An Improved Method for the Preparation of Schardinger β‐Dextrin on a Industrial Scale by Cyclodextrin Glycosyl Transferase of an Alkalophilic <i>Bacillus Sp.</i> (ATCC 21783)

Matzuzawa, M.; Kawano, Miki; Nakamura, Nobuyuki; Horikoshi, Koki

doi:10.1002/star.19750271204

Cited by 42 publications

(9 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Owing to the high conversion rate, CDs could be directly crystallized from the hydrolyzate of starch without the addition of organic solvents. 41) These simple methods developed reduced the cost of β-CD from 199,000 yen to 1,000 yen/kg, and that of α-CD to within 3,000 yen/kg. This has paved the way for its use in large quantities in foodstuffs, chemicals, and pharmaceuticals.…”

Section: )mentioning

confidence: 99%

Alkaliphiles

Horikoshi

2004

Proc. Jpn. Acad., Ser. B

View full text Add to dashboard Cite

Abstract:The term alkaliphile is used for microorganisms that grow optimally or very well at pH values above 9, but cannot grow or grow only slowly at the near neutral pH value of 6.5. Alkaliphiles include prokaryotes, eukaryotes, and archaea. Alkaliphiles can be isolated from normal environments such as garden soil, although viable counts of alkaliphiles are higher in samples from alkaline environments. The cell surface plays a key role in keeping the intracellular pH value in the range between 7 and 8.5, allowing alkaliphiles to thrive in alkaline environments. Alkaliphiles have made a great impact in industrial applications. Biological detergents contain alkaline enzymes, such as alkaline cellulases and/or alkaline proteases that have been produced from alkaliphiles. Another important application is the industrial production of cyclodextrin with alkaline cyclomaltodextrin glucanotransferase. This enzyme reduced the production cost and paved the way for cyclodextrin use in large quantities in foodstuffs, chemicals and pharmaceuticals. It has also been reported that alkali-treated wood pulp could be biologically bleached by xylanases produced by alkaliphiles.

show abstract

Section: )mentioning

confidence: 99%

Alkaliphiles

Horikoshi

2004

Proc. Jpn. Acad., Ser. B

View full text Add to dashboard Cite

show abstract

“…strain 38-2 by Matsuzawa and coworkers [165], there have been many other similar reports [18,68,164,247,275] documenting the production of more thermostable CGTases at pH optima ranging from 5.0 to 10.0. Industrial production of cyclodextrins has benefited from the biocatalytic process since a-, b-, and c-CD could be produced on a large scale with a high conversion rate of substrates such as amylase and potato starch and without use of organic solvents to precipitate the CDs.…”

Section: Amylasementioning

confidence: 92%

Alkaliphilic bacteria: applications in industrial biotechnology

Sarethy

Saxena

Kapoor

et al. 2011

J Ind Microbiol Biotechnol

126

View full text Add to dashboard Cite

Alkaliphiles are interesting groups of extremophilic organisms that thrive at pH of 9.0 and above. Many of their products, in particular enzymes, have found widespread applications in industry, primarily in the detergent and laundry industries. While the enzymes have been a runaway success from the industrial point of view, many more products have been reported from alkaliphiles such as antibiotics and carotenoids. Less known are their potential for degradation of xenobiotics. They also play a key role in biogeocycling of important inorganic compounds. This review provides an insight into the huge diversity of alkaliphilic bacteria, the varied products obtained from them, and the need for further investigations on these interesting bacteria.

show abstract

“…2-4, 23, 29 Other genus of which CGTases have been purified were Klebsiella, Thermoanaerobacter and Brevibacterium. 10,[30][31] All strains were found to excrete their CGTases in the extracellular medium.…”

Section: Immunoaffinity Purification Of Cgtasementioning

confidence: 99%

“…Different ratios of CD products were reported for CGTases from other bacteria, ie 2.7 : 1.0 : 1.0 for α-CGTase of B. macerans, 2 and 1.0 : 11.0 : 1.5 for β-CGTase of alkalophilic Bacillus sp. 38-2, 10 while the CGTase of B. fermus/lentus 290-3 was known to produce γ-CGTase in the initial phase of enzyme production. 32 The enzyme source is hence one important parameter in specifying the product ratio.…”

Section: 1238-39mentioning

confidence: 99%

“…9 Several reports on CGTase purification were found to be involved the precipitation with organic solvents or ammonium sulphate, the adsorption on starch, chromatography on DEAE-cellulose, and electrophoresis. [3][4]10 Very efficient purification of CGTase from Bacillus macerans was achieved on α-CD-derivatized agarose. 11 Affinity chromatography on a β-CD polymer of CGTases from different strains of Bacillus sp.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Untitled

Rojtinnakorn¹,

Kim²,

Laloknam³

et al. 2001

ScienceAsia

View full text Add to dashboard Cite

The purified IgG fraction of anti-CGTase was coupled to CNBr-activated Sepharose 4B and used as immunoaffinity gel to purify CGTase from Bacillus circulans A11. The enzyme was successfully purified to approximately 155 folds with a 45% yield and specific activity of 3302 units/mg protein. It was a single polypeptide of 72 KDa. The amino acid composition of this CGTase was found to contain high amounts of Asx, Glx, Gly, Ala, and Thr and low amounts of His, Met, Cys, and Trp. N-Terminal sequence was A P D T S V S N K Q N F S T D V I Y Q I. Chemical modification and substrate protection studies indicate the presence of Trp, His, Tyr, and Asx/Glx residues at the active site of CGTase, while Cys, Lys, and Ser were proved to have no influence on CGTase catalysis. From HPLC analysis of products of enzymatic reaction, this CGTase produced mainly β-CD. The ratio of α : β : γ -CD was 1 : 4.1 : 1.1. When analyzed by non-denaturing PAGE, the enzyme demonstrates the isoform pattern. Four isoforms with the same molecular mass but different in quantity and pI values were observed. All isoforms demonstrate amylolytic and cyclizing activities of CGTase.

show abstract

An Improved Method for the Preparation of Schardinger β‐Dextrin on a Industrial Scale by Cyclodextrin Glycosyl Transferase of an Alkalophilic Bacillus Sp. (ATCC 21783)

Cited by 42 publications

References 10 publications

Alkaliphiles

Alkaliphiles

Alkaliphilic bacteria: applications in industrial biotechnology

Untitled

Contact Info

Product

Resources

About