Wheat proteinase

Among the EST database of ragi sequences, there are two groups of bifunctional proteinase inhibitor trypsin a-amylase from seeds of ragi sequences. The upper clade was further subdivided (Fig. 6.10). Wang et al. (2008) concluded that there was great diversity in the sequence of different Bowman-Birk inhibitors in emmer wheat both within and between populations. 

Proteolysis occurring in sourdough and its rheological consequences related to gluten degradation are mainly caused by wheat proteinases that are activated in... 

Belozersky, M.A., Sarbakanova, S.T., Dunaevsky, Y.E. 1989. Aspartic proteinase from wheat seeds Isolation, properties and action on gliadin. Planta 177 321-326. 

Bleukx, W., Brijs, K., Torrekens, S., Van Leuven, F., Delcour, I. A. 1998. Specificity of a wheat gluten aspartic proteinase. Biochim Biophys Acta 1387 317-324. 

Bottari, A., Capocchi, A., Fontanini, D., Galleschi, L. 1996. Major proteinase hydrolysing gliadin during wheat germination. Phytochemistry 43 39 44. 

First, the structure of wheat serine carboxypeptidase II described by Liao et al. (1992) serves as good evidence of possible relationships. Serine carboxypeptidases are found in virtually every higher organism (Breddam, 1986), and some are of considerable importance, such as the proteinase involved in the regulation of blood pressure in humans (Odya and Erdos, 1981). 

P.H.A. Sneath, J.T. Staley, and S.T. Williams, eds), 9th Ed. Williams and Wilkins, Baltimore. Bleukx, W. and Delcour, J.A. 2000. A second aspartic proteinase associated with wheat gluten. 

Every, D., Farrell, J.A., Stufkens, M.W., and Wallace, A.R. 1998. Wheat cultivar susceptibility to grain damage by the New Zealand wheat bug, Nysius huttoni, and cultivar susceptibility to the effects of bug proteinase on baking quality. J. Cereal Sci. 27, 37 46. 

In Hoffman (1999), the following statanent is made Some of the sources noted for various protease inhibitors and proteinase inhibitors include black-eyed peas, lima beans, kidney beans, wheat and rye germ, potatoes, bovine cartilage, bee venom, and viper venom. Human bronchial secretions and guinea pig blood are other sources. 

Studies on the early responses of aleurone layers to GA have shown that a-amy-lase is not the first enzyme to be secreted. Within 5 h of the addition of GA to isolated aleurone layers of barley (cv. Betzes) there is increased secretion into the surrounding medium of several hydrolytic enzymes, including an ATP-ase, phytase, j -glucosidase and phosphomonoesterase, as well as some soluble carbohydrate [96] (probably sucrose). Similar observations were made using GA-treated half-grains of both barley and wheat (the distal embryoless half), although in barley additional enzymes, e.g. an esterase, phosphodiesterase and a-galactosidase were also found to be secreted early [96]. From the limited information available to date it appears that some enzymes which are secreted early after GA addition (e.g. phosphomonoesterase and phosphodiesterase) do so in response to lower concentrations of GA than do the later ones (e.g. a-amylase) [97]. Furthermore, a-amylase and proteinase, which are secreted simultaneously, have identical GA dose-response curves (Fig. 7.5A and B). There are exceptions, however, and further work on more enzymes is required to determine if the sequence of enzyme production by aleurone tissue is related to GA concentration in the cells. 

Fig. 15.37. The effect of a proteinase preparation on resistance to extension (in extensogram units) of a wheat flour dough (according to Sproessler, 1980). Proteinase preparation 1 fungal, 2 papain, and 3 bacterial. Unb proteinase activity units determined with hemoglobin as a substrate...

In the works of A. Konarev (Konarev et al. 1999 Konarev et al., 2004) shows in detail the variability of inhibitors of trypsin-like proteinases in cereals due to resistance to various grain pests. So in wheat trypsin inhibitors are represented by several genetically independent systems of proteins controlled by the genome and B chromosomes ID (endosperm), 3Dp (aleurone layer), IDS and 3Ap (leaf). Trypsin inhibitors of rye are controlled chromosome 3R and barley 3H. The most complex structure of inhibitors was wheat leaves, with the genomic formula AABBDD. In general, it is the sum of the spectra of trypsin inhibitors from several tetraploid (T. turgidum) (AABB) and (Aegilops tauschii Coss.) (DD) (Konarev, 1986 Konarev et al., 2004). 

Konarev, Al.V. (1986). Analysis of proteinase inhibitors from wheat grain by gelatin replicas. Biochemistry, Vol. 51, No. 2, pp. 195-200, ISSN 1608-3040... 

Yuldasheva, G.A., Zhidomirov, G.M., Ilin, A.I. (2011). A quantum-chemical model of the inhibition mechanism of viral DNA HIV-1 replication by Iodine complex compounds. Natural Science, Vol. 3, No. 7, pp. 573-579, ISSN 2150-4091 Zemke, K.J., Muller-Fahrnow, A., Jany, K. (1991). The three-dimensional structure of the bifunctional proteinase K/ alpha-amylase inhibitor from wheat (PK13) at 2.5 A resolution. PEES, Vol. 397, pp.240-242, ISSN 1742-4658... 

---