The Experts below are selected from a list of 8967 Experts worldwide ranked by ideXlab platform
Akihiko Kondo - One of the best experts on this subject based on the ideXlab platform.
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p hydroxycinnamic acid production directly from cellulose using endoglucanase and tyrosine Ammonia Lyase expressing streptomyces lividans
Microbial Cell Factories, 2013Co-Authors: Yoshifumi Kawai, Chiaki Ogino, Shuhei Noda, Naoko Okai, Yasunobu Takeshima, Tsutomu Tanaka, Akihiko KondoAbstract:Background p-Hydroxycinnamic acid (pHCA) is an aromatic compound that serves as a starting material for the production of many commercially valuable chemicals, such as fragrances and pharmaceuticals, and is also used in the synthesis of thermostable polymers. However, chemical synthesis of pHCA is both costly and harmful to the environment. Although pHCA production using microbes has been widely studied, there remains a need for more cost-effective methods, such as the use of biomass as a carbon source. In this study, we produced pHCA using tyrosine Ammonia Lyase-expressing Streptomyces lividans. In order to improve pHCA productivity from cellulose, we constructed a tyrosine Ammonia Lyase- and endoglucanase (EG)-expressing S. lividans transformant and used it to produce pHCA from cellulose.
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p hydroxycinnamic acid production directly from cellulose using endoglucanase and tyrosine Ammonia Lyase expressing streptomyces lividans
Microbial Cell Factories, 2013Co-Authors: Yoshifumi Kawai, Chiaki Ogino, Shuhei Noda, Naoko Okai, Yasunobu Takeshima, Tsutomu Tanaka, Akihiko KondoAbstract:p-Hydroxycinnamic acid (pHCA) is an aromatic compound that serves as a starting material for the production of many commercially valuable chemicals, such as fragrances and pharmaceuticals, and is also used in the synthesis of thermostable polymers. However, chemical synthesis of pHCA is both costly and harmful to the environment. Although pHCA production using microbes has been widely studied, there remains a need for more cost-effective methods, such as the use of biomass as a carbon source. In this study, we produced pHCA using tyrosine Ammonia Lyase-expressing Streptomyces lividans. In order to improve pHCA productivity from cellulose, we constructed a tyrosine Ammonia Lyase- and endoglucanase (EG)-expressing S. lividans transformant and used it to produce pHCA from cellulose. A Streptomyces lividans transformant was constructed to express tyrosine Ammonia Lyase derived from Rhodobacter sphaeroides (RsTAL). The transformant produced 786 or 736 mg/L of pHCA after 7 days of cultivation in medium containing 1% glucose or cellobiose as the carbon source, respectively. To enhance pHCA production from phosphoric acid swollen cellulose (PASC), we introduced the gene encoding EG into RsTAL-expressing S. lividans. After 7 days of cultivation, this transformant produced 753, 743, or 500 mg/L of pHCA from 1% glucose, cellobiose, or PASC, respectively. RsTAL-expressing S. lividans can produce pHCA from glucose and cellobiose. Similarly, RsTAL- and EG-expressing S. lividans can produce pHCA from glucose and cellobiose with excess EG activity remaining in the supernatant. This transformant demonstrated improved pHCA production from cellulose. Further enhancements in the cellulose degradation capability of the transformant will be necessary in order to achieve further improvements in pHCA production from cellulose.
Chiaki Ogino - One of the best experts on this subject based on the ideXlab platform.
