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Effect of the polymerization degree. moisture content. and temperature on kinetics of hydrolysis of corn starch by a-Amylase was studied. The degree of hydrolysis of the corn starch by a-amylase at low moisture content was shown to be strongly dependent on the initial starch polymerization degree and the thermodynamic activity of water in the system. Der EinfluR des Polymerisationsgrades, des Feuchtigkeitsgehaltes und der Temperatur auf die Kinetik der Hydrolyse von Maisstarke durch alpha-Amylase. Die Wirkung des Polynicrisationsgrades. des Feuchtigkeitsgehaltes und der Temperatur auf die Kinetik der Hydrolyse von Maisstarke durch a-Amylase wurde untersucht. Der Hydrolysegrad der Maisstarke durch a-Amylase bei niedrigem Feuchtigkeitsgehalt war stark abhangig von dem anfanglichen Polymerisationsgrad und dcr thermodynamischen Aktivitat des Wassers in dem System. ' ) Contribution No. 92-57'2-5 from Kansas Agricultural Experiment Station. Manhattan, KS 66506. \rarch/starke 45 (1991) Nr. 2. S. 65-70 t? VCH Verlagsgesellschaft mbH. D-6940 Weinheim. 1993 0038-905h/93/0202-~5$03.50+.25/0

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A biotechnological method for the modification of grain legume meals (pea, faba bean) is proposed. The essence of this method is the inducing of biochemical processes, which occur at the germination, through the treatment of a meal with an acid protease. Modified meals can replace soybean protein isolate as meat extenders. In particular, the modification of pea meal improves the colour of combined meat products and eliminates their beany off-flavour. The concentration of six-carbon aldehydes in combined sausages is reduced after the modification of pea meal.

The specific integral hydrophobicity of denatured forms of legumin and legumin-T from broad beans was evaluated through their hydration heat capacities. These were calculated as differences between partial heat capacities obtained from differential scanning microcalorimetry data and heat capacities in the gas phase, which were calculated by the use of the method of additive group contributions, taking into account the expansion of protein molecule in the gas phase. It is shown that there is no significant difference between the data for denatured forms of both proteins. The comparative evaluation of the hydration heat capacities of native forms of legumin and legumin-T was carried out. It is shown that the native legumin-T has a greater value of the hydration heat capacity and respectively is more hydrophobic than the native legumin. On the basis of the values of differences between the heat capacities in denatured and native states it is shown that the accessible hydrophobic surface of the native legumin-T related to a mean amino acid residue is 8-13 A* greater than that of the native legumin.