Gene cloning, nucleotide sequence and biochemical properties of a cytoplasmic cyclomaltodextrinase (neopullulanase) from<i>Alicyclobacillus acidocaldarius</i>, reclassification of a group of enzymes

Matzke, Jutta; Herrmann, Anja; Schneider, Erwin; Bakker, Evert P.

doi:10.1111/j.1574-6968.2000.tb08933.x

Cited by 50 publications

(16 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…According to literature, the amylase enzymes produced by microorganisms have optimum temperature ranges that vary from 45 to 115 ºC. 6,30 The results found in the present study were similar to those from studies by Bai et al, 26 and Matzke et al, 5 in the production of amylase by A. acidocaldarius.…”

Section: Determination Of Optimum Ph and Temperature Of Amylasesupporting

confidence: 82%

“…29 With respect to species of Alicyclobacillus, the optimum pH range obtained in the present study was in accordance with the range reported in literature. The amylase enzyme produced by A. acidocaldarius ATCC 27009 had an optimum pH of 3.0, in a study by Matzke et al 5 In studies by Kumar et al, 25 of the production of amylase produced by A. acidocaldarius MTCC 8766, the optimum pH was 6.0. An acidic α-amylase produced by Alicyclobacillus sp.…”

Section: Determination Of Optimum Ph and Temperature Of Amylasementioning

confidence: 99%

“…1 Enzymes produced by such microorganisms have been studied for use in various industrial applications, including galactosidase, esterases, proteases and amylases, due to their thermostable characteristics. [2][3][4][5] The Alicyclobacillus acidocaldarius and Alicyclobacillus sendaiensis species have been evaluated for the production of both amylase and collagenase, respectively.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Biosynthesis of industrial enzymes by free and immobilized Alicyclobacillus in different matrices and the use of ultrafiltration in the enzymes concentration

et al. 2017

View full text Add to dashboard Cite

The biosynthesis of amylase and collagenase, produced by A. acidocaldarius and A. sendaiensis respectively, were studied, and different matrices evaluated for the microorganisms immobilization and enzymes production optimization, such as loofa sponge, alginate-sponge and alginate, followed by concentration through ultrafiltration. Using a wheat bran substrate, the amylase enzyme displayed enzymatic activity of 0.45 U mL -1 and optimum temperature and pH conditions of 75 °C and pH 3.0, respectively. Thermal stability was in the range of 55 to 60 °C. The apparent Km and Vmax were 3.2 mg mL -1 and 0.5 U mL -1, respectively. The production of collagenase by A. sendaiensis was carried out with potato dextrose broth substrate and the activity obtained was 7.2 U mL -1 . For amylase, the best results were obtained from immobilization in loofa sponge and the use of ultrafiltration (0.67 U mL -1) and for the collagenase extract, from the free biomass and ultrafiltration (13.6 U mL -1 ). The use of an ultrafiltration system enabled an average increase of 54% in the activity of both enzymes. Therefore, Alicyclobacillus are capable of producing enzymes of industrial interest, with the possibility of economically viable application of the substrate, and the use of immobilization and ultrafiltration produced positive results.

show abstract

Section: Determination Of Optimum Ph and Temperature Of Amylasesupporting

confidence: 82%

Section: Determination Of Optimum Ph and Temperature Of Amylasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Biosynthesis of industrial enzymes by free and immobilized Alicyclobacillus in different matrices and the use of ultrafiltration in the enzymes concentration

et al. 2017

View full text Add to dashboard Cite

show abstract

“…docaldarius (29,56). We note that the intracellular location of AaManA and its preference for longer substrates requires a special manno-oligosaccharide uptake system, because such substrates are too large to passively cross the membrane.…”

Section: Resultsmentioning

confidence: 99%

Biochemical and Structural Characterization of the Intracellular Mannanase AaManA of Alicyclobacillus acidocaldarius Reveals a Novel Glycoside Hydrolase Family Belonging to Clan GH-A

