Cyclodextrin production by cyclodextrin glycosyltransferase from Bacillus circulans DF 9R

2007 ◽  
Vol 98 (15) ◽  
pp. 2886-2891 ◽  
Author(s):  
Natalia Szerman ◽  
Ignacio Schroh ◽  
Ana Lía Rossi ◽  
Adriana Mabel Rosso ◽  
Norberto Krymkiewicz ◽  
...  
Keyword(s):  
Bacillus Circulans ◽  
Cyclodextrin Glycosyltransferase ◽  
Cyclodextrin Production

Rational design of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 to increase α-cyclodextrin production 1 1Edited by G. Von Heijne

2000 ◽  
Vol 296 (4) ◽  
pp. 1027-1038 ◽  
Author(s):  
Bart A van der Veen ◽  
Joost C.M Uitdehaag ◽  
Dirk Penninga ◽  
Gert-Jan W.M van Alebeek ◽  
Loraine M Smith ◽  
...  
Keyword(s):  
Rational Design ◽  
Bacillus Circulans ◽  
Cyclodextrin Glycosyltransferase ◽  
Cyclodextrin Production

scholarly journals The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms

2000 ◽  
Vol 267 (3) ◽  
pp. 658-665 ◽  
Author(s):  
Bart A. van der Veen ◽  
Gert-Jan W. M. van Alebeek ◽  
Joost C. M. Uitdehaag ◽  
Bauke W. Dijkstra ◽  
Lubbert Dijkhuizen
Keyword(s):  
Bacillus Circulans ◽  
Cyclodextrin Glycosyltransferase ◽  
Kinetic Mechanisms

Maltooligosaccharides production catalysed by cyclodextrin glycosyltransferase from Bacillus circulans DF 9R in batch and continuous operation

2012 ◽  
Vol 47 (12) ◽  
pp. 2562-2565 ◽  
Author(s):  
Jorgelina Andrea Rodríguez Gastón ◽  
Hernán Costa ◽  
Ana Lía Rossi ◽  
Norberto Krymkiewicz ◽  
Susana Alicia Ferrarotti
Keyword(s):  
Continuous Operation ◽  
Bacillus Circulans ◽  
Cyclodextrin Glycosyltransferase

Rapid Affinity Purification Processes for Cyclodextrin Glycosyltransferase from Bacillus circulans

2005 ◽  
Vol 27 (16) ◽  
pp. 1171-1175 ◽  
Author(s):  
A. Rosso ◽  
S. Ferrarotti ◽  
M.V. Miranda ◽  
N. Krymkiewicz ◽  
B.C. Nudel ◽  
...  
Keyword(s):  
Affinity Purification ◽  
Bacillus Circulans ◽  
Cyclodextrin Glycosyltransferase

Biochemical properties and cyclodextrin production profiles of isoforms of cyclodextrin glycosyltransferase

2010 ◽  
Vol 70 (3-4) ◽  
pp. 377-383 ◽  
Author(s):  
Wanchai Yenpetch ◽  
Kanoktip Packdibamrung ◽  
Wolfgang Zimmermann ◽  
Piamsook Pongsawasdi
Keyword(s):  
Biochemical Properties ◽  
Cyclodextrin Glycosyltransferase ◽  
Cyclodextrin Production

scholarly journals Enhancing the α-Cyclodextrin Specificity of Cyclodextrin Glycosyltransferase from Paenibacillus macerans by Mutagenesis Masking Subsite −7

2016 ◽  
Vol 82 (8) ◽  
pp. 2247-2255 ◽  
Author(s):  
Lei Wang ◽  
Xuguo Duan ◽  
Jing Wu
Keyword(s):  
Active Site ◽  
Wild Type ◽  
Cyclodextrin Glycosyltransferase ◽  
Wild Type Enzyme ◽  
Widespread Application ◽  
Content Type ◽  
Hydrogen Bonding Interactions ◽  
Paenibacillus Macerans ◽  
Site Blocking ◽  
Cyclodextrin Production

ABSTRACTCyclodextrin glycosyltransferases (CGTases) (EC 2.4.1.19) catalyze the conversion of starch or starch derivates into mixtures of α-, β-, and γ-cyclodextrins. Because time-consuming and expensive purification procedures hinder the widespread application of single-ingredient cyclodextrins, enzymes with enhanced specificity are needed. In this study, we tested the hypothesis that the α-cyclodextrin selectivity ofPaenibacillus maceransα-CGTase could be augmented by masking subsite −7 of the active site, blocking the formation of larger cyclodextrins, particularly β-cyclodextrin. Five single mutants and three double mutants designed to remove hydrogen-bonding interactions between the enzyme and substrate at subsite −7 were constructed and characterized in detail. Although the rates of α-cyclodextrin formation varied only modestly, the rate of β-cyclodextrin formation decreased dramatically in these mutants. The increase in α-cyclodextrin selectivity was directly proportional to the increase in the ratio of theirkcatvalues for α- and β-cyclodextrin formation. The R146A/D147P and R146P/D147A double mutants exhibited ratios of α-cyclodextrin to total cyclodextrin production of 75.1% and 76.1%, approximately one-fifth greater than that of the wild-type enzyme (63.2%), without loss of thermostability. Thus, these double mutants may be more suitable for the industrial production of α-cyclodextrin than the wild-type enzyme. The production of β-cyclodextrin by these mutants was almost identical to their production of γ-cyclodextrin, which was unaffected by the mutations in subsite −7, suggesting that subsite −7 was effectively blocked by these mutations. Further increases in α-cyclodextrin selectivity will require identification of the mechanism or mechanisms by which these small quantities of larger cyclodextrins are formed.

scholarly journals Nucleotide Sequence and X-ray Structure of Cyclodextrin Glycosyltransferase from Bacillus circulans Strain 251 in a Maltose-dependent Crystal Form

1994 ◽  
Vol 236 (2) ◽  
pp. 590-600 ◽  
Author(s):  
Catherine L. Lawson ◽  
Rob van Montfort ◽  
Boris Strokopytov ◽  
Henriëtte J. Rozeboom ◽  
Kor H. Kalk ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Crystal Form ◽  
Bacillus Circulans ◽  
Cyclodextrin Glycosyltransferase ◽  
X Ray
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