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Immunocytochemical Identification and Localization of Active and Inactive alpha-Amylase and Pullulanase in Cells of Clostridium thermosulfurogenes EM1.

Applied and environmental microbiology

Specka U, Spreinat A, Antranikian G, Mayer F.
PMID: 16348456
Appl Environ Microbiol. 1991 Apr;57(4):1062-9. doi: 10.1128/aem.57.4.1062-1069.1991.

Clostridium thermosulfurogenes EM1 formed blebs, i.e., protrusions still in contact with the cytoplasmic membrane, that originated from the cytoplasmic membrane during growth in batch culture and continuous culture. They could be observed squeezed between the cell wall and cytoplasmic...

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Specka U, Spreinat A, Antranikian G, et al. Immunocytochemical Identification and Localization of Active and Inactive alpha-Amylase and Pullulanase in Cells of Clostridium thermosulfurogenes EM1. Appl Environ Microbiol. 1991;57(4):1062-9doi: 10.1128/aem.57.4.1062-1069.1991.
Specka, U., Spreinat, A., Antranikian, G., & Mayer, F. (1991). Immunocytochemical Identification and Localization of Active and Inactive alpha-Amylase and Pullulanase in Cells of Clostridium thermosulfurogenes EM1. Applied and environmental microbiology, 57(4), 1062-9. https://doi.org/10.1128/aem.57.4.1062-1069.1991
Specka, U, et al. "Immunocytochemical Identification and Localization of Active and Inactive alpha-Amylase and Pullulanase in Cells of Clostridium thermosulfurogenes EM1." Applied and environmental microbiology vol. 57,4 (1991): 1062-9. doi: https://doi.org/10.1128/aem.57.4.1062-1069.1991
Specka U, Spreinat A, Antranikian G, Mayer F. Immunocytochemical Identification and Localization of Active and Inactive alpha-Amylase and Pullulanase in Cells of Clostridium thermosulfurogenes EM1. Appl Environ Microbiol. 1991 Apr;57(4):1062-9. doi: 10.1128/aem.57.4.1062-1069.1991. PMID: 16348456; PMCID: PMC182846.
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Thermostable amylolytic enzymes from a new clostridium isolate.

Applied and environmental microbiology

Madi E, Antranikian G, Ohmiya K, Gottschalk G.
PMID: 16347392
Appl Environ Microbiol. 1987 Jul;53(7):1661-7. doi: 10.1128/aem.53.7.1661-1667.1987.

A new Clostridium strain was isolated on starch at 60 degrees C. Starch, pullulan, maltotriose, and maltose induced the synthesis of alpha-amylase and pullulanase, while glucose, ribose, fructose, and lactose did not. The formation of the amylolytic enzymes was...

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Madi E, Antranikian G, Ohmiya K, et al. Thermostable amylolytic enzymes from a new clostridium isolate. Appl Environ Microbiol. 1987;53(7):1661-7doi: 10.1128/aem.53.7.1661-1667.1987.
Madi, E., Antranikian, G., Ohmiya, K., & Gottschalk, G. (1987). Thermostable amylolytic enzymes from a new clostridium isolate. Applied and environmental microbiology, 53(7), 1661-7. https://doi.org/10.1128/aem.53.7.1661-1667.1987
Madi, E, et al. "Thermostable amylolytic enzymes from a new clostridium isolate." Applied and environmental microbiology vol. 53,7 (1987): 1661-7. doi: https://doi.org/10.1128/aem.53.7.1661-1667.1987
Madi E, Antranikian G, Ohmiya K, Gottschalk G. Thermostable amylolytic enzymes from a new clostridium isolate. Appl Environ Microbiol. 1987 Jul;53(7):1661-7. doi: 10.1128/aem.53.7.1661-1667.1987. PMID: 16347392; PMCID: PMC203927.
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Purification and Properties of a Highly Thermostable, Sodium Dodecyl Sulfate-Resistant and Stereospecific Proteinase from the Extremely Thermophilic Archaeon Thermococcus stetteri.

Applied and environmental microbiology

Klingeberg M, Galunsky B, Sjoholm C, Kasche V, Antranikian G.
PMID: 16535107
Appl Environ Microbiol. 1995 Aug;61(8):3098-104. doi: 10.1128/aem.61.8.3098-3104.1995.

The cultivation of the extremely thermophilic archaeon Thermococcus stetteri in a dialysis membrane reactor was paralleled by the production of an extremely heat-stable proteinase(s). By applying preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, an SDS-resistant proteinase was purified 67-fold...

