Large-scale purification and characterization of barley limit dextrinase, a member of the α-amylase structural family

Cereal Chemistry

Volumn 75, Issue 4, 1998, Pages 473-479

  Kristensen, Michael ^a,b   Planchot, Véronique ^c   Abe, Jun Ichi ^d   Svensson, Birte ^a  

^a CARLSBERG LABORATORY   (Denmark)

^b Danish Pest Infestation Laboratory   (Denmark)

^c CEMAGREF   (France)

^d KAGOSHIMA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; AMMONIUM SULFATE; AMYLASE; ANION EXCHANGE CHROMATOGRAPHY; CHARACTERIZATION; CYCLODEXTRIN SEPHAROSE; FLOUR; GERMINATION; HYDROLYSIS; ISOLATION PROCEDURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYPEPTIDE; PRECIPITATION; PURIFICATION; SEQUENCE ANALYSIS;

AFFINITY CHROMATOGRAPHY; ASCORBIC ACID; CYCLODEXTRINS; NITROGEN COMPOUNDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PURIFICATION; SULFUR COMPOUNDS;

AMMONIUM SULFATE; ANION EXCHANGE CHROMATOGRAPHY; DIETHYLAMINOETHYL; LARGE-SCALES; LIMIT DEXTRINASE; POLYPEPTIDES CHAINS; PURIFICATION PROTOCOL; RP-HPLC; SDS-PAGE; SEQUENCE ANALYSIS;

AMYLASES;

EID: 0031873219     PISSN: 00090352     EISSN: None     Source Type: Journal    
DOI: 10.1094/CCHEM.1998.75.4.473     Document Type: Article

References (66)

