Enhanced maltose production through mutagenesis of acceptor binding subsite +2 in Bacillus stearothermophilus maltogenic amylase

2016 ◽  
Vol 217 ◽  
pp. 53-61 ◽  
Author(s):  
Yecheng Sun ◽  
Xuguo Duan ◽  
Lei Wang ◽  
Jing Wu
Keyword(s):  
Bacillus Stearothermophilus ◽  
Maltogenic Amylase

Transglycosylation of tagatose with maltotriose by Bacillus stearothermophilus maltogenic amylase (BSMA)

2005 ◽  
Vol 16 (1) ◽  
pp. 77-82 ◽  
Author(s):  
Hoe-Jin Roh ◽  
Su-Cheol Kang ◽  
Hee-Seob Lee ◽  
Doo-Kyung Kim ◽  
Sung-Bae Byun ◽  
...  
Keyword(s):  
Bacillus Stearothermophilus ◽  
Maltogenic Amylase

Synthesis of acarbose transfer products by Bacillus stearothermophilus maltogenic amylase with simmondsin

2000 ◽  
Vol 12 (3) ◽  
pp. 173-182 ◽  
Author(s):  
Jin Sook Baek ◽  
Hye Young Kim ◽  
Seung Seok Yoo ◽  
Tae Kyou Cheong ◽  
Myo Jeong Kim ◽  
...  
Keyword(s):  
Bacillus Stearothermophilus ◽  
Maltogenic Amylase

Preparation and characterization of maltosyl-sucrose isomers produced by transglycosylation of maltogenic amylase from Bacillus stearothermophilus

2003 ◽  
Vol 26 (3-6) ◽  
pp. 293-305 ◽  
Author(s):  
Hye-Young Lee ◽  
Myo-Jeong Kim ◽  
Jin-Sook Baek ◽  
Hee-Seob Lee ◽  
Hyun-Ju Cha ◽  
...  
Keyword(s):  
Bacillus Stearothermophilus ◽  
Maltogenic Amylase

scholarly journals Bacillus stearothermophilus Neopullulanase Selective Hydrolysis of Amylose to Maltose in the Presence of Amylopectin

2002 ◽  
Vol 68 (4) ◽  
pp. 1658-1664 ◽  
Author(s):  
Hiroshi Kamasaka ◽  
Kazuhisa Sugimoto ◽  
Hiroki Takata ◽  
Takahisa Nishimura ◽  
Takashi Kuriki
Keyword(s):  
Substrate Specificity ◽  
Bacillus Licheniformis ◽  
Bacillus Megaterium ◽  
Bacillus Stearothermophilus ◽  
Main Product ◽  
Selective Hydrolysis ◽  
Amylolytic Enzymes ◽  
Order Of Magnitude ◽  
Maltogenic Amylase ◽  
Hydrolysis Of

ABSTRACT The specificity of Bacillus stearothermophilus TRS40 neopullulanase toward amylose and amylopectin was analyzed. Although this neopullulanase completely hydrolyzed amylose to produce maltose as the main product, it scarcely hydrolyzed amylopectin. The molecular mass of amylopectin was decreased by only one order of magnitude, from approximately 108 to 107 Da. Furthermore, this neopullulanase selectively hydrolyzed amylose when starch was used as a substrate. This phenomenon, efficient hydrolysis of amylose but not amylopectin, was also observed with cyclomaltodextrinase from alkaliphilic Bacillus sp. strain A2-5a and maltogenic amylase from Bacillus licheniformis ATCC 27811. These three enzymes hydrolyzed cyclomaltodextrins and amylose much faster than pullulan. Other amylolytic enzymes, such as bacterial saccharifying α-amylase, bacterial liquefying α-amylase, β-amylase, and neopullulanase from Bacillus megaterium, did not exhibit this distinct substrate specificity at all, i.e., the preference of amylose to amylopectin.

Preliminary X-ray crystallographic analysis of a novel maltogenic amylase from Bacillus stearothermophilus ET1

1998 ◽  
Vol 54 (3) ◽  
pp. 416-418 ◽  
Author(s):  
Moon-Ju Cho ◽  
Sun-Shin Cha ◽  
Jong-Hyeok Park ◽  
Hyun-Ju Cha ◽  
Hee-Seob Lee ◽  
...  
Keyword(s):  
Bacillus Stearothermophilus ◽  
Crystallographic Analysis ◽  
Glycosidic Bond ◽  
Diffusion Method ◽  
High Concentration ◽  
Unit Structure ◽  
Isomorphous Replacement ◽  
Cell Dimensions ◽  
Maltogenic Amylase ◽  
Unit Cell Dimensions

A novel maltogenic amylase from Bacillus stearothermophilus ET1, which has a dual activity of α-1,4- and α-1,6-glycosidic bond cleavages and α-1,6-glycosidic bond formation, was crystallized by using the hanging-drop vapor-diffusion method. The best crystals were obtained by employing a high concentration of protein (56 mg ml−1) and a precipitant containing 22% glycerol, 1.6 M ammonium sulfate in 0.1 M Tris–HCl (pH 8.5). Native diffraction data to 2.66 Å resolution have been obtained from crystals flash-frozen at 110 K. The crystals belong to the space group P212121 with unit-cell dimensions of a = 77.62, b = 121.23, c = 244.29 Å, and contain three or four protomers per asymmetric unit. Structure determination by multiple isomorphous replacement is in progress.

Transglycosylation reactions of Bacillus stearothermophilus maltogenic amylase with acarbose and various acceptors

1998 ◽  
Vol 313 (3-4) ◽  
pp. 235-246 ◽  
Author(s):  
Kwan Hwa Park ◽  
Myo Jeong Kim ◽  
Hee Seob Lee ◽  
Nam Soo Han ◽  
Doman Kim ◽  
...  
Keyword(s):  
Bacillus Stearothermophilus ◽  
Maltogenic Amylase

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.

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