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Klingeberg M, Galunsky B, Sjoholm C, et al. Purification and Properties of a Highly Thermostable, Sodium Dodecyl Sulfate-Resistant and Stereospecific Proteinase from the Extremely Thermophilic Archaeon Thermococcus stetteri. Appl Environ Microbiol. 1995;61(8):3098-104doi: 10.1128/aem.61.8.3098-3104.1995.
Klingeberg, M., Galunsky, B., Sjoholm, C., Kasche, V., & Antranikian, G. (1995). Purification and Properties of a Highly Thermostable, Sodium Dodecyl Sulfate-Resistant and Stereospecific Proteinase from the Extremely Thermophilic Archaeon Thermococcus stetteri. Applied and environmental microbiology, 61(8), 3098-104. https://doi.org/10.1128/aem.61.8.3098-3104.1995
Klingeberg, M, et al. "Purification and Properties of a Highly Thermostable, Sodium Dodecyl Sulfate-Resistant and Stereospecific Proteinase from the Extremely Thermophilic Archaeon Thermococcus stetteri." Applied and environmental microbiology vol. 61,8 (1995): 3098-104. doi: https://doi.org/10.1128/aem.61.8.3098-3104.1995
Klingeberg M, Galunsky B, Sjoholm C, Kasche V, Antranikian G. Purification and Properties of a Highly Thermostable, Sodium Dodecyl Sulfate-Resistant and Stereospecific Proteinase from the Extremely Thermophilic Archaeon Thermococcus stetteri. Appl Environ Microbiol. 1995 Aug;61(8):3098-104. doi: 10.1128/aem.61.8.3098-3104.1995. PMID: 16535107; PMCID: PMC1388561.
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Towards a sustainable biobased industry - Highlighting the impact of extremophiles.

New biotechnology

Krüger A, Schäfers C, Schröder C, Antranikian G.
PMID: 28512003
N Biotechnol. 2018 Jan 25;40:144-153. doi: 10.1016/j.nbt.2017.05.002. Epub 2017 May 13.

The transition of the oil-based economy towards a sustainable economy completely relying on biomass as renewable feedstock requires the concerted action of academia, industry, politics and civil society. An interdisciplinary approach of various fields such as microbiology, molecular biology,...

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Krüger A, Schäfers C, Schröder C, et al. Towards a sustainable biobased industry - Highlighting the impact of extremophiles. N Biotechnol. 2017;40:144-153doi: 10.1016/j.nbt.2017.05.002.
Krüger, A., Schäfers, C., Schröder, C., & Antranikian, G. (2018). Towards a sustainable biobased industry - Highlighting the impact of extremophiles. New biotechnology, 40144-153. https://doi.org/10.1016/j.nbt.2017.05.002
Krüger, Anna, et al. "Towards a sustainable biobased industry - Highlighting the impact of extremophiles." New biotechnology vol. 40 (2018): 144-153. doi: https://doi.org/10.1016/j.nbt.2017.05.002
Krüger A, Schäfers C, Schröder C, Antranikian G. Towards a sustainable biobased industry - Highlighting the impact of extremophiles. N Biotechnol. 2018 Jan 25;40:144-153. doi: 10.1016/j.nbt.2017.05.002. Epub 2017 May 13. PMID: 28512003.
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Biomass-degrading glycoside hydrolases of archaeal origin.

Biotechnology for biofuels

Suleiman M, Krüger A, Antranikian G.
PMID: 32905355
Biotechnol Biofuels. 2020 Sep 02;13:153. doi: 10.1186/s13068-020-01792-y. eCollection 2020.

During the last decades, the impact of hyperthermophiles and their enzymes has been intensively investigated for implementation in various high-temperature biotechnological processes. Biocatalysts of hyperthermophiles have proven to show extremely high thermo-activities and thermo-stabilities and are identified as suitable...

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Suleiman M, Krüger A, Antranikian G. Biomass-degrading glycoside hydrolases of archaeal origin. Biotechnol Biofuels. 2020;13:153doi: 10.1186/s13068-020-01792-y.
Suleiman, M., Krüger, A., & Antranikian, G. (2020). Biomass-degrading glycoside hydrolases of archaeal origin. Biotechnology for biofuels, 13153. https://doi.org/10.1186/s13068-020-01792-y
Suleiman, Marcel, et al. "Biomass-degrading glycoside hydrolases of archaeal origin." Biotechnology for biofuels vol. 13 (2020): 153. doi: https://doi.org/10.1186/s13068-020-01792-y
Suleiman M, Krüger A, Antranikian G. Biomass-degrading glycoside hydrolases of archaeal origin. Biotechnol Biofuels. 2020 Sep 02;13:153. doi: 10.1186/s13068-020-01792-y. eCollection 2020. PMID: 32905355; PMCID: PMC7469102.
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Keratin Degradation by Fervidobacterium pennavorans, a Novel Thermophilic Anaerobic Species of the Order Thermotogales.

