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Journal articles on the topic 'Limit dextrinase and limit dextrinase inhibitor'

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Author: Grafiati

Published: 10 December 2022

Last updated: 29 January 2023

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1

Peng, Ya Li, and Fei Hu. "Purification and Characterization of Limit Dextrinase from Malted Barley." Advanced Materials Research 550-553 (July 2012): 1747–54. http://dx.doi.org/10.4028/www.scientific.net/amr.550-553.1747.

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Limit dextrinase is one of three main amylases in malted barley, which plays a significant role during the mashing stage of brewing. Due to very low content and similar properties compared to other amylases in malted barley, limit dextrinase is hard to separate effectively. Our work had been directed towards the extraction and purification of limit dextrinase from malted barley. Final products were obtained through fraction precipitation with ammonium sulfate and column chromatography, and purified limit dextrinase acquired a high purity of 31.23 times as much as that of crude extracts. The previous results were also confirmed by sodiumdodecyl sulphate poly-acrylamide gel electrophoresis (SDS-PAGE) revealing a single band of protein (~97KDa). Effect of temperature, pH value, and metal ion on hydrolysis characterization of limit dextrinase was investigated. The results indicated that the maximum activity of purified samples changed significantly compared with that of crude extracts. The activity of purified limit dextrinase could be activated by lower concentration of Mg2+、Ca2+、Mn2+ and inhibited by the action of Zn2+、Fe2+. But this influence was not so obvious for K+.

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2

Macri, L. J., A. W. MacGregor, S. W. Schroeder, and S. L. Bazin. "Detection of a Limit Dextrinase Inhibitor in Barley." Journal of Cereal Science 18, no. 2 (September 1993): 103–6. http://dx.doi.org/10.1006/jcrs.1993.1038.

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3

Huang, Yuqing, Shengguan Cai, and Guoping Zhang. "The relationship of limit dextrinase, limit dextrinase inhibitor and malt quality parameters in barley and their genetic analysis." Journal of Cereal Science 70 (July 2016): 140–45. http://dx.doi.org/10.1016/j.jcs.2016.05.027.

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4

Møller, Marie S., Malene B. Vester-Christensen, Johanne M. Jensen, Maher Abou Hachem, Anette Henriksen, and Birte Svensson. "Crystal Structure of Barley Limit Dextrinase-Limit Dextrinase Inhibitor (LD-LDI) Complex Reveals Insights into Mechanism and Diversity of Cereal Type Inhibitors." Journal of Biological Chemistry 290, no. 20 (March 19, 2015): 12614–29. http://dx.doi.org/10.1074/jbc.m115.642777.

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5

MacGregor, E. Ann. "The proteinaceous inhibitor of limit dextrinase in barley and malt." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1696, no. 2 (February 2004): 165–70. http://dx.doi.org/10.1016/j.bbapap.2003.09.018.

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6

MacGregor, E. A., S. L. Bazin, E. W. Ens, J. Lahnstein, L. J. Macri, N. J. Shirley, and A. W. MacGregor. "Structural Models of Limit Dextrinase Inhibitors from Barley." Journal of Cereal Science 31, no. 1 (January 2000): 79–90. http://dx.doi.org/10.1006/jcrs.1999.0284.

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7

MacGregor, A. W., S. L. Bazin, and S. W. Schroeder. "Effect of Starch Hydrolysis Products on the Determination of Limit Dextrinase and Limit Dextrinase Inhibitors in Barley and Malt." Journal of Cereal Science 35, no. 1 (January 2002): 17–28. http://dx.doi.org/10.1006/jcrs.2001.0408.

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8

Jensen, Johanne Mørch, Per Hägglund, Hans Erik Mølager Christensen, and Birte Svensson. "Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction." FEBS Letters 586, no. 16 (June 19, 2012): 2479–82. http://dx.doi.org/10.1016/j.febslet.2012.06.009.

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9

MacGregor, A. W., L. J. Macri, S. W. Schroeder, and S. L. Bazin. "Purification and Characterisation of Limit Dextrinase Inhibitors from Barley." Journal of Cereal Science 20, no. 1 (July 1994): 33–41. http://dx.doi.org/10.1006/jcrs.1994.1042.

