Cyclodextrin Degrading Enzymes

Saha, Badal C.; Zeikus, J. G.

doi:10.1002/star.19920440809

Cited by 19 publications

(8 citation statements)

References 28 publications

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“…Properties of some common glucoamylases, are represented in Table 1. In the review of cyclodextrin degrading enzymes (Saha and Zeikus 1992), some glucoamylases with the ability to hydrolyse cyclodextrin have been identified. In particular, glucoamylase produced by Flavobacterium sp.…”

Section: Properties Of Glucoamylasementioning

confidence: 99%

Glucoamylases: Microbial Sources, Industrial Applications and Molecular Biology ? A Review

James

Lee

1997

J Food Biochemistry

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Glucoamylase (EC 3.2.1.3) hydrolyzes polysaccharides from the nonreducing chain ends by cleaving α‐1,4 and α‐1,6 glycosidic bonds consecutively. Glucoamylases are used mainly in the production glucose syrup, high fructose corn syrup, and in whole grain and starch hydrolysis for alcohol production. This paper reviews the status of glucoamylases with respect to microbial sources, biochemical and physical properties. Methods used to assay glucoamylase activity are also compared, with reference being made to the specificity of spectrophotometric methods in detecting end products of the enzyme action. Commercial glucoamylases and development of immobilization techniques are discussed. Also, structural analysis of glucoamylase and the main amino acids involved in catalysis and starch binding are emphasized. The cloning of the glucoamylase gene in Saccharomyces cerevisiae for the brewing of low calorie beer is presented. This review highlights the use of glucoamylase in the food industry.

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Section: Properties Of Glucoamylasementioning

confidence: 99%

Glucoamylases: Microbial Sources, Industrial Applications and Molecular Biology ? A Review

James

Lee

1997

J Food Biochemistry

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“…Several CD-degrading enzymes have been isolated [3][4][5][6][7][8]. They are from various bacterial sources and generally prefer CDs but also accept other maltodextrins, converting them to a broad spectrum of products.…”

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confidence: 99%

Covalent and three‐dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92

Fritzsche

Schwede

Schulz

2003

European Journal of Biochemistry

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Starting with oligopeptide sequences and using PCR, the gene of the cyclodextrinase from Flavobacterium sp. no. 92 was derived from the genomic DNA. The gene was sequenced and expressed in Escherichia coli; the gene product was purified and crystallized. An X‐ray diffraction analysis using seleno‐methionines with multiwavelength anomalous diffraction techniques yielded the refined 3D structure at 2.1 Å resolution. The enzyme hydrolyzes α(1,4)‐glycosidic bonds of cyclodextrins and linear malto‐oligosaccharides. It belongs to the glycosylhydrolase family no. 13 and has a chain fold similar to that of α‐amylases, cyclodextrin glycosyltransferases, and other cyclodextrinases. In contrast with most family members but in agreement with other cyclodextrinases, the enzyme contains an additional characteristic N‐terminal domain of about 100 residues. This domain participates in the formation of a putative D2‐symmetric tetramer but not in cyclodextrin binding at the active center as observed with the other cyclodextrinases. Moreover, the domain is located at a position quite different from that of the other cyclodextrinases. Whether oligomerization facilitates the cyclodextrin deformation required for hydrolysis is discussed.

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“…This strain was equally unable to grow on starch or any of the three natural CDs as the sole carbon and energy source. Furthermore, since some microorganisms have recently been reported to secrete cyclodextrinases (24), our strain was tested and found to be unable to break open any natural CD. Furthermore, the presence of 5 or 15 mM ␤-CD was shown to have no effect on either the growth profile or respiration rate of P. putida in a minimal salt medium containing 2 g of glucose per liter.…”

Section: Resultsmentioning

confidence: 99%

Cyclodextrin-enhanced degradation of toluene and p-toluic acid by Pseudomonas putida

Schwartz

Bar

1995

Appl Environ Microbiol

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Degradation of an immiscible aromatic solvent, toluene, and a water-soluble aromatic compound, p-toluic acid, by a Pseudomonas putida strain in the presence of ␤-cyclodextrin (␤-CD) was investigated. The ability of CDs to interact with hydrophobic organics and form inclusion compounds was exploited in this study to remove or alleviate the toxicities of substrates and consequently to enable or enhance degradation. Liquid toluene was found to be highly toxic to P. putida. However, this phase toxicity was removed when crystalline ␤-CDcomplexed toluene was provided as the substrate. The latter was fully degraded at a concentration of up to 10 g/liter. Degradation of toluene vapors was enhanced in the presence of ␤-CD as a result of reduced molecular toxicity and facilitated absorption of the gaseous substrate. Similarly, ␤-CD alleviated the inhibitory effect of p-toluic acid on P. putida. This protective effect of CD was remarkably more prominent when the microbial culture was shock loaded with an otherwise toxic dose of p-toluic acid (1.8 g/liter).

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Cyclodextrin Degrading Enzymes

Abstract: Cyclodextrinase is an enzyme that hydrolyzes cyclodextrins. Some amylolytic enzymes can also hydrolyze cyclodextrins. A comprehensive review of these cyclodextrin degrading enzymes and their action pattern is presented.

Cited by 19 publications

References 28 publications

Glucoamylases: Microbial Sources, Industrial Applications and Molecular Biology ? A Review

Glucoamylases: Microbial Sources, Industrial Applications and Molecular Biology ? A Review

Covalent and three‐dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92

Cyclodextrin-enhanced degradation of toluene and p-toluic acid by Pseudomonas putida

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