Applied and environmental microbiology

Friedrich AB, Antranikian G.
PMID: 16535379
Appl Environ Microbiol. 1996 Aug;62(8):2875-82. doi: 10.1128/aem.62.8.2875-2882.1996.

From a hot spring of the Azores islands a novel thermophilic bacterium belonging to the Thermotogales order was isolated. This strain, which grows optimally at 70(deg)C and pH 6.5, is the first known extreme thermophile that is able to...

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Friedrich AB, Antranikian G. Keratin Degradation by Fervidobacterium pennavorans, a Novel Thermophilic Anaerobic Species of the Order Thermotogales. Appl Environ Microbiol. 1996;62(8):2875-82doi: 10.1128/aem.62.8.2875-2882.1996.
Friedrich, A. B., & Antranikian, G. (1996). Keratin Degradation by Fervidobacterium pennavorans, a Novel Thermophilic Anaerobic Species of the Order Thermotogales. Applied and environmental microbiology, 62(8), 2875-82. https://doi.org/10.1128/aem.62.8.2875-2882.1996
Friedrich, A B, and Antranikian, G. "Keratin Degradation by Fervidobacterium pennavorans, a Novel Thermophilic Anaerobic Species of the Order Thermotogales." Applied and environmental microbiology vol. 62,8 (1996): 2875-82. doi: https://doi.org/10.1128/aem.62.8.2875-2882.1996
Friedrich AB, Antranikian G. Keratin Degradation by Fervidobacterium pennavorans, a Novel Thermophilic Anaerobic Species of the Order Thermotogales. Appl Environ Microbiol. 1996 Aug;62(8):2875-82. doi: 10.1128/aem.62.8.2875-2882.1996. PMID: 16535379; PMCID: PMC1388917.
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Purification and Properties of a Thermostable Pullulanase from a Newly Isolated Thermophilic Anaerobic Bacterium, Fervidobacterium pennavorans Ven5.

Applied and environmental microbiology

Koch R, Canganella F, Hippe H, Jahnke KD, Antranikian G.
PMID: 16535541
Appl Environ Microbiol. 1997 Mar;63(3):1088-94. doi: 10.1128/aem.63.3.1088-1094.1997.

Extremely thermophilic anaerobic fermentative bacteria growing at temperatures between 50 and 80(deg)C (optimum, 65 to 70(deg)C) were isolated from mud samples collected at Abano Terme spa (Italy). The cells were gram-negative motile rods, about 1.8 (mu)m in length and...

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Koch R, Canganella F, Hippe H, et al. Purification and Properties of a Thermostable Pullulanase from a Newly Isolated Thermophilic Anaerobic Bacterium, Fervidobacterium pennavorans Ven5. Appl Environ Microbiol. 1997;63(3):1088-94doi: 10.1128/aem.63.3.1088-1094.1997.
Koch, R., Canganella, F., Hippe, H., Jahnke, K. D., & Antranikian, G. (1997). Purification and Properties of a Thermostable Pullulanase from a Newly Isolated Thermophilic Anaerobic Bacterium, Fervidobacterium pennavorans Ven5. Applied and environmental microbiology, 63(3), 1088-94. https://doi.org/10.1128/aem.63.3.1088-1094.1997
Koch, R, et al. "Purification and Properties of a Thermostable Pullulanase from a Newly Isolated Thermophilic Anaerobic Bacterium, Fervidobacterium pennavorans Ven5." Applied and environmental microbiology vol. 63,3 (1997): 1088-94. doi: https://doi.org/10.1128/aem.63.3.1088-1094.1997
Koch R, Canganella F, Hippe H, Jahnke KD, Antranikian G. Purification and Properties of a Thermostable Pullulanase from a Newly Isolated Thermophilic Anaerobic Bacterium, Fervidobacterium pennavorans Ven5. Appl Environ Microbiol. 1997 Mar;63(3):1088-94. doi: 10.1128/aem.63.3.1088-1094.1997. PMID: 16535541; PMCID: PMC1389135.
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Production of Thermostable alpha-Amylase, Pullulanase, and alpha-Glucosidase in Continuous Culture by a New Clostridium Isolate.

