayers depended on the method of sample preparation. Amide proton H/D exchange experiments showed that 60−80% of the NH bonds in these TMDs did not exchange with bulk water in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) multilayers. FTIR results showed that peptides corresponding to TMDs one, two, and seven were mostly α-helical in DMPC multilayers. Peptides corresponding to TMDs three and six assumed predominantly β-sheet structures, whereas those corresponding to TMDs four and five were a mixture of α-helices and β-sheets. ATR-FTIR showed that in DMPC the α-helices of TMDs two and five oriented with tilt angles of 34° and 32°, respectively, with respect to the mu...

  • probing the binding domain of the saccharomyces cerevisiae alpha Mating Factor receptor with rluorescent ligands
    Biochemistry, 2001
    Co-Authors: Faxiang Ding, Jeffrey M Becker, Byungkwon Lee, Melinda Hauser, Lesley Davenport, Fred Naider
    Abstract:

    Three analogues of the alpha-Mating Factor pheromone of Saccharomyces cerevisiae containing the 7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD) group were synthesized that had high binding affinity to the receptor and retained biological activity. The fluorescence emission maximum of the NBD group in [K7(NBD),Nle(12)]-alpha-Factor was blue shifted by 35 nm compared to buffer when the pheromone bound to its receptor. Fluorescence quenching experiments revealed that the NBD group in [K7(NBD),Nle(12)]-alpha-Factor bound to the receptor was shielded from collision with iodide anion when in aqueous buffer. In contrast, the emission maximum of NBD in [K7(ahNBD),Nle(12)]-alpha-Factor or [Orn7(NBD),Nle(12)]-alpha-Factor was not significantly shifted and iodide anion efficiently quenched the fluorescence of these derivatives when they were bound to receptor. The fluorescence investigation suggests that when the alpha-Factor is bound to its receptor, K7 resides in an environment that has both hydrophobic and hydrophilic groups within a few angstroms of each other.

  • studies on the yeast α Mating Factor a model for mammalian peptide hormones
    Biopolymers, 1992
    Co-Authors: Fred Naider, Chubiao Xue, John Gounarides, Effimia Bargiota, Jeffrey M Becker
    Abstract:

    Small peptides initiate sexual conjugation in the yeast Saccharomyces cerevisiae and this phenomenon is an ideal paradigm for studying the mode of action of mammalian peptide hormones. 1H-nmr spectroscopy was used to examine the conformation of linear and cyclic analogues of the alpha-Factor (WHWLQLKPGQPMY) in aqueous solution. In all cases peptides that exhibit nmr parameters expected for a type II beta-turn have higher biological activities than those that do not appear to assume this conformation. Based on a simple model for the interaction of the pheromone with its receptor, we prepared fragments of the alpha-Factor. Several of these fragments either antagonize or potentiate the activity of the alpha-Factor. The latter represent the first example of peptide fragments that synergize the activity of the parent pheromone.

Jeong Eun Hyeon - One of the best experts on this subject based on the ideXlab platform.

  • cellulosic alcoholic fermentation using recombinant saccharomyces cerevisiae engineered for the production of clostridium cellulovorans endoglucanase and saccharomycopsis fibuligeraβ glucosidase
    Fems Microbiology Letters, 2009
    Co-Authors: Eugene Jeon, Jeong Eun Hyeon, Byeoung Soo Park
    Abstract:

    In this study, Saccharomyces cerevisiae was engineered for simultaneous saccharification and fermentation of cellulose by the overexpression of the endoglucanase D (EngD) from Clostridium cellulovorans and the β-glucosidase (Bgl1) from Saccharomycopsis fibuligera. To promote secretion of the two enzymes, the genes were fused to the secretion signal of the S. cerevisiaeα Mating Factor gene. The recombinant developed yeast could produce ethanol through simultaneous production of sufficient extracellular endoglucanase and β-glucosidase. When direct ethanol fermentation from 20 g L−1β-glucan as a substrate was performed with our recombinant strains, the ethanol concentration reached 9.15 g L−1 after 50 h of fermentation. The conversion ratio of ethanol from β-glucan was 80.3% of the theoretical ethanol concentration produced from 20 g L−1β-glucan. In conclusion, we have demonstrated the construction of a yeast strain capable of conversion of a cellulosic substrate to ethanol, representing significant progress towards the realization of processing of cellulosic biomass in a consolidated bioprocessing configuration.

  • cellulosic alcoholic fermentation using recombinant saccharomyces cerevisiae engineered for the production of clostridium cellulovorans endoglucanase and saccharomycopsis fibuligeraβ glucosidase
    Fems Microbiology Letters, 2009
    Co-Authors: Eugene Jeon, Jeong Eun Hyeon, Byeoung Soo Park, Lee Sung Eun, Seung Woo Kim, Jinwon Lee, Sung Ok Han
    Abstract:

    In this study, Saccharomyces cerevisiae was engineered for simultaneous saccharification and fermentation of cellulose by the overexpression of the endoglucanase D (EngD) from Clostridium cellulovorans and the beta-glucosidase (Bgl1) from Saccharomycopsis fibuligera. To promote secretion of the two enzymes, the genes were fused to the secretion signal of the S. cerevisiaealpha Mating Factor gene. The recombinant developed yeast could produce ethanol through simultaneous production of sufficient extracellular endoglucanase and beta-glucosidase. When direct ethanol fermentation from 20 g L(-1)beta-glucan as a substrate was performed with our recombinant strains, the ethanol concentration reached 9.15 g L(-1) after 50 h of fermentation. The conversion ratio of ethanol from beta-glucan was 80.3% of the theoretical ethanol concentration produced from 20 g L(-1)beta-glucan. In conclusion, we have demonstrated the construction of a yeast strain capable of conversion of a cellulosic substrate to ethanol, representing significant progress towards the realization of processing of cellulosic biomass in a consolidated bioprocessing configuration.

  • production of cellulosic ethanol in saccharomyces cerevisiae heterologous expressing clostridium thermocellum endoglucanase and saccharomycopsis fibuligera β glucosidase genes
    Molecules and Cells, 2009
    Co-Authors: Eugene Jeon, Jeong Eun Hyeon, Kwang Ho Song
    Abstract:

    Heterologous secretory expression of endoglucanase E (Clostridium thermocellum) and β-glucosidase 1 (Saccharomycopsis fibuligera) was achieved in Saccharomyces cerevisiae fermentation cultures as an α-Mating Factor signal peptide fusion, based on the native enzyme coding sequence. Ethanol production depends on simultaneous saccharification of cellulose to glucose and fermentation of glucose to ethanol by a recombinant yeast strain as a microbial biocatalyst. Recombinant yeast strain expressing endoglucanase and β-glucosidase was able to produce ethanol from β-glucan, CMC and acid swollen cellulose. This indicates that the resultant yeast strain of this study acts efficiently as a whole cell biocatalyst.