Recombinant Bacterial Amylopullulanases: Developments and Perspectives

Overview

Journal Bioengineered

Date 2013 May 7

PMID 23645215

Citations 11

Authors

M Nisha

T Satyanarayana

Affiliations

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Abstract

Pullulanases are endo-acting enzymes capable of hydrolyzing α-1, 6-glycosidic linkages in starch, pullulan, amylopectin, and related oligosaccharides, while amylopullulanases are bifunctional enzymes with an active site capable of cleaving both α-1, 4 and α-1, 6 linkages in starch, amylose and other oligosaccharides, and α-1, 6 linkages in pullulan. The amylopullulanases are classified in GH13 and GH57 family enzymes based on the architecture of catalytic domain and number of conserved sequences. The enzymes with two active sites, one for the hydrolysis of α-1, 4- glycosidic bond and the other for α-1, 6-glycosidic bond, are called α-amylase-pullulanases, while amylopullulanases have only one active site for cleaving both α-1, 4- and α-1, 6-glycosidic bonds. The amylopullulanases produced by bacteria find applications in the starch and baking industries as a catalyst for one step starch liquefaction-saccharification for making various sugar syrups, as antistaling agent in bread and as a detergent additive.

Citing Articles

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References

Lin F, Leu K . Cloning, expression, and characterization of thermostable region of amylopullulanase gene from Thermoanaerobacter ethanolicus 39E. Appl Biochem Biotechnol. 2002; 97(1):33-44. DOI: 10.1385/abab:97:1:33. View

Nisha M, Satyanarayana T . Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification. Appl Microbiol Biotechnol. 2012; 97(14):6279-92. DOI: 10.1007/s00253-012-4538-6. View

Dong G, Vieille C, Zeikus J . Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl Environ Microbiol. 1997; 63(9):3577-84. PMC: 168663. DOI: 10.1128/aem.63.9.3577-3584.1997. View

Kim J, Sunako M, Ono H, Murooka Y, Fukusaki E, Yamashita M . Characterization of gene encoding amylopullulanase from plant-originated lactic acid bacterium, Lactobacillus plantarum L137. J Biosci Bioeng. 2008; 106(5):449-59. DOI: 10.1263/jbb.106.449. View

Suzuki K, Taiyoji M, Sugawara N, Nikaidou N, Henrissat B, Watanabe T . The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases. Biochem J. 1999; 343 Pt 3:587-96. PMC: 1220590. View

Brown S, Kelly R . Characterization of Amylolytic Enzymes, Having Both alpha-1,4 and alpha-1,6 Hydrolytic Activity, from the Thermophilic Archaea Pyrococcus furiosus and Thermococcus litoralis. Appl Environ Microbiol. 1993; 59(8):2614-21. PMC: 182328. DOI: 10.1128/aem.59.8.2614-2621.1993. View

Kuriki T, Imanaka T . The concept of the alpha-amylase family: structural similarity and common catalytic mechanism. J Biosci Bioeng. 2005; 87(5):557-65. DOI: 10.1016/s1389-1723(99)80114-5. View

Kim J, Sunako M, Ono H, Murooka Y, Fukusaki E, Yamashita M . Characterization of the C-terminal truncated form of amylopullulanase from Lactobacillus plantarum L137. J Biosci Bioeng. 2009; 107(2):124-9. DOI: 10.1016/j.jbiosc.2008.10.019. View

Melasniemi H . Purification and some properties of the extracellular alpha-amylase-pullulanase produced by Clostridium thermohydrosulfuricum. Biochem J. 1988; 250(3):813-8. PMC: 1148928. DOI: 10.1042/bj2500813. View

10.

Henrissat B, Gaboriaud C, Bissery V, Morgat A, Mornon J . Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences. Biochimie. 1990; 72(8):555-74. DOI: 10.1016/0300-9084(90)90120-6. View

11.

MacGregor E, Janecek S, Svensson B . Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. Biochim Biophys Acta. 2001; 1546(1):1-20. DOI: 10.1016/s0167-4838(00)00302-2. View

12.

Watanabe T, Ito Y, Yamada T, Hashimoto M, Sekine S, Tanaka H . The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J Bacteriol. 1994; 176(15):4465-72. PMC: 196264. DOI: 10.1128/jb.176.15.4465-4472.1994. View

13.

Ells L, Seal C, Kettlitz B, Bal W, Mathers J . Postprandial glycaemic, lipaemic and haemostatic responses to ingestion of rapidly and slowly digested starches in healthy young women. Br J Nutr. 2005; 94(6):948-55. DOI: 10.1079/bjn20051554. View

14.

Hatada Y, Igarashi K, Ozaki K, Ara K, Hitomi J, Kobayashi T . Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes alpha-1,4 and alpha-1,6 linkages in polysaccharides at different active sites. J Biol Chem. 1996; 271(39):24075-83. DOI: 10.1074/jbc.271.39.24075. View

15.

Janecek S, Svensson B, MacGregor E . Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals. Enzyme Microb Technol. 2011; 49(5):429-40. DOI: 10.1016/j.enzmictec.2011.07.002. View

16.

Lee S, Morikawa M, Takagi M, Imanaka T . Cloning of the aapT gene and characterization of its product, alpha-amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601. Appl Environ Microbiol. 1994; 60(10):3764-73. PMC: 201885. DOI: 10.1128/aem.60.10.3764-3773.1994. View

17.

Kataeva I, Seidel 3rd R, Shah A, West L, Li X, Ljungdahl L . The fibronectin type 3-like repeat from the Clostridium thermocellum cellobiohydrolase CbhA promotes hydrolysis of cellulose by modifying its surface. Appl Environ Microbiol. 2002; 68(9):4292-300. PMC: 124122. DOI: 10.1128/AEM.68.9.4292-4300.2002. View

18.

Lin F, Ma H, Lin H, Liu S, Tzou W . Biochemical characterization of two truncated forms of amylopullulanase from Thermoanaerobacterium saccharolyticum NTOU1 to identify its enzymatically active region. Appl Biochem Biotechnol. 2011; 165(3-4):1047-56. DOI: 10.1007/s12010-011-9319-7. View

19.

Jiao Y, Wang S, Lv M . [Structural and functional analysis of GH57 family thermostable amylopullulanase--a review]. Wei Sheng Wu Xue Bao. 2011; 51(1):21-8. View

20.

Chen J, Chen M, Chen L, Chu W . Structure and expression of an amylopullulanase gene from Bacillus stearothermophilus TS-23. Biotechnol Appl Biochem. 2001; 33(3):189-99. DOI: 10.1042/ba20010003. View