Applied and environmental microbiology

Antranikian G, Herzberg C, Gottschalk G.
PMID: 16347393
Appl Environ Microbiol. 1987 Jul;53(7):1668-73. doi: 10.1128/aem.53.7.1668-1673.1987.

The production of alpha-amylase, pullulanase, and alpha-glucosidase and the formation of fermentation products by the newly isolated thermophilic Clostridium sp. strain EM1 were investigated in continuous culture with a defined medium and an incubation temperature of 60 degrees C....

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Antranikian G, Herzberg C, Gottschalk G. Production of Thermostable alpha-Amylase, Pullulanase, and alpha-Glucosidase in Continuous Culture by a New Clostridium Isolate. Appl Environ Microbiol. 1987;53(7):1668-73doi: 10.1128/aem.53.7.1668-1673.1987.
Antranikian, G., Herzberg, C., & Gottschalk, G. (1987). Production of Thermostable alpha-Amylase, Pullulanase, and alpha-Glucosidase in Continuous Culture by a New Clostridium Isolate. Applied and environmental microbiology, 53(7), 1668-73. https://doi.org/10.1128/aem.53.7.1668-1673.1987
Antranikian, G, et al. "Production of Thermostable alpha-Amylase, Pullulanase, and alpha-Glucosidase in Continuous Culture by a New Clostridium Isolate." Applied and environmental microbiology vol. 53,7 (1987): 1668-73. doi: https://doi.org/10.1128/aem.53.7.1668-1673.1987
Antranikian G, Herzberg C, Gottschalk G. Production of Thermostable alpha-Amylase, Pullulanase, and alpha-Glucosidase in Continuous Culture by a New Clostridium Isolate. Appl Environ Microbiol. 1987 Jul;53(7):1668-73. doi: 10.1128/aem.53.7.1668-1673.1987. PMID: 16347393; PMCID: PMC203928.
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Heat-stable enzymes from extremely thermophilic and hyperthermophilic microorganisms.

World journal of microbiology & biotechnology

Leuschner C, Antranikian G.
PMID: 24414414
World J Microbiol Biotechnol. 1995 Jan;11(1):95-114. doi: 10.1007/BF00339139.

Only in the last decade have microorganisms been discovered which grow near or above 100°C. The enzymes that are formed by these extremely thermophilic (growth temperature 65 to 85°C) and hyperthermophilic (growth temperature 85 to 110°C) microorganisms are of...

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Leuschner C, Antranikian G. Heat-stable enzymes from extremely thermophilic and hyperthermophilic microorganisms. World J Microbiol Biotechnol. 1995;11(1):95-114doi: 10.1007/BF00339139.
Leuschner, C., & Antranikian, G. (1995). Heat-stable enzymes from extremely thermophilic and hyperthermophilic microorganisms. World journal of microbiology & biotechnology, 11(1), 95-114. https://doi.org/10.1007/BF00339139
Leuschner, C, and Antranikian, G. "Heat-stable enzymes from extremely thermophilic and hyperthermophilic microorganisms." World journal of microbiology & biotechnology vol. 11,1 (1995): 95-114. doi: https://doi.org/10.1007/BF00339139
Leuschner C, Antranikian G. Heat-stable enzymes from extremely thermophilic and hyperthermophilic microorganisms. World J Microbiol Biotechnol. 1995 Jan;11(1):95-114. doi: 10.1007/BF00339139. PMID: 24414414.
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Complete genome sequence of Thermus brockianus GE-1 reveals key enzymes of xylan/xylose metabolism.

Standards in genomic sciences

Schäfers C, Blank S, Wiebusch S, Elleuche S, Antranikian G.
PMID: 28174620
Stand Genomic Sci. 2017 Feb 03;12:22. doi: 10.1186/s40793-017-0225-7. eCollection 2017.

No abstract available.

