Conditions for the overproduction and excretion of thermostable ?-amylase and pullulanase from Clostridium thermohydrosulfuricum DSM 567

G. Antranikian; P. Zablowski; G. Gottschalk

doi:10.1007/bf00257257

Conditions for the overproduction and excretion of thermostable ?-amylase and pullulanase from Clostridium thermohydrosulfuricum DSM 567

Applied Microbiology and Biotechnology ◽

10.1007/bf00257257 ◽

1987 ◽

Vol 27 (1) ◽

Cited By ~ 27

Author(s):

G. Antranikian ◽

P. Zablowski ◽

G. Gottschalk

Keyword(s):

Clostridium Thermohydrosulfuricum ◽

Thermostable Amylase

Effect of Carbon Source on Production of Thermostable -Amylase, Pullulanase and -Glucosidase by Clostridium Thermohydrosulfuricum

Microbiology ◽

10.1099/00221287-133-4-883 ◽

1987 ◽

Vol 133 (4) ◽

pp. 883-890 ◽

Cited By ~ 1

Author(s):

H. Melasniemi

Keyword(s):

Carbon Source ◽

Clostridium Thermohydrosulfuricum ◽

Thermostable Amylase

Characterization of α-amylase and pullulanase activities of Clostridium thermohydrosulfuricum. Evidence for a novel thermostable amylase

Biochemical Journal ◽

10.1042/bj2460193 ◽

1987 ◽

Vol 246 (1) ◽

pp. 193-197 ◽

Cited By ~ 34

Author(s):

H Melasniemi

Keyword(s):

High Temperatures ◽

Isoelectric Focusing ◽

Enzyme Preparation ◽

Crude Enzyme ◽

Crude Enzyme Preparation ◽

Identical Manner ◽

Clostridium Thermohydrosulfuricum ◽

Thermostable Amylase

Thermostable extracellular α-amylase and pullulanase activities of Clostridium thermohydrosulfuricum E 101-69 were characterized in a crude enzyme preparation. The activities responded similarly to temperature and pH, with optima at 85-90 degrees C and pH 5.6. The activities were stable at 65 degrees C, but were inactivated gradually in an identical manner at higher temperatures in the absence of Ca2+ and substrate. Ca2+ stabilized both activities similarly at high temperatures. Ca2+ also stimulated both activities, whereas EDTA reversed this stimulation. The activities were similarly inactivated at pH extremes. The two activities distributed in the same way during isoelectric focusing. The results suggest that the two activities are properties of the same protein, representing a novel, thermostable, amylase.

Exemplar Abstract for Thermoanaerobacter thermohydrosulfuricus (Klaushofer and Parkkinen 1965) Lee et al. 1993 and Clostridium thermohydrosulfuricum Klaushofer and Parkkinen 1965 (Approved Lists 1980).

The NamesforLife Abstracts ◽

10.1601/ex.4039 ◽

2003 ◽

Author(s):

Charles Thomas Parker ◽

Dorothea Taylor ◽

George M Garrity

Keyword(s):

Clostridium Thermohydrosulfuricum

Statistical optimization of a novel extracellular alkaline and thermostable amylase production from thermophilic Actinomadura keratinilytica sp. Cpt29 and its potential application in detergent industry

Biocatalysis and Agricultural Biotechnology ◽

10.1016/j.bcab.2021.102068 ◽

2021 ◽

pp. 102068

Author(s):

Marwa Kherouf ◽

Amina Habbeche ◽

Fatiha Benamia ◽

Boudjema Saoudi ◽

Bilal Kerouaz ◽

...

Keyword(s):

Potential Application ◽

Statistical Optimization ◽

Detergent Industry ◽

Amylase Production ◽

Thermostable Amylase

Thermostable amylase from an aerobic, gram-negative, non-spore forming thermophilic bacterium

Biotechnology Letters ◽

10.1007/bf01024399 ◽

1990 ◽

Vol 12 (6) ◽

pp. 433-438 ◽

Cited By ~ 4

Author(s):

Anwar Sunna ◽

Fuad Hashwa

Keyword(s):

Thermophilic Bacterium ◽

Gram Negative ◽

Thermostable Amylase

Corrigendum to “Enzymatic preparation of maltohexaose, maltoheptaose, and maltooctaose by the preferential cyclomaltooligosaccharide (cyclodextrin) ring-opening reaction of Pyrococcus furiosus thermostable amylase”

Carbohydrate Research ◽

10.1016/j.carres.2006.02.016 ◽

2006 ◽

Vol 341 (9) ◽

pp. 1192 ◽

Cited By ~ 1

Author(s):

Sung-Jae Yang ◽

Hee-Seob Lee ◽

Jung-Woo Kim ◽

Myoung-Hee Lee ◽

Joong-Hyuck Auh ◽

...

Keyword(s):

Ring Opening ◽

Pyrococcus Furiosus ◽

Enzymatic Preparation ◽

Ring Opening Reaction ◽

Thermostable Amylase

The α-Amylase-Pullulanase (apu) Gene from Clostridium thermohydrosulfuricum: Nucleotide Sequence and Expression in Escherichia coli

Brock/Springer Series in Contemporary Bioscience - Genetics and Molecular Biology of Anaerobic Bacteria ◽

10.1007/978-1-4615-7087-5_32 ◽

1993 ◽

pp. 432-442

Author(s):

Hannes Melasniemi

Keyword(s):

Escherichia Coli ◽

Nucleotide Sequence ◽

Expression In Escherichia Coli ◽

Clostridium Thermohydrosulfuricum

Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70.

Journal of Bacteriology ◽

10.1128/jb.174.7.2236-2240.1992 ◽

1992 ◽

Vol 174 (7) ◽

pp. 2236-2240 ◽

Cited By ~ 41

Author(s):

P Messner ◽

R Christian ◽

J Kolbe ◽

G Schulz ◽

U B Sleytr

Keyword(s):

Surface Layer ◽

Crystalline Surface ◽

Clostridium Thermohydrosulfuricum

Silica carriers for immobilization of thermostable ?-amylase

Acta Biotechnologica ◽

10.1002/abio.370110318 ◽

1991 ◽

Vol 11 (3) ◽

pp. 263-268 ◽

Cited By ~ 4

Author(s):

E. Dobreva ◽

V. Ivanova

Keyword(s):

Thermostable Amylase

Purification and characterization of thermostable amylase from a strain of thermoactinomyces thalpophilus KSV 17

Rajiv Gandhi University of Health Sciences Journal of Pharmaceutical Sciences ◽

10.5530/rjps.2012.1.12 ◽

2012 ◽

Vol 2 (1) ◽

pp. 83-89 ◽

Cited By ~ 3

Author(s):

Sreenivasa Rao ◽

P Ellaiah ◽

Karnakumar V Biradar

Keyword(s):

Purification And Characterization ◽

Thermostable Amylase