1. Amemura, A., Chakraborty, R., Fujita, M., Noumi, T., and Futai, M. 1988. Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amyloderemosa SB-15. J. Bacteriol. 263:9271-9275.
2. Doehlert, D. C., and Knutson, C. A. 1991. Two classes of starch debranching enzymes from developing maize kernels. J. Plant Physiol. 138:566-572.
3. Dunn, G., and Manners, D. J. 1975. The limit dextrinases from ungerminated oats (Avena sativa L.) and ungerminated rice (Oryza sativa L.). Carbohydr. Res. 39:283-293.
4. Gibson, R. M., and Svensson, B. 1987. Identification of tryptophanyl residues involved in binding of carbohydrate ligands to barley α-amylase 2. Carlsberg Res. Commun. 52:373-379.
5. Hardie, D. G. 1975. Control of carbohydrase formation by gibberellic acid in barley endosperms. Phytochem. 14:1719-1722.
6. Hardie, D. G., Manners, D. J., and Yellowlees, D. 1976. The limit dextrinase from malted sorghum (Sorghum vulgare). Carbohydr. Res. 50:75-85.
7. Igarashi, K., Ara, K., Saeki, K., Ozaki, K., Kawai, S., and Ito, S. 1992. Nucleotide sequence of the gene that encodes a neopullulanase from an alkalophilic Bacillus. Biosci. Biotech. Biochem. 56:514-516.
8. Iwamoto, H., Ohmori, M., Ohno, M., Hirose, J., Hiromi, K., Fukada, H., Takahashi, K., Hashimoto, H., and Sakai, S. 1993. Interaction between pullulanase from Klebsiella pneumoniae and cyclodextrins. J. Biochem 113:93-96.
9. James, M. G., Robertson, D. S., and Myers, A. M. 1995. Characterization of the maize sugary1, a determinant of starch composition in kernels. Plant Cell 7:417-429.
10. 8-barrel enzymes: Chance of homology. Prot. Sci. 4:1239-1242.
11. 8-barrel domain and evolutionary relationship to other amylolytic enzymes. J. Prot. Chem. 12:791-805.
12. Jespersen, H. M., MacGregor, E. A., Sierks, M. R., and Svensson, B. 1991. Comparison of the domain level organization of starch hydrolases and related enzymes. Biochem. J. 280:51-55.
13. Johnson, T. C., Wada, K., Buchanan, B. B., and Holmgren, A. 1987. Reduction of purothionin by the wheat seed thioredoxin system. Plant Physiol. 85:446-451.
14. Kainuma, K., Kobayashi T., and Harada, T. 1978. Action of Pseudomonas isoamylase on various branched oligo- and poly-saccharides. Carbohydr. Res. 61:345-357.
15. Katsuragi, N., Takizawa, N., and Murooka, Y. 1987. Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70. J. Bacteriol. 169:2301-2306.
16. Kelly, A. P., Diderichsen, B., Jorgensen, S., and McConnell, A. 1994. Molecular genetic analysis of the pullulanase B gene of Bacillus acidopullulyticus. FEMS Microbiol. Lett. 115:97-106.
17. Kobrehel, K., Wong, J. H., Balog, A., Kiss, F., Yee, B. C., and Buchanan, B. B. 1992. Specific reduction of wheat storage proteins by thioredoxin h. Plant Physiol. 99:919-924.
18. Kristensen, M., Abe, J., Larsen, J., Mundy, J., and Svensson, B. 1995. Barley limit dextrinase during malting and seed development. Pages 18-20 in: Proc. Progress in Plant Polymeric Carbohydrate Research. F. Meuser, D. J. Manners, and W. Siebel, eds. Behr's Verlag GmbH & Co.: Hamburg.
19. Kristensen, M., Svensson, B., and Larsen, J. 1993. Purification and characterization of barley limit dextrinase during malting. Proc. Congr. Eur. Brew. Conv. 24:37-43.
20. Kuriki, T., and Imanaka, T. 1989. Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus. J. Gen. Microbiol. 135:1521-1528.
21. Kuriki, T., Okada, S., and Imanaka, T. 1988. New type of pullulanase from Bacillus stearothermophilus and molecular cloning and expression of the gene in Bacillus subtilis. J. Bacteriol. 170:1554-1559.
22. Kuriki, T., Park, J., and Imanaka, T. 1990. Characteristics of thermostable pullulanase from Bacillus stearothermophilus and the nucleotide sequence of the gene. J. Ferm. Bioeng. 69:204-210.
23. Larson, S. B., Greenwood, A., Cascio, D., Day, J., and McPherson, A. 1994. Refined molecular structure of pig pancreatic α-amylase at 2.1 A resolution. J. Mol. Biol. 235:1560-1584.
24. Lecommandeur, D., MacGregor, A. W., and Daussant, J. 1988. Purification of germinated barley α-amylase and limit dextrinase by chromatofocusing and affinity chromatography. J. Chromatogr. 441:436-442.
25. Lee, W. J., and Pyler, R. E. 1984. Barley limit dextrinase: Varietal, environmental and malting effects. J. Am. Soc. Brew. 42:11-17.
26. Lenoir, P., MacGregor, A. W., Moll, M., and Daussant, J. 1984. Identification of debranching enzyme from barley and malt by isoelectric focusing. CR Acad. Sci. Paris 298:243-248.
27. Li, B., Servaites, C., and Geiger, D. R. 1992. Characterization and subcellular localization of debranching enzyme and endoamylase from leaves of sugar beet. Plant Physiol. 98:1277-284.
28. Longstaff, M. A., and Bryce, J. H. 1991. Levels of limit dextrinase activity in malting barley. Proc. Congr. Eur. Brew. Conv. 23:593-600.
29. Longstaff, M. A., and Bryce, J. H. 1993. Development of limit dextrinase in germinated barley (Hordeum vulgare L.). Plant Physiol. 101:881-889.
30. Ludwig, I., Ziegler, P., and Beck, E. 1984. Purification and properties of spinach leaf debranching enzyme. Plant Physiol. 74:856-861.
31. MacGregor, A. W. 1987. α-Amylase, limit dextrinase, and α-glucosidase enzymes in barley and malt. CRC Crit. Rev. Biotech. 5:117-128.
32. MacGregor, A. W., Macri, L. J., Schroeder, S. W., and Bazin, S. L. 1994. Limit dextrinase from malted barley: Extraction, purification, and characterization. Cereal Chem. 71:610-617.
33. Macri, L. J., MacGregor, A. W., Schroeder, S. W., and Bazin, S. L. 1993. Detection of a limit dextrinase inhibitor in barley. J. Cereal Sci. 18:103-106.