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Schäfers C, Blank S, Wiebusch S, et al. Complete genome sequence of Thermus brockianus GE-1 reveals key enzymes of xylan/xylose metabolism. Stand Genomic Sci. 2017;12:22doi: 10.1186/s40793-017-0225-7.
Schäfers, C., Blank, S., Wiebusch, S., Elleuche, S., & Antranikian, G. (2017). Complete genome sequence of Thermus brockianus GE-1 reveals key enzymes of xylan/xylose metabolism. Standards in genomic sciences, 1222. https://doi.org/10.1186/s40793-017-0225-7
Schäfers, Christian, et al. "Complete genome sequence of Thermus brockianus GE-1 reveals key enzymes of xylan/xylose metabolism." Standards in genomic sciences vol. 12 (2017): 22. doi: https://doi.org/10.1186/s40793-017-0225-7
Schäfers C, Blank S, Wiebusch S, Elleuche S, Antranikian G. Complete genome sequence of Thermus brockianus GE-1 reveals key enzymes of xylan/xylose metabolism. Stand Genomic Sci. 2017 Feb 03;12:22. doi: 10.1186/s40793-017-0225-7. eCollection 2017. PMID: 28174620; PMCID: PMC5292009.
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Purification and Properties of a Thermoactive Glucoamylase from Clostridium thermosaccharolyticum.

Applied and environmental microbiology

Specka U, Mayer F, Antranikian G.
PMID: 16348541
Appl Environ Microbiol. 1991 Aug;57(8):2317-23. doi: 10.1128/aem.57.8.2317-2323.1991.

A bacterial glucoamylase was purified from the anaerobic thermophilic bacterium Clostridium thermosaccharolyticum and characterized. The enzyme, which was purified 63-fold, with a yield of 36%, consisted of a single subunit with an apparent molecular mass of 75 kDa. The...

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Specka U, Mayer F, Antranikian G. Purification and Properties of a Thermoactive Glucoamylase from Clostridium thermosaccharolyticum. Appl Environ Microbiol. 1991;57(8):2317-23doi: 10.1128/aem.57.8.2317-2323.1991.
Specka, U., Mayer, F., & Antranikian, G. (1991). Purification and Properties of a Thermoactive Glucoamylase from Clostridium thermosaccharolyticum. Applied and environmental microbiology, 57(8), 2317-23. https://doi.org/10.1128/aem.57.8.2317-2323.1991
Specka, U, et al. "Purification and Properties of a Thermoactive Glucoamylase from Clostridium thermosaccharolyticum." Applied and environmental microbiology vol. 57,8 (1991): 2317-23. doi: https://doi.org/10.1128/aem.57.8.2317-2323.1991
Specka U, Mayer F, Antranikian G. Purification and Properties of a Thermoactive Glucoamylase from Clostridium thermosaccharolyticum. Appl Environ Microbiol. 1991 Aug;57(8):2317-23. doi: 10.1128/aem.57.8.2317-2323.1991. PMID: 16348541; PMCID: PMC183570.
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Preliminary crystallographic analysis of an extremely thermostable glutamate dehydrogenase from the archaeon Pyrococcus woesei.

Acta crystallographica. Section D, Biological crystallography

Knapp S, Karshikoff A, Waldkötter K, Rüdiger A, Antranikian G, Ladenstein R.
PMID: 15299309
Acta Crystallogr D Biol Crystallogr. 1995 May 01;51:395-8. doi: 10.1107/S0907444994011224.

The extremely heat-stable glutamate dehydrogenase (GluDH) from Pyrococcus woesei was crystallized by the hanging-drop vapour-diffusion method. Crystals suitable for X-ray crystallographic investigations were obtained using polyethylene glycol (PEG) 4000 and ammonium acetate as precipitating agents. The crystals obtained diffract...

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Knapp S, Karshikoff A, Waldkötter K, et al. Preliminary crystallographic analysis of an extremely thermostable glutamate dehydrogenase from the archaeon Pyrococcus woesei. Acta Crystallogr D Biol Crystallogr. 1995;51:395-8doi: 10.1107/S0907444994011224.
Knapp, S., Karshikoff, A., Waldkötter, K., Rüdiger, A., Antranikian, G., & Ladenstein, R. (1995). Preliminary crystallographic analysis of an extremely thermostable glutamate dehydrogenase from the archaeon Pyrococcus woesei. Acta crystallographica. Section D, Biological crystallography, 51395-8. https://doi.org/10.1107/S0907444994011224
Knapp, S, et al. "Preliminary crystallographic analysis of an extremely thermostable glutamate dehydrogenase from the archaeon Pyrococcus woesei." Acta crystallographica. Section D, Biological crystallography vol. 51 (1995): 395-8. doi: https://doi.org/10.1107/S0907444994011224
Knapp S, Karshikoff A, Waldkötter K, Rüdiger A, Antranikian G, Ladenstein R. Preliminary crystallographic analysis of an extremely thermostable glutamate dehydrogenase from the archaeon Pyrococcus woesei. Acta Crystallogr D Biol Crystallogr. 1995 May 01;51:395-8. doi: 10.1107/S0907444994011224. PMID: 15299309.
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