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p hydroxycinnamic acid production directly from cellulose using endoglucanase and tyrosine Ammonia Lyase expressing streptomyces lividans
Microbial Cell Factories, 2013Co-Authors: Yoshifumi Kawai, Chiaki Ogino, Shuhei Noda, Naoko Okai, Yasunobu Takeshima, Tsutomu Tanaka, Akihiko KondoAbstract:p-Hydroxycinnamic acid (pHCA) is an aromatic compound that serves as a starting material for the production of many commercially valuable chemicals, such as fragrances and pharmaceuticals, and is also used in the synthesis of thermostable polymers. However, chemical synthesis of pHCA is both costly and harmful to the environment. Although pHCA production using microbes has been widely studied, there remains a need for more cost-effective methods, such as the use of biomass as a carbon source. In this study, we produced pHCA using tyrosine Ammonia Lyase-expressing Streptomyces lividans. In order to improve pHCA productivity from cellulose, we constructed a tyrosine Ammonia Lyase- and endoglucanase (EG)-expressing S. lividans transformant and used it to produce pHCA from cellulose. A Streptomyces lividans transformant was constructed to express tyrosine Ammonia Lyase derived from Rhodobacter sphaeroides (RsTAL). The transformant produced 786 or 736 mg/L of pHCA after 7 days of cultivation in medium containing 1% glucose or cellobiose as the carbon source, respectively. To enhance pHCA production from phosphoric acid swollen cellulose (PASC), we introduced the gene encoding EG into RsTAL-expressing S. lividans. After 7 days of cultivation, this transformant produced 753, 743, or 500 mg/L of pHCA from 1% glucose, cellobiose, or PASC, respectively. RsTAL-expressing S. lividans can produce pHCA from glucose and cellobiose. Similarly, RsTAL- and EG-expressing S. lividans can produce pHCA from glucose and cellobiose with excess EG activity remaining in the supernatant. This transformant demonstrated improved pHCA production from cellulose. Further enhancements in the cellulose degradation capability of the transformant will be necessary in order to achieve further improvements in pHCA production from cellulose.
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p hydroxycinnamic acid production directly from cellulose using endoglucanase and tyrosine Ammonia Lyase expressing streptomyces lividans
Microbial Cell Factories, 2013Co-Authors: Yoshifumi Kawai, Chiaki Ogino, Shuhei Noda, Naoko Okai, Yasunobu Takeshima, Tsutomu Tanaka, Akihiko KondoAbstract:Background p-Hydroxycinnamic acid (pHCA) is an aromatic compound that serves as a starting material for the production of many commercially valuable chemicals, such as fragrances and pharmaceuticals, and is also used in the synthesis of thermostable polymers. However, chemical synthesis of pHCA is both costly and harmful to the environment. Although pHCA production using microbes has been widely studied, there remains a need for more cost-effective methods, such as the use of biomass as a carbon source. In this study, we produced pHCA using tyrosine Ammonia Lyase-expressing Streptomyces lividans. In order to improve pHCA productivity from cellulose, we constructed a tyrosine Ammonia Lyase- and endoglucanase (EG)-expressing S. lividans transformant and used it to produce pHCA from cellulose.
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cinnamic acid production using streptomyces lividans expressing phenylalanine Ammonia Lyase
Journal of Industrial Microbiology & Biotechnology, 2011Co-Authors: Shuhei Noda, Takaya Miyazaki, Takanori Miyoshi, Michiru Miyake, Naoko Okai, Chiaki OginoAbstract:Cinnamic acid production was demonstrated using Streptomyces as a host. A gene encoding phenylalanine Ammonia Lyase (PAL) from Streptomyces maritimus was introduced into Streptomyces lividans, and its expression was confirmed by Western blot analysis. After 4 days cultivation using glucose as carbon source, the maximal level of cinnamic acid reached 210 mg/L. When glycerol (30 g/L) was used as carbon source, the maximal level of produced cinnamic acid reached 450 mg/L. In addition, using raw starch, xylose or xylan as carbon source, the maximal level of cinnamic acid reached 460, 300, and 130 mg/L, respectively. We demonstrated that S. lividans has great potential to produce cinnamic acid as well as other aromatic compounds.
Bradley S. Moore - One of the best experts on this subject based on the ideXlab platform.
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biochemical characterization of a prokaryotic phenylalanine Ammonia Lyase
Journal of Bacteriology, 2005Co-Authors: Longkuan Xiang, Bradley S. MooreAbstract:The committed biosynthetic reaction to benzoyl-coenzyme A in the marine bacterium “Streptomyces maritimus” is carried out by the novel prokaryotic phenylalanine Ammonia Lyase (PAL) EncP, which converts the primary amino acid l-phenylalanine to trans-cinnamic acid. Recombinant EncP is specific for l-phenylalanine and shares many biochemical features with eukaryotic PALs, which are substantially larger proteins by ∼200 amino acid residues.