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10

Huang, Yuqing, Shengguan Cai, Lingzhen Ye, Yong Han, Dezhi Wu, Fei Dai, Chengdao Li, and Guoping Zhang. "Genetic architecture of limit dextrinase inhibitor (LDI) activity in Tibetan wild barley." BMC Plant Biology 14, no. 1 (2014): 117. http://dx.doi.org/10.1186/1471-2229-14-117.

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11

Du, Juan, Shumin Hu, Jianjun Dong, Ruihan Wu, Junhong Yu, and Hua Yin. "Exploring the factors that affect the themostability of barley limit dextrinase – Inhibitor complex." Journal of Molecular Graphics and Modelling 109 (December 2021): 108043. http://dx.doi.org/10.1016/j.jmgm.2021.108043.

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12

Ross, H. A., J. Sungurtas, L. Ducreux, J. S. Swanston, H. V. Davies, and G. J. McDougall. "Limit dextrinase in barley cultivars of differing malting quality: activity, inhibitors and limit dextrin profiles." Journal of Cereal Science 38, no. 3 (November 2003): 325–34. http://dx.doi.org/10.1016/s0733-5210(03)00048-1.

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13

Stahl, Y., R. D. Alexander, S. Coates, J. H. Bryce, H. R. Jenkinson, and P. C. Morris. "The barley limit dextrinase inhibitor: Gene expression, protein location and interaction with 14-3-3 protein." Plant Science 172, no. 3 (March 2007): 452–61. http://dx.doi.org/10.1016/j.plantsci.2006.10.008.

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14

Jensen, Johanne Mørch, Malene Bech Vester-Christensen, Marie Sofie Møller, Birgit C. Bønsager, Hans Erik Mølager Christensen, Maher Abou Hachem, and Birte Svensson. "Efficient secretory expression of functional barley limit dextrinase inhibitor by high cell-density fermentation of Pichia pastoris." Protein Expression and Purification 79, no. 2 (October 2011): 217–22. http://dx.doi.org/10.1016/j.pep.2011.04.009.

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15

Stahl, Yvonne, Steve Coates, James H. Bryce, and Peter C. Morris. "Antisense downregulation of the barley limit dextrinase inhibitor modulates starch granule size distribution, starch composition and amylopectin structure." Plant Journal 39, no. 4 (August 2004): 599–611. http://dx.doi.org/10.1111/j.1365-313x.2004.02159.x.

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16

MacGregor, A. W., L. J. Donald, E. A. MacGregor, and H. W. Duckworth. "Stoichiometry of the Complex formed by Barley Limit Dextrinase with its Endogenous Inhibitor. Determination by Electrospray Time-of-flight Mass Spectrometry." Journal of Cereal Science 37, no. 3 (May 2003): 357–62. http://dx.doi.org/10.1006/jcrs.2002.0500.

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17

Sissons, M. J., R. C. M. Lance, and D. H. B. Sparrow. "Studies on Limit Dextrinase in Barley. 3. Limit Dextrinase in Developing Kernels." Journal of Cereal Science 17, no. 1 (January 1993): 19–24. http://dx.doi.org/10.1006/jcrs.1993.1003.

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18

Sissons, M. J., R. C. M. Lance, and D. H. B. Sparrow. "Studies on limit dextrinase in barley I. Purification of malt limit dextrinase and production of monospecific antibodies." Journal of Cereal Science 16, no. 2 (September 1992): 107–16. http://dx.doi.org/10.1016/s0733-5210(09)80143-4.

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19

Bøjstrup, Marie, Caspar Elo Christensen, Michael Skovbo Windahl, Anette Henriksen, and Ole Hindsgaul. "A chromogenic assay for limit dextrinase and pullulanase activity." Analytical Biochemistry 449 (March 2014): 45–51. http://dx.doi.org/10.1016/j.ab.2013.12.004.

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20

McCleary, Barry V. "Measurement of the content of limit-dextrinase in cereal flours." Carbohydrate Research 227 (April 1992): 257–68. http://dx.doi.org/10.1016/0008-6215(92)85076-c.