34. Maeda, I., Jimi, N., Taniguchi, H., and Nakamura, M. 1979. Purification of R-enzyme from malted barley and its role in in vivo digestion of barley starch granules. J. Jap. Soc. Starch Sci. 26:117-127.
35. Maeda, I., Nikuni, Z., Taniguchi, H., and Nakamura, M. 1978. Purification of a debranching enzyme (R-enzyme) from malted barley, and the role of the enzyme in the digestion of starch granules during the germination of barley seeds. Carbohydr. Res. 61:309-320.
36. Manners, D. J., and Yellowlees, D. 1973. Studies on debranching enzymes. I. The limit dextrinase activity of extracts of certain higher plants and commercial malts. J. Inst. Brew. 79:77-385.
37. Matsuura, Y., Kusunoki, M., Harada, W., and Kakudo, M. 1984. Structure and possible catalytic residues of Taka-amylase A. J. Biochem. 95:697-702.
38. McCleary, B. 1992. Measurement of the content of limit-dextrinase in cereal flours. Carbohydr. Res. 227:257-268.
39. Melasniemi, H. 1988. Purification and some properties of the extracellular α-amylase-pullulanase produced by Clostridium thermohydrosulfuricum. Biochem. J. 250:813-818.
40. Melasniemi, H., Paloheimo, M., and Heimo, L. 1990 Nucleotide sequence of the α-amylase-pullulanase gene from Clostridium thermohydrosulfuricum. J. Gen. Microbiol. 136:447-454.
41. Mikami, B., Hehre, E. J., Sato, M., Katsube, Y., Hirose, M., Morita, Y., and Sacchettini, J. C. 1993. The 2.0-Å resolution structure of soybean β-amylase complexed with α-cyclodextrin. Biochem. 32:6836-6845.
42. Mundy, J. 1982. Isolation and characterization of two immunologically distinct forms of α-amylase and a β-amylase from seeds of germinated Sorghum bicolar (L.). Carlsberg Res. Commun. 47:263-274.
43. Nakamura, Y., Umemoto, T., Ogata, N., Kuboki, Y., Yano, M., and Sasaki, T. 1996. Starch debranching enzyme (R-enzyme or pullulanase) from developing rice endosperm: purification, cDNA and chromosomal localization of the gene. Planta 199:209-218.
44. Saha, B. C., Mathupala, S. P., and Zeikus, J. G. 1988. Purification and characterization of a highly thermostable novel pullulanase from Clostridium thermohydrosulfuricum. Biochem. J. 252: 343-348.
45. Sakano, Y., Hiraiwa, S., Fukushima, J., and Kobayashi, T. 1982. Enzymatic properties and action patterns of Thermoactinomyces vulgaris α-amylase. Agric. Biol. Chem. 46:1121-1129.
46. Sakano, Y., Masuda, N., and Kobayashi, T. 1971. Hydrolysis of pullulan by a novel enzyme from Aspergillus niger. Agric. Biol. Chem. 35:971-73.
47. Sashihara, N., Nakamura, N., and Horikoshi, K. 1993. Subcloning and nucleotide sequencing of the pul gene of Thermus sp. AMD-33. Starch/Staerke 45:144-150.
48. Schuler, G. D., Altshul, S. F., and Lipman, D. J. 1991. Workbench for multiple alignment construction and analysis. Proteins Struct. Funct. Genet. 9:180-190.
49. Serre, L., and Lauriere, C. 1990. Specific assay of α-dextrin 6-glucanohydrolase using labeled pullulan. Anal. Biochem. 186:312-315.
50. Silvanovich, M. P., and Hill, R. D. 1976. Affinity chromatography of cereal α-amylase. Anal. Biochem. 71:430-433.
51. Sissons, M. J., Lance, R. C. M., and Sparrow, D. H. B. 1992a. Studies on limit dextrinase in barley. 1. Purification of malt limit dextrinase and production of monospecific antibodies. J. Cereal Sci. 16:107-116.
52. Sissons, M. J., Lance, R. C. M., and Sparrow, D. H. B. 1992b. Studies on limit dextrinase in barley. 2. Application of an ELISA and immunoblotting to studies of genetic variability and malting effects. J. Cereal Sci. 16:117-128.
53. Sissons, M. J., Lance, R. C. M., and Sparrow, D. H. B. 1993. Studies on limit dextrinase in barley. 3. Limit dextrinase in developing kernels. J. Cereal Sci. 17:19-24.
54. Svensson, B. 1994. Protein engineering in the α-amylase family: Catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol. 25:41-157.
55. Svensson, B., and Søgaard, M. 1993. Mutational analysis of glycosylase function. J. Biotechnol. 29:1-37.
56. Svensson, B., Jespersen, H. M., Sierks, M. R., and MacGregor, E. A. 1989. Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes. Biochem. J. 264:309-311.
57. Svensson, B., Larsen, K., and Svendsen, I. 1983. Amino acid sequence of tryptic fragments of glucoamylase G1 from Aspergillus niger. Carlsberg Res. Commun. 48:517-527
58. Søgaard, M., Kadziola, A., Haser, R., and Svensson, B. 1993. Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley α-amylase 1. J. Biol. Chem. 268:22480-22484.
59. Tonozuka, T., Ohtsuka, M., Mogi, S., Sakai, H., Ohta, T., and Sakano, Y. 1993. A neopullulanase-type α-amylase gene from Thermoactinomyces vulgaris R-47. Biosci. Biotech. Biochem. 57:395-401.
60. Tonuzaka, T., Mogi, S., Shimura, Y. Ibuka, A., Sakai, H., Matsuzawa, H., Sakano, Y., and Ohta, T. 1995. Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47. Biochim. Biophys. Acta 1252:35-42.
61. Totsuka, A., and Fukazawa, C. 1993. Affinity purification of β-amylase originating from plant using cyclomaltohexaose-immobilized Sepharose 6B in the presence of ammonium sulfate. Prot. Exp. Purif. 4:333-336.
62. 2+ on the activation of amylopectin-1,6-glucosidase activity in pea seedlings. Physiol. Plant. 25:363-368.
63. Warner, D. A., Grove, M. J., and Knutson, C. A. 1991. Isolation and characterization of α-amylases from endosperm of germinating maize. Cereal Chem. 68:383-390.
64. Wrobel, R., and Jones, B. L. 1992. Appearance of endoproteolytic enzymes during the germination of barley. Plant Physiol. 100:1508-1516.
65. Yamada, J. 1981. Conversion of active and inactive debranching enzymes in rice seeds. Agric. Biol. Chem. 45:747-750.
66. Yellowlees, D. 1980. Purification and characterization of limit dextrinase from Pisum sativum. Carbohydr. Res. 83:109-118.