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inactivation complementation and heterologous expression of encp a novel bacterial phenylalanine Ammonia Lyase gene
Journal of Biological Chemistry, 2002Co-Authors: Longkuan Xiang, Bradley S. MooreAbstract:Abstract The enzyme phenylalanine Ammonia-Lyase, which catalyzes the nonoxidative deamination ofl-phenylalanine to trans-cinnamic acid, is ubiquitously distributed in plants. We now report its characterization for the first time in a bacterium. The phenylalanine Ammonia-Lyase homologous gene encP from the “Streptomyces maritimus” enterocin biosynthetic gene cluster was functionally characterized and shown to encode the first enzyme in the pathway to the enterocin polyketide synthase starter unit benzoyl-coenzyme A. The disruption of the encP gene completely inhibited the production of cinnamate and enterocin, whereas complementation of the mutant with benzoyl-coenzyme A pathway intermediates or with the wild-type gene encP restored the formation of the benzoate-primed polyketide antibiotic enterocin. Heterologous expression of the encP gene under the control of the ermE* promoter in Streptomyces coelicolor furthermore led to the production of cinnamic acid in the fermented cultures, confirming that the encP gene indeed encodes a novel bacterial phenylalanine Ammonia-Lyase.
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inactivation complementation and heterologous expression of encp a novel bacterial phenylalanine Ammonia Lyase gene
Journal of Biological Chemistry, 2002Co-Authors: Longkuan Xiang, Bradley S. MooreAbstract:Abstract The enzyme phenylalanine Ammonia-Lyase, which catalyzes the nonoxidative deamination ofl-phenylalanine to trans-cinnamic acid, is ubiquitously distributed in plants. We now report its characterization for the first time in a bacterium. The phenylalanine Ammonia-Lyase homologous gene encP from the “Streptomyces maritimus” enterocin biosynthetic gene cluster was functionally characterized and shown to encode the first enzyme in the pathway to the enterocin polyketide synthase starter unit benzoyl-coenzyme A. The disruption of the encP gene completely inhibited the production of cinnamate and enterocin, whereas complementation of the mutant with benzoyl-coenzyme A pathway intermediates or with the wild-type gene encP restored the formation of the benzoate-primed polyketide antibiotic enterocin. Heterologous expression of the encP gene under the control of the ermE* promoter in Streptomyces coelicolor furthermore led to the production of cinnamic acid in the fermented cultures, confirming that the encP gene indeed encodes a novel bacterial phenylalanine Ammonia-Lyase.
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inactivation complementation and heterologous expression ofencp a novel bacterial phenylalanine Ammonia Lyase gene
Journal of Biological Chemistry, 2002Co-Authors: Longkuan Xiang, Bradley S. MooreAbstract:Abstract The enzyme phenylalanine Ammonia-Lyase, which catalyzes the nonoxidative deamination ofl-phenylalanine to trans-cinnamic acid, is ubiquitously distributed in plants. We now report its characterization for the first time in a bacterium. The phenylalanine Ammonia-Lyase homologous gene encP from the “Streptomyces maritimus” enterocin biosynthetic gene cluster was functionally characterized and shown to encode the first enzyme in the pathway to the enterocin polyketide synthase starter unit benzoyl-coenzyme A. The disruption of the encP gene completely inhibited the production of cinnamate and enterocin, whereas complementation of the mutant with benzoyl-coenzyme A pathway intermediates or with the wild-type gene encP restored the formation of the benzoate-primed polyketide antibiotic enterocin. Heterologous expression of the encP gene under the control of the ermE* promoter in Streptomyces coelicolor furthermore led to the production of cinnamic acid in the fermented cultures, confirming that the encP gene indeed encodes a novel bacterial phenylalanine Ammonia-Lyase.
Shuhei Noda - One of the best experts on this subject based on the ideXlab platform.
