The identification of a barley haze active protein that influences beer haze stability: Cloning and characterisation of the barley SE protein as a barley trypsin inhibitor of the chloroform/methanol type

Robinson, Louise H.; Juttner, Juan; Milligan, Andrew S.; Lahnstein, Jelle; Eglinton, J.; Evans, D. E.

doi:10.1016/j.jcs.2006.08.012

Cited by 52 publications

(40 citation statements)

References 32 publications

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“…There are three major groups of protein in barleybrewed beer. The first consists of a group of proline-rich fragments originating from hordein (15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32) that are involved in haze formation (14)(15)(16). The second is lipid transfer protein 1 (LTP1; 9.7 kDa in pure form), involved in foam stability (17)(18)(19).…”

Section: Introductionmentioning

confidence: 99%

Changes in protein molecular weight during cloudy wheat beer brewing

Zhang

et al. 2015

J. Inst. Brew.

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To investigate the changes in protein in cloudy wheat beer (CWB) brewing, the molecular weight (M w ) of protein components in wort, fermenting wort, beer and beer foam were analysed by high-performance size-exclusion chromatography. It was found that the M w of protein during brewing was mainly distributed between 100 and 0 kDa. From mash to the final beer, the most abundant protein component was the 7.6-2.1 kDa fraction, which occupied more than 40% of the total protein.The extraction of soluble protein from malts into wort mainly focused on the protein rest process, where the 100.0-32.1 and 7.6-2.1 kDa fractions increased significantly. In addition, the 100.0-13.2 kDa fraction was the predominant thermolabile protein that decreased during lautering and boiling. The dominant protein constituting the fine coagulum, the 100.0-13.2 kDa fraction, also decreased during fermentation and maturation. The CWB, defoamed CWB and CWB foam had similar protein M w distributions, while the CWB foam concentrated much more protein and the 7.6-2.1 kDa fraction was the major protein in the CWB foam.

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Section: Introductionmentioning

confidence: 99%

Changes in protein molecular weight during cloudy wheat beer brewing

Zhang

et al. 2015

J. Inst. Brew.

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“…During the malting and brewing process, malt proteinases completely or partially hydrolyse storage proteins and modify other proteins (5). The solubilization of malt storage proteins affects the qualities of the malt and the wort, and finally affects the beer quality, including the beer's nutritional value (6), haze stability (7) and foam characteristics.…”

Section: Introductionmentioning

confidence: 99%

Relationship between Kolbach index and other quality parameters of wheat malt

Jin

Zhang

et al. 2012

J. Inst. Brew.

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In order to determine suitable Kolbach indices in wheat malting, the relationships between the Kolbach index and other quality parameters in wheat malt were studied. Eight white wheat malts with different Kolbach indices (31.4, 33.1, 37.0, 37.6, 39.5, 40.7, 42.8 and 45.5%) from the same wheat variety were prepared. The increase ratio of the ALSP (albumins and other soluble proteins) and the decrease ratio of the glutenins were found to have a significant positive correlation with the Kolbach index, and the corresponding r-values were 0.883 and 0.975 (p < 0.01). The ALSP of the wheat malts had a positive correlation with chromaticity, extract, free amino nitrogen (FAN), viscosity, acidity, xylan glycosidase activity, endo-b-1,4-xylanase activity and malting loss (p < 0.05). When the Kolbach indices were 31.4, 33.1, 37.0, 37.6 and 39.5%, there was a positive correlation between the soluble xylan and the viscosity, and the r-value was 0.888 (p < 0.05). Comparing the malts, it could be concluded that, for this particular wheat variety, when the Kolbach index was 39.5%, the wheat malts exhibited the best characteristics; the extract was 81.98%, the FAN content was 166.03 mg per 100 mg, the saccharifying power was 496.72 WK, the viscosity was 1.61 cP, and the saccharification time was 6 min.

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“…A number of authors have pointed out that some CMproteins could be potentially useful for the transformation of plants of agronomic interest (Alfonso-Rubi et al 2003); moreover, the role played by some proteins of this group in the process of beer fermentation and their impact on the Wnal quality of this beverage has been highlighted (Robinson et al 2007). …”

Section: Introductionmentioning

confidence: 99%

WCI, a novel wheat chymotrypsin inhibitor: purification, primary structure, inhibitory properties and heterologous expression

Maro

Farisei

Panichi

et al. 2011

Planta

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A novel chymotrypsin inhibitor, detected in the endosperm of Triticum aestivum, was purified and characterized with respect to the main physical-chemical properties. On the basis of its specificity, this inhibitor was named WCI (wheat chymotrypsin inhibitor). WCI is a monomeric neutral protein made up of 119 residues and molecular mass value of 12,933.40 Da. Automated sequence and mass spectrometry analyses, carried out on several samples of purified inhibitor, evidenced an intrinsic molecular heterogeneity due to the presence of the isoform [des-(Thr)WCI], accounting for about 40% of the total sample. In vitro, WCI acted as a strong inhibitor of bovine pancreatic chymotrypsin as well as of chymotryptic-like activities isolated from the midgut of two phytophagous insects, Helicoverpa armigera (Hüb.) and Tenebrio molitor L., respectively. No inhibitory activities were detected against bacterial subtilisins, bovine pancreatic trypsin, porcine pancreatic elastase or human leukocyte elastase. The primary structure of WCI was significantly similar (45.7-89.1%) to those of several proteins belonging to the cereal trypsin/α-amylase inhibitor super-family and showed the typical sequence motif of this crowed protein group. The cDNA of the inhibitor (wci-cDNA) was isolated from wheat immature caryopses and employed to obtain a recombinant product in E. coli. Experimental evidences indicated that the recombinant inhibitor was localized in the inclusion bodies from which it was recovered as soluble and partially active protein by applying an appropriate refolding procedure. WCI reactive site localization, as well as its inhibitory specificity, was investigated by molecular modeling approach.

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The identification of a barley haze active protein that influences beer haze stability: Cloning and characterisation of the barley SE protein as a barley trypsin inhibitor of the chloroform/methanol type

Cited by 52 publications

References 32 publications

Changes in protein molecular weight during cloudy wheat beer brewing

Changes in protein molecular weight during cloudy wheat beer brewing

Relationship between Kolbach index and other quality parameters of wheat malt

WCI, a novel wheat chymotrypsin inhibitor: purification, primary structure, inhibitory properties and heterologous expression

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