Relevant bibliographies by topics / Limit dextrinase and limit dextrinase inhibitor

Academic literature on the topic 'Limit dextrinase and limit dextrinase inhibitor'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Limit dextrinase and limit dextrinase inhibitor"

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Stahl, Yvonne. "Characterisation of the barley limit dextrinase inhibitor and manipulation of its expression in transgenic barley." Thesis, Heriot-Watt University, 2003. http://hdl.handle.net/10399/417.

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McCafferty, Calum A. "Limit dextrinase activity during malting, mashing and distillery fermentation." Thesis, Heriot-Watt University, 2001. http://hdl.handle.net/10399/474.

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Gibson, Catherine Elizabeth. "The expression of hydrolytic enzymes in germinating barley grain." Thesis, 2017. http://hdl.handle.net/2440/114266.

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Modification of the barley grain endosperm in germination is fundamental to successful plant growth but also has important ramifications for down-stream industrial uses of barley, particularly in the malting and brewing industries. There are a battery of enzymes that are involved in the modification process but the sites of synthesis and action of only of a few of these have been described in detail and most have only been studied in isolated tissues. The development of a sensitive and robust in situ mRNA hybridization (ISH) procedure, which allows the detection of specific transcripts representing proteins in grain sections is described here. This first required the optimization of grain fixation, embedding and sectioning procedures as well as the adaptation of a staining method using calcofluor white to accurately assess the modification state of each grain prior to processing. Once these technical parameters were established, the non-radioactive ISH protocol was developed to allow the detection of transcripts of (1,3;1,4)-β-glucanases, (1→4)-β-endo-xylanases, limit dextrinase and limit dextrinase inhibitor in grain sections of the two barley cultivars Sloop and Himalaya. The panel of enzymes selected for study covers several aspects of grain modification, such as (1,3;1,4)-β-glucan, xylan and starch breakdown, which are all important for successful grain germination. The successful ISH technique proved sensitive enough to discriminate between the (1,3;1,4)-β-glucanase and xylanase isoenzymes and clearly defined whether the transcipts for these enzymes were synthesized in both a tissue-specific manner and a fixed temporal sequence during grain germination. The use of monoclonal antibodies specific for the two (1,3;1,4)-β-glucanase isoforms in a related immunolabelling procedure, using the same fixed grains, also allowed the patterns of transcript and protein appearance to be correlated. As expected, use of the ISH method showed that the transcripts of the (1,3;1,4)-β-glucanase, xylanase and limit dextrinase inhibitor genes are variously found in the aleurone cells, the starchy endosperm tissue and the scutellum. However, there were also substantial amounts of transcript detected in the tissues of the growing embryo which suggests that these enzymes may also contribute substantially to early seedling development.
Thesis (Ph.D.) -- University of Adelaide, School of Agriculture, Food and Wine, 2018
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"Studies of barley limit dextrinase." Title page, contents and summary only, 1991. http://web4.library.adelaide.edu.au/theses/09PH/09phs6185.pdf.

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Sissons, Michael John. "Studies of barley limit dextrinase." 1991. http://hdl.handle.net/2440/21633.

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Sissons, Michael John. "Studies of barley limit dextrinase." Thesis, 1991. http://hdl.handle.net/2440/21633.

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Books on the topic "Limit dextrinase and limit dextrinase inhibitor"

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Steholm, Katharina. Malt limit dextrinase and its importance in brewing. 1997.

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Book chapters on the topic "Limit dextrinase and limit dextrinase inhibitor"

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Bryce, James. "Limit Dextrinase." In Handbook of Food Enzymology. CRC Press, 2002. http://dx.doi.org/10.1201/9780203910450.ch60.

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MacGregor, E. "Limit Dextrinase/Pullulanase." In Handbook of Food Enzymology. CRC Press, 2002. http://dx.doi.org/10.1201/9780203910450.ch59.

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