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p hydroxycinnamic acid production directly from cellulose using endoglucanase and tyrosine Ammonia Lyase expressing streptomyces lividans
Microbial Cell Factories, 2013Co-Authors: Yoshifumi Kawai, Chiaki Ogino, Shuhei Noda, Naoko Okai, Yasunobu Takeshima, Tsutomu Tanaka, Akihiko KondoAbstract:p-Hydroxycinnamic acid (pHCA) is an aromatic compound that serves as a starting material for the production of many commercially valuable chemicals, such as fragrances and pharmaceuticals, and is also used in the synthesis of thermostable polymers. However, chemical synthesis of pHCA is both costly and harmful to the environment. Although pHCA production using microbes has been widely studied, there remains a need for more cost-effective methods, such as the use of biomass as a carbon source. In this study, we produced pHCA using tyrosine Ammonia Lyase-expressing Streptomyces lividans. In order to improve pHCA productivity from cellulose, we constructed a tyrosine Ammonia Lyase- and endoglucanase (EG)-expressing S. lividans transformant and used it to produce pHCA from cellulose. A Streptomyces lividans transformant was constructed to express tyrosine Ammonia Lyase derived from Rhodobacter sphaeroides (RsTAL). The transformant produced 786 or 736 mg/L of pHCA after 7 days of cultivation in medium containing 1% glucose or cellobiose as the carbon source, respectively. To enhance pHCA production from phosphoric acid swollen cellulose (PASC), we introduced the gene encoding EG into RsTAL-expressing S. lividans. After 7 days of cultivation, this transformant produced 753, 743, or 500 mg/L of pHCA from 1% glucose, cellobiose, or PASC, respectively. RsTAL-expressing S. lividans can produce pHCA from glucose and cellobiose. Similarly, RsTAL- and EG-expressing S. lividans can produce pHCA from glucose and cellobiose with excess EG activity remaining in the supernatant. This transformant demonstrated improved pHCA production from cellulose. Further enhancements in the cellulose degradation capability of the transformant will be necessary in order to achieve further improvements in pHCA production from cellulose.
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p hydroxycinnamic acid production directly from cellulose using endoglucanase and tyrosine Ammonia Lyase expressing streptomyces lividans
Microbial Cell Factories, 2013Co-Authors: Yoshifumi Kawai, Chiaki Ogino, Shuhei Noda, Naoko Okai, Yasunobu Takeshima, Tsutomu Tanaka, Akihiko KondoAbstract:Background p-Hydroxycinnamic acid (pHCA) is an aromatic compound that serves as a starting material for the production of many commercially valuable chemicals, such as fragrances and pharmaceuticals, and is also used in the synthesis of thermostable polymers. However, chemical synthesis of pHCA is both costly and harmful to the environment. Although pHCA production using microbes has been widely studied, there remains a need for more cost-effective methods, such as the use of biomass as a carbon source. In this study, we produced pHCA using tyrosine Ammonia Lyase-expressing Streptomyces lividans. In order to improve pHCA productivity from cellulose, we constructed a tyrosine Ammonia Lyase- and endoglucanase (EG)-expressing S. lividans transformant and used it to produce pHCA from cellulose.
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cinnamic acid production using streptomyces lividans expressing phenylalanine Ammonia Lyase
Journal of Industrial Microbiology & Biotechnology, 2011Co-Authors: Shuhei Noda, Takaya Miyazaki, Takanori Miyoshi, Michiru Miyake, Naoko Okai, Chiaki OginoAbstract:Cinnamic acid production was demonstrated using Streptomyces as a host. A gene encoding phenylalanine Ammonia Lyase (PAL) from Streptomyces maritimus was introduced into Streptomyces lividans, and its expression was confirmed by Western blot analysis. After 4 days cultivation using glucose as carbon source, the maximal level of cinnamic acid reached 210 mg/L. When glycerol (30 g/L) was used as carbon source, the maximal level of produced cinnamic acid reached 450 mg/L. In addition, using raw starch, xylose or xylan as carbon source, the maximal level of cinnamic acid reached 460, 300, and 130 mg/L, respectively. We demonstrated that S. lividans has great potential to produce cinnamic acid as well as other aromatic compounds.
Naoko Okai - One of the best experts on this subject based on the ideXlab platform.
