Exemplar Abstract for Geobacillus stearothermophilus (Donk 1920) Nazina et al. 2001 emend. Coorevits et al. 2012 and Bacillus stearothermophilus Donk 1920 (Approved Lists 1980).

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Nicole Danielle Osier ◽  
George M Garrity ◽  
Dorothea Taylor
Keyword(s):  
Bacillus Stearothermophilus ◽  
Geobacillus Stearothermophilus

Protein engineering applications of industrially exploitable enzymes: Geobacillus stearothermophilus LDH and Candida methylica FDH

2007 ◽  
Vol 35 (6) ◽  
pp. 1610-1615 ◽  
Author(s):  
N.G. Karagüler ◽  
R.B. Sessions ◽  
B. Binay ◽  
E.B. Ordu ◽  
A.R. Clarke
Keyword(s):  
Protein Engineering ◽  
Large Scale ◽  
Bacillus Stearothermophilus ◽  
Biological Properties ◽  
Site Directed Mutagenesis ◽  
Dna Shuffling ◽  
Directed Mutagenesis ◽  
Scale Production ◽  
Geobacillus Stearothermophilus ◽  
Coenzyme Specificity

Enzymes have become important tools in several industries due to their ability to produce chirally pure and complex molecules with interesting biological properties. The NAD+-dependent LDH (lactate dehydrogenase) [bsLDH [Geobacillus stearothermophilus (formerly Bacillus stearothermophilus) LDH] from G. stearothermophilus and the NAD+-dependent FDH (formate dehydrogenase) [cmFDH (Candida methylica FDH)] enzyme from C. methylica are particularly crucial enzymes in the pharmaceutical industry and are related to each other in terms of NADH use and regeneration. LDH catalyses the interconversion of pyruvate (oxo acid) and lactate (α-hydroxy acid) using the NADH/NAD+ pair as a redox cofactor. Employing LDH to reduce other oxo acids can generate chirally pure α-hydroxy acids of use in the production of pharmaceuticals. One important use of FDH is to regenerate the relatively expensive NADH cofactor that is used by NAD+-dependent oxidoreductases such as LDH. Both LDH and FDH from organisms of interest were previously cloned and overproduced. Therefore they are available at a low cost. However, both of these enzymes show disadvantages in the large-scale production of chirally pure compounds. We have applied two routes of protein engineering studies to improve the properties of these two enzymes, namely DNA shuffling and site-directed mutagenesis. Altering the substrate specificity of bsLDH by DNA shuffling and changing the coenzyme specificity of cmFDH by site-directed mutagenesis are the most successful examples of our studies. The present paper will also include the details of these examples together with some other applications of protein engineering regarding these enzymes.

Влияниe ферментативного трансгликозилирования гликозидов Стевии на их вкусовые характеристики

2019 ◽  
pp. 86-97
Author(s):  
Кристина Викторовна Чхан ◽  
Марина Борисовна Мойсеяк
Keyword(s):  
Bacillus Stearothermophilus

Ферментативное трансгликозилирование эффективно для структурной модификации биологически активных соединений, включая высокоинтенсивные подсластители. Проведена ферментативная модификация гликозидов стевии. В качестве продуцентов цикломальтодекстрин глюканотрансферазы (ЦГТазa) был использован Bacillus stearothermophilus St-88. ЦГТазa может быть эффективным биокатализатором в реакции трансглюкозилирования Ребаудиозида А, Ребаудиозида D и Ребаудиозида М в присутствии циклодекстринов и крахмала в качестве доноров. Показана возможность получения глюкозилированных гликозидов стевии с различной длиной боковых цепочек. Выделение и очистку индивидуальных производных РебD-G1/G2 осуществляли на 10-ти колонках, соединённых друг с другом. Использовали макропористую смолу Diaion HP-20 (аналогично РебD-G1/G2, проводили выделение и очистку РебM-G1/G2, РебA-G1/G2). Показано, что глюкозилированные гликозиды стевии могут быть превосходными высокоинтенсивными подсластителями, а также подходящими высокоактивными ингредиентами для модуляции вкусовых качеств немодифицированных гликозидов.

scholarly journals Thermostable α-Amylase of Bacillus stearothermophilus

1961 ◽  
Vol 236 (11) ◽  
pp. 2952-2957 ◽  
Author(s):  
Gilbert B. Manning ◽  
L. Leon Campbell
Keyword(s):  
Bacillus Stearothermophilus
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