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21

Mangan, David, Barry V. McCleary, Claudio Cornaggia, Ruth Ivory, Edward Rooney, and Vincent McKie. "Colourimetric and fluorimetric substrates for the assay of limit dextrinase." Journal of Cereal Science 62 (March 2015): 50–57. http://dx.doi.org/10.1016/j.jcs.2014.12.006.

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22

TARAVEL, Francois R., Roelf DATEMA, Wolfgang WOLOSZCZUK, J. John MARSHALL, and William J. WHELAN. "Purification and Characterization of a Pig Intestinal α-Limit Dextrinase." European Journal of Biochemistry 130, no. 1 (March 3, 2005): 147–53. http://dx.doi.org/10.1111/j.1432-1033.1983.tb07129.x.

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23

Schroeder, S. W., and A. W. MacGregor. "Synthesis of Limit Dextrinase in Germinated Barley Kernels and Aleurone Tissues." Journal of the American Society of Brewing Chemists 56, no. 1 (January 1998): 32–37. http://dx.doi.org/10.1094/asbcj-56-0032.

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24

Stenholm, Katharina, and Silja Home. "A New Approach to Limit Dextrinase and its Role in Mashing*." Journal of the Institute of Brewing 105, no. 4 (1999): 205–10. http://dx.doi.org/10.1002/j.2050-0416.1999.tb00020.x.

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25

Macgregor, Alexander W. "α-Amylase, Limit Dextrinase, and α-Glucosidase Enzymes in Barley and Malt." Critical Reviews in Biotechnology 5, no. 2 (January 1987): 117–28. http://dx.doi.org/10.3109/07388558709086972.

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26

Møller, Marie S., Michael S. Windahl, Lyann Sim, Marie Bøjstrup, Maher Abou Hachem, Ole Hindsgaul, Monica Palcic, Birte Svensson, and Anette Henriksen. "Oligosaccharide and Substrate Binding in the Starch Debranching Enzyme Barley Limit Dextrinase." Journal of Molecular Biology 427, no. 6 (March 2015): 1263–77. http://dx.doi.org/10.1016/j.jmb.2014.12.019.

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27

Wang, Xiaolei, Xuelei Zhang, Shengguan Cai, Lingzhen Ye, Meixue Zhou, Zhonghua Chen, Guoping Zhang, and Fei Dai. "Genetic Diversity and QTL Mapping of Thermostability of Limit Dextrinase in Barley." Journal of Agricultural and Food Chemistry 63, no. 14 (April 6, 2015): 3778–83. http://dx.doi.org/10.1021/acs.jafc.5b00190.

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28

Jin, Xiaoli, Shengguan Cai, Lingzhen Ye, Zhonghua Chen, Meixue Zhou, and Guoping Zhang. "Association of HvLDI with limit dextrinase activity and malt quality in barley." Biotechnology Letters 35, no. 4 (December 22, 2012): 639–45. http://dx.doi.org/10.1007/s10529-012-1106-1.

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29

McCafferty, Calum A., Helen R. Jenkinson, James M. Brosnan, and James H. Bryce. "Limit Dextrinase - Does Its Malt Activity Relate to Its Activity During Brewing?" Journal of the Institute of Brewing 110, no. 4 (2004): 284–96. http://dx.doi.org/10.1002/j.2050-0416.2004.tb00623.x.

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30

Sissons, Michael J. "Studies on the Activation and Release of Bound Limit Dextrinase in Malted Barley." Journal of the American Society of Brewing Chemists 54, no. 1 (January 1996): 19–25. http://dx.doi.org/10.1094/asbcj-54-0019.

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31

Walker, J. W., T. A. Bringhurst, A. L. Broadhead, J. M. Brosnan, and S. Y. Pearson. "The Survival of Limit Dextrinase during Fermentation in the Production of Scotch Whisky." Journal of the Institute of Brewing 107, no. 2 (2001): 99–106. http://dx.doi.org/10.1002/j.2050-0416.2001.tb00082.x.