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p hydroxycinnamic acid production directly from cellulose using endoglucanase and tyrosine Ammonia Lyase expressing streptomyces lividans
Microbial Cell Factories, 2013Co-Authors: Yoshifumi Kawai, Chiaki Ogino, Shuhei Noda, Naoko Okai, Yasunobu Takeshima, Tsutomu Tanaka, Akihiko KondoAbstract:p-Hydroxycinnamic acid (pHCA) is an aromatic compound that serves as a starting material for the production of many commercially valuable chemicals, such as fragrances and pharmaceuticals, and is also used in the synthesis of thermostable polymers. However, chemical synthesis of pHCA is both costly and harmful to the environment. Although pHCA production using microbes has been widely studied, there remains a need for more cost-effective methods, such as the use of biomass as a carbon source. In this study, we produced pHCA using tyrosine Ammonia Lyase-expressing Streptomyces lividans. In order to improve pHCA productivity from cellulose, we constructed a tyrosine Ammonia Lyase- and endoglucanase (EG)-expressing S. lividans transformant and used it to produce pHCA from cellulose. A Streptomyces lividans transformant was constructed to express tyrosine Ammonia Lyase derived from Rhodobacter sphaeroides (RsTAL). The transformant produced 786 or 736 mg/L of pHCA after 7 days of cultivation in medium containing 1% glucose or cellobiose as the carbon source, respectively. To enhance pHCA production from phosphoric acid swollen cellulose (PASC), we introduced the gene encoding EG into RsTAL-expressing S. lividans. After 7 days of cultivation, this transformant produced 753, 743, or 500 mg/L of pHCA from 1% glucose, cellobiose, or PASC, respectively. RsTAL-expressing S. lividans can produce pHCA from glucose and cellobiose. Similarly, RsTAL- and EG-expressing S. lividans can produce pHCA from glucose and cellobiose with excess EG activity remaining in the supernatant. This transformant demonstrated improved pHCA production from cellulose. Further enhancements in the cellulose degradation capability of the transformant will be necessary in order to achieve further improvements in pHCA production from cellulose.
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p hydroxycinnamic acid production directly from cellulose using endoglucanase and tyrosine Ammonia Lyase expressing streptomyces lividans
Microbial Cell Factories, 2013Co-Authors: Yoshifumi Kawai, Chiaki Ogino, Shuhei Noda, Naoko Okai, Yasunobu Takeshima, Tsutomu Tanaka, Akihiko KondoAbstract:Background p-Hydroxycinnamic acid (pHCA) is an aromatic compound that serves as a starting material for the production of many commercially valuable chemicals, such as fragrances and pharmaceuticals, and is also used in the synthesis of thermostable polymers. However, chemical synthesis of pHCA is both costly and harmful to the environment. Although pHCA production using microbes has been widely studied, there remains a need for more cost-effective methods, such as the use of biomass as a carbon source. In this study, we produced pHCA using tyrosine Ammonia Lyase-expressing Streptomyces lividans. In order to improve pHCA productivity from cellulose, we constructed a tyrosine Ammonia Lyase- and endoglucanase (EG)-expressing S. lividans transformant and used it to produce pHCA from cellulose.
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cinnamic acid production using streptomyces lividans expressing phenylalanine Ammonia Lyase
Journal of Industrial Microbiology & Biotechnology, 2011Co-Authors: Shuhei Noda, Takaya Miyazaki, Takanori Miyoshi, Michiru Miyake, Naoko Okai, Chiaki OginoAbstract:Cinnamic acid production was demonstrated using Streptomyces as a host. A gene encoding phenylalanine Ammonia Lyase (PAL) from Streptomyces maritimus was introduced into Streptomyces lividans, and its expression was confirmed by Western blot analysis. After 4 days cultivation using glucose as carbon source, the maximal level of cinnamic acid reached 210 mg/L. When glycerol (30 g/L) was used as carbon source, the maximal level of produced cinnamic acid reached 450 mg/L. In addition, using raw starch, xylose or xylan as carbon source, the maximal level of cinnamic acid reached 460, 300, and 130 mg/L, respectively. We demonstrated that S. lividans has great potential to produce cinnamic acid as well as other aromatic compounds.