Zhang

Peng

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

An intracellular mannanase was identified from the thermoacidophile Alicyclobacillus acidocaldarius Tc-12-31. This enzyme is particularly interesting, because it shows no significant sequence similarity to any known glycoside hydrolase. Gene cloning, biochemical characterization, and structural studies of this novel mannanase are reported in this paper. The gene consists of 963 bp and encodes a 320-amino acid protein, AaManA. Based on its substrate specificity and product profile, AaManA is classified as an endo-␤-1,4-mannanase that is capable of transglycosylation. Kinetic analysis studies revealed that the enzyme required at least five subsites for efficient hydrolysis. The crystal structure at 1.9 Å resolution showed that AaManA adopted a (␤/␣) 8 -barrel fold. Two catalytic residues were identified: Glu 151 at the C terminus of ␤-stand ␤4 and Glu 231 at the C terminus of ␤7. Based on the structure of the enzyme and evidence of its transglycosylation activity, AaManA is placed in clan GH-A. Superpositioning of its structure with that of other clan GH-A enzymes revealed that six of the eight GH-A key residues were functionally conserved in AaManA, with the exceptions being residues Thr 95 and Cys 150 . We propose a model of substrate binding in AaManA in which Glu 282 interacts with the axial OH-C(2) in ؊2 subsites. Based on sequence comparisons, the enzyme was assigned to a new glycoside hydrolase family (GH113) that belongs to clan GH-A.Mannans are polysaccharides found in plants and consist of a backbone of ␤-1,4-linked mannose and glucose units. Mannose residues often carry an ␣-galactosyl substitute at O-6, and the degree of substitution depends on the plant of origin (Fig. 1A) (1). Mannans are widely distributed in nature in parts of the hemicellulose fraction in hardwoods and softwoods (1), legume seeds (2), and beans of carob trees (3).Endo-␤-1,4-mannanases (mannanases; EC 3.2.1.78) are glycoside hydrolases that randomly cleave the ␤-1,4-linkage in mannans (Fig. 1, A and B) (4); these enzymes have been isolated from bacteria, fungi, plants, and some mollusks (5-8). Interest in these enzymes has been increasing due to their importance in hemicellulose hydrolysis and various other applications (5, 9, 10). During the last 2 decades, more than 80 sequences of the catalytic domains of mannanase have been reported (see the CAZy site on the World Wide Web) and classified into glycoside hydrolase (GH) 2 families 5 and 26, based on their sequence similarities (11). In recent years, crystallographic resolution of the structures of these enzymes has yielded information on their structure. At present, the tertiary structures of seven mannanases have been determined, of which five are from GH family 5 (12-16) and two are from family 26 (17, 18). All of these mannanases share a common (␤/␣) 8 barrel fold, a retaining reaction mechanism (Fig. 1C), and two conserved catalytic residues (two glutamate residues at the C termini of ␤4 and ␤7, respectively). Therefore, all of these enzymes have been assigned to the same GH ...

show abstract

“…Pullulan hydrolase type I (neopullulanase) and type II (isopullulanase) are only able to cleave α -1,4 glucosidic linkages in pullulan, releasing panose and isopanose, and are highly active on cyclodextrins [32–34]. The enzymes that degrade cyclodextrins faster than starch are sometimes designated cyclodextrinases (EC 3.2.1.54, cyclomaltodextrinase) [3, 34]. Interestingly, cyclomaltodextrinases are intracellular enzymes whereas most enzymes involved in starch conversion are extracellular [35].…”

Section: Starch-debranching Enzymesmentioning

confidence: 99%

Pullulanase: Role in Starch Hydrolysis and Potential Industrial Applications

et al. 2012

View full text Add to dashboard Cite

The use of pullulanase (EC 3.2.1.41) has recently been the subject of increased applications in starch-based industries especially those aimed for glucose production. Pullulanase, an important debranching enzyme, has been widely utilised to hydrolyse the α-1,6 glucosidic linkages in starch, amylopectin, pullulan, and related oligosaccharides, which enables a complete and efficient conversion of the branched polysaccharides into small fermentable sugars during saccharification process. The industrial manufacturing of glucose involves two successive enzymatic steps: liquefaction, carried out after gelatinisation by the action of α-amylase; saccharification, which results in further transformation of maltodextrins into glucose. During saccharification process, pullulanase has been used to increase the final glucose concentration with reduced amount of glucoamylase. Therefore, the reversion reaction that involves resynthesis of saccharides from glucose molecules is prevented. To date, five groups of pullulanase enzymes have been reported, that is, (i) pullulanase type I, (ii) amylopullulanase, (iii) neopullulanase, (iv) isopullulanase, and (v) pullulan hydrolase type III. The current paper extensively reviews each category of pullulanase, properties of pullulanase, merits of applying pullulanase during starch bioprocessing, current genetic engineering works related to pullulanase genes, and possible industrial applications of pullulanase.

show abstract

Gene cloning, nucleotide sequence and biochemical properties of a cytoplasmic cyclomaltodextrinase (neopullulanase) fromAlicyclobacillus acidocaldarius, reclassification of a group of enzymes

Cited by 50 publications

References 28 publications

Biosynthesis of industrial enzymes by free and immobilized Alicyclobacillus in different matrices and the use of ultrafiltration in the enzymes concentration

Biosynthesis of industrial enzymes by free and immobilized Alicyclobacillus in different matrices and the use of ultrafiltration in the enzymes concentration

Biochemical and Structural Characterization of the Intracellular Mannanase AaManA of Alicyclobacillus acidocaldarius Reveals a Novel Glycoside Hydrolase Family Belonging to Clan GH-A

Pullulanase: Role in Starch Hydrolysis and Potential Industrial Applications

Contact Info

Product

Resources

About