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32

Sissons, Michael, Marcus Taylor, and Michael Proudlove. "Barley Malt Limit Dextrinase: Its Extraction, Heat Stability, and Activity During Malting and Mashing." Journal of the American Society of Brewing Chemists 53, no. 3 (June 1995): 104–10. http://dx.doi.org/10.1094/asbcj-53-0104.

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33

Longstaff, M. A., and J. H. Bryce. "Development of Limit Dextrinase in Germinated Barley (Hordeum vulgare L.) (Evidence of Proteolytic Activation)." Plant Physiology 101, no. 3 (March 1, 1993): 881–89. http://dx.doi.org/10.1104/pp.101.3.881.

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34

Siapush, Samaneh, and Azar Shahpiri. "Ethephon advances the release time of limit dextrinase from gibberellic acid-treated aleurone layer." Biocatalysis and Agricultural Biotechnology 9 (January 2017): 174–76. http://dx.doi.org/10.1016/j.bcab.2016.12.011.

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35

McDougall, Gordon J., Heather A. Ross, J. Stuart Swanston, and Howard V. Davies. "Limit dextrinase from germinating barley has endotransglycosylase activity, which explains its activation by maltodextrins." Planta 218, no. 4 (February 1, 2004): 542–51. http://dx.doi.org/10.1007/s00425-003-1141-1.

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36

Li, Fen, Jun-e. Zhang, Hong-Mei Liu, Shu-juan Tian, Xian-Guang Yang, Ji-Xian Ma, and Meng-Xiang Sun. "Comparative Study of Activity and Heat Stability of Limit Dextrinase in 16 Barley Cultivars." Cereal Chemistry Journal 85, no. 3 (May 2008): 271–75. http://dx.doi.org/10.1094/cchem-85-3-0271.

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37

Wang, Xu-dong, Juan Yang, and Guo-ping Zhang. "Genotypic and environmental variation in barley limit dextrinase activity and its relation to malt quality." Journal of Zhejiang University SCIENCE B 7, no. 5 (May 2006): 386–92. http://dx.doi.org/10.1631/jzus.2006.b0386.

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38

Nguemogne, A. C., Z. S. C. Desobgo, and E. J. Nso. "Comparative Study of Limit Dextrinase Potential of Three Sorghum Cultivars (Safrari, Madjeru, and S.35)." Journal of the American Society of Brewing Chemists 75, no. 3 (June 2017): 255–61. http://dx.doi.org/10.1094/asbcj-2017-3015-01.

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39

McCafferty, Calum A., Niklaus Perch-Nielsen, and James H. Bryce. "Effects of Aerobic and Anaerobic Germination on the Debranching Enzyme, Limit Dextrinase, in Barley Malt." Journal of the American Society of Brewing Chemists 58, no. 2 (April 2000): 47–50. http://dx.doi.org/10.1094/asbcj-58-0047.

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40

Vester-Christensen, Malene Bech, Maher Abou Hachem, Henrik Naested, and Birte Svensson. "Secretory expression of functional barley limit dextrinase by Pichia pastoris using high cell-density fermentation." Protein Expression and Purification 69, no. 1 (January 2010): 112–19. http://dx.doi.org/10.1016/j.pep.2009.08.016.

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41

Lecommandeur, Didier, Alexander W. MacGregor, and Jean Daussant. "Purification of germinated barley α-amylase isozymes and limit-dextrinase by chromatofocusing and affinity chromatography." Journal of Chromatography A 441, no. 2 (January 1988): 436–42. http://dx.doi.org/10.1016/s0021-9673(01)83891-7.

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42

Yang, Xinquan, Sharon Westcott, Xue Gong, Evan Evans, Xiao-Qi Zhang, Reg C. M. Lance, and Chengdao Li. "Amino acid substitutions of the limit dextrinase gene in barley are associated with enzyme thermostability." Molecular Breeding 23, no. 1 (August 15, 2008): 61–74. http://dx.doi.org/10.1007/s11032-008-9214-2.

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43

MacGregor, A. W., S. L. Bazin, L. J. Macri, and J. C. Babb. "Modelling the Contribution ofAlpha-Amylase,Beta-Amylase and Limit Dextrinase to Starch Degradation During Mashing." Journal of Cereal Science 29, no. 2 (March 1999): 161–69. http://dx.doi.org/10.1006/jcrs.1998.0233.

