Annual Progress Report on Malting Barley Research March, 2002

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142 Personnel Dr. B.L. Jones, Supervisory Research Chemist Mr. A.D. Budde, Plant Physiologist Mr. M.E. Marinac, Physical Science Tech. Ms. L.M. Short, Laboratory Tech.* Mr. C.H. Martens, Biological Science Tech. Mr. E.D. Goplin, Laboratory Tech.** Mr. L.E. Hornbacher, Physical Science Tech. Dr. D.M. Peterson, Research Leader Ms. D.K. Schaefer, Secretary *AMBA supported ** Partially AMBA supported
143 CHARACTERIZATION OF THE PROTEIN HYDROLYZING SYSTEMS OF MASHES AND MALTS Berne L. Jones, Debora Fontanini and Laurie Marinac. Cereal Crops Research Unit, USDA, ARService and Department of Agronomy, University of Wisconsin, Madison, WI Overall Objectives To further define the biology and biochemistry of the protein hydrolysis processes that occur during the malting and mashing operations of brewing. The hydrolysis of proteins into metabolizable low-molecular-weight nitrogenous compounds is one of the most important aspects of malting and brewing, yet there are still many aspects of this process that are not known. This is an ongoing study to determine which proteolytic enzymes are involved in these processes, what barley and malt endogenous inhibitors can repress the activities of these proteinases, and which of the proteinases and inhibitors really affect the release of ‘soluble protein’ during malting and mashing. Knowing these things will make it possible to more scientifically and efficiently design malting barleys that are even better suited for their particular end uses. Purification and characterization of three cysteine proteases from green malt Laurie Marinac and Berne L. Jones Objective The objective of this study is to purify and characterize some of the green malt cysteine class proteases that have not been investigated previously. The enzymes being studied have gelatinase activities that are stable throughout kilning and they maintain their activities during mashing until they are inactivated during the ‘conversion’ step, when the temperature is increased to 72°C. One of these enzymes hydrolyzes the substrate protein gelatin in vitro at a very high rate during incubation at 40 o C. The others digest gelatin at about the same rate as the two cysteine proteases that we have studied previously; the 30 and 31 kiloDalton proteases that were purified and characterized by Poulle (Plant Physiol., 88: 1454_1460, 1988) and Zhang (Planta 199:565-572, 1996) respectively. All three of the enzymes being studied, however, digest significant amounts of gelatin within 30 min of incubation at 40 o C after separation with a 2-D, IEF x PAGE analysis method, and thus are some of the most active ones that occur in green malt extracts. The cysteine proteases of barley are apparently the main enzymes that are responsible for breaking down the insoluble storage proteins into low molecular weight compounds during malting. The characteristics of the enzymes that are now being studied differ significantly from those studied previously, and understanding the roles of the various proteases is fundamental to understanding how the protein hydrolyzing system in barley functions. This, in turn, is critical for gaining a more complete understanding of what happens to the barley proteins during malting and mashing and how this affects brewing.
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Annual Pro
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-i- INTRODUCTION The March 2002 <st
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Barley Transformation G.J. Muehlbau
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1 2000/2001 WINTER NURSERY: BARLEY
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3 2001 Barley Stripe Rust Screening
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5 Triumph/Tyra//Arupo, a selection
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7 Washington (Fossum Cereals and Wa
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9 This project is supported by the
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11 ‘Triumph’, ‘Valier’, ‘
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13 Table 2. Agronomic data for sele
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15 Table 4. Agronomic data for sele
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17 Table 8. Malting quality data* f
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19 Six-rowed barley selections of c
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21 Table 14. Agronomic data for sel
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23 Table 16. Agronomic data for win
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25 Table 19. Malting quality data*
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Garnet/98Ab11865 Garnet/98Ab12895 9
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29 rust resistant NSGC accessions o
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31 DEVELOPMENT OF SIX-ROWED MALTING
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33 backcrossing. The selfed lines w
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35 MINNESOTA BARLEY IMPROVEMENT PRO
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37 ADVANCED LINE EVALUATION Varieti
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39 OTHER BARLEY DISEASES In 2001, r
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41 Wingbermuehle, W. J., K.M. Belin
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43 In 2001 winter/spring, over 300
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45 assessments were made by countin
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47 IDENTIFICATION OF NOVEL DISEASE
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49 Unfortunately, disease levels in
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51 BARLEY TRANSFORMATION G.J. Muehl
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53 We have available the sugarcane
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55 Secondly, we tried to grow F. gr
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57 References: Issac, S. and Jennin
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59 Huntley-dryland) with two replic
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61 Table 2. 1992 thru 2001 Overall
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63 performance for Montana farmers.
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65 Blake, T,. Hensleigh P., Boss D.
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67 settling tower cannot accommodat
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Table 3. Seedling reaction to strip
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71 TWO-ROWED BARLEY IMPROVEMENT PRO
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Table 1. Agronomic trait comparison
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75 mutants reduce plant vigor and g
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77 SIX-ROWED BARLEY IMPROVEMENT PRO
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79 this variety has decreased over
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Table 7. Malt quality comparisons o
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83 • Management studies for malt
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85 STUDIES ON BARLEY DISEASES AND T
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87 With funding from the US Wheat a
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89 MALTING AND BREWING QUALITY OF B
Page 99 and 100: 91 β-glucans, it might be most ins
Page 101 and 102: 10 9 8 7 6 5 4 3 2 1 0 93 Figure 1.
Page 103 and 104: 95 Bolin, P., Schwarz, P., Jones, B
Page 105 and 106: 97 Results Results from field and g
Page 107 and 108: 99 DEVELOPING BARLEY TISSUE CULTURE
Page 109 and 110: 101 trials of plants regenerated fr
Page 111 and 112: 103 Table 2. Agronomic performance
Page 113 and 114: 105 BSMV spread between entries. Ho
Page 115 and 116: 107 involving two susceptible backg
Page 117 and 118: 109 THE OREGON BARLEY IMPROVEMENT P
Page 119 and 120: 111 for traits that are difficult/e
Page 121 and 122: Germplasm Development: 113 Crosses:
Page 123 and 124: 115 • All lines in spring yield t
Page 125 and 126: 117 Table 2. Agronomic data for Ore
Page 127 and 128: 119 Table 6. Malting quality of win
Page 129 and 130: 121 Table 7. Across location summar
Page 131 and 132: 123 MOLECULAR MARKER ASSISTED MODIF
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Page 135 and 136: 127 exchanges. Spring and winter ba
Page 137 and 138: 129 Table 2. 2000-2001 Agronomic Pe
Page 139 and 140: 131 Table 7. Spring 2- and 6-Row #
Page 141 and 142: 133 2. Direct Seeding Cropping Syst
Page 143 and 144: 135 D.M. Wesenberg - spring and win
Page 145 and 146: 137 A STUDY OF THE MALTING QUALITY
Page 147 and 148: 139 Methods. Our malting schedule.
Page 149: 141 modification measures indicated
Page 153 and 154: 145 Purification of a serine endope
Page 155 and 156: 147 STUDIES ON THE PROTEINASES THAT
Page 157 and 158: 149 with the proteinase T will be s
Page 159 and 160: 151 10°C increase in thermostabili
Page 161 and 162: 153 Sissons MJ and MacGregor AW (19
Page 163 and 164: µM Carbohydrate / Unit of α-Gluco
Page 165 and 166: 157 Tissue-specific gene products f
Page 167 and 168: 159 The promoters were subcloned fr
Page 169: 161 Fig. 3. Expression of Trx-Hth f
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Annual Progress Report on Malting Barley Research March, 2002

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