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44

Heisner, Craig B., and Charles W. Bamforth. "Thioredoxin in Barley: Could It Have a Role in Releasing Limit Dextrinase in Brewery Mashes?" Journal of the Institute of Brewing 114, no. 2 (2008): 122–26. http://dx.doi.org/10.1002/j.2050-0416.2008.tb00316.x.

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45

Zeeman, Samuel C., Thierry Delatte, Gaëlle Messerli, Martin Umhang, Michaela Stettler, Tabea Mettler, Sebastian Streb, Heike Reinhold, and Oliver Kötting. "Starch breakdown: recent discoveries suggest distinct pathways and novel mechanisms." Functional Plant Biology 34, no. 6 (2007): 465. http://dx.doi.org/10.1071/fp06313.

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The aim of this article is to provide an overview of current models of starch breakdown in leaves. We summarise the results of our recent work focusing on Arabidopsis, relating them to other work in the field. Early biochemical studies of starch containing tissues identified numerous enzymes capable of participating in starch degradation. In the non-living endosperms of germinated cereal seeds, starch breakdown proceeds by the combined actions of α-amylase, limit dextrinase (debranching enzyme), β-amylase and α-glucosidase. The activities of these enzymes and the regulation of some of the respective genes on germination have been extensively studied. In living plant cells, additional enzymes are present, such as α-glucan phosphorylase and disproportionating enzyme, and the major pathway of starch breakdown appears to differ from that in the cereal endosperm in some important aspects. For example, reverse-genetic studies of Arabidopsis show that α-amylase and limit-dextrinase play minor roles and are dispensable for starch breakdown in leaves. Current data also casts doubt on the involvement of α-glucosidase. In contrast, several lines of evidence point towards a major role for β-amylase in leaves, which functions together with disproportionating enzyme and isoamylase (debranching enzyme) to produce maltose and glucose. Furthermore, the characterisation of Arabidopsis mutants with elevated leaf starch has contributed to the discovery of previously unknown proteins and metabolic steps in the pathway. In particular, it is now apparent that glucan phosphorylation is required for normal rates of starch mobilisation to occur, although a detailed understanding of this step is still lacking. We use this review to give a background to some of the classical genetic mutants that have contributed to our current knowledge.

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46

Furegon, L., A. D. B. Peruffo, and A. Curioni. "Immobilization of rice limit dextrinase on γ-alumina beads and its possible use in starch processing." Process Biochemistry 32, no. 2 (February 1997): 113–20. http://dx.doi.org/10.1016/s0032-9592(96)00054-4.

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47

Bøjstrup, Marie, Lucia Marri, Finn Lok, and Ole Hindsgaul. "A Chromogenic Assay Suitable for High-Throughput Determination of Limit Dextrinase Activity in Barley Malt Extracts." Journal of Agricultural and Food Chemistry 63, no. 50 (December 10, 2015): 10873–78. http://dx.doi.org/10.1021/acs.jafc.5b04596.

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48

Kristensen, Michael, Finn Lok, Véronique Planchot, Ib Svendsen, Robert Leah, and Birte Svensson. "Isolation and characterization of the gene encoding the starch debranching enzyme limit dextrinase from germinating barley." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1431, no. 2 (May 1999): 538–46. http://dx.doi.org/10.1016/s0167-4838(99)00077-1.

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49

Evans, Evan, Bianca van Wegen, Yuefang Ma, and Jason Eglinton. "The Impact of the Thermostability of α-Amylase, β-Amylase, and Limit Dextrinase on Potential Wort Fermentability." Journal of the American Society of Brewing Chemists 61, no. 4 (September 2003): 210–18. http://dx.doi.org/10.1094/asbcj-61-0210.

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50

Kristensen, Michael, Véronique Planchot, Jun-ichi Abe, and Birte Svensson. "Large-Scale Purification and Characterization of Barley Limit Dextrinase, a Member of the α-Amylase Structural Family." Cereal Chemistry Journal 75, no. 4 (July 1998): 473–79. http://dx.doi.org/10.1094/cchem.1998.75.4.473.

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