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Enzyme value chains

As mentioned before, the number of o-glucosidic linkages split by malt a-amylase in the dextrinization period decreases with the degree of acid hydrolysis and when a is about 0.6 (60%) there is no further dextrinization (Table XXVIII). This is due to the fact mentioned before that the enzyme attacks chains with less than about eight members only with very low velocity. When the number of chain molecules with longer chains is calculated for different degrees of hydrolysis, values for the extent of the dextrinization are found which agree fairly well with those found in the experiment. [Pg.310]

The steady structure determined by the value of Kw (Fig. 1) for the entire class of carboxylic CP obtained by precipitation copolymerization is one of the most important factors determining the possibility of reversible bonding of proteins absorbed by carboxylic CP with a high sorption capacity [16,19]. Thus, for the MA-HHTT system (Fig. 2), a complete desorption of enzyme is carried out on crosslinked copolymers characterized by low Kw values. In crosslinked structures exhibiting looser structure (Kw P 1), owing to the mobility of chain fragments of CP especially in the process of desorption, the macromolecules of sorbed protein are irreversibly captured as a result of a marked polyfunctional interaction. [Pg.7]

The activities of pectic enzymes present in cultivation medium (98 mg of protein extracted from 2.5 1 of pectin medium) were poor, not leading to the clarification of cultivation medium indicating the cleavage of pectate chains, with values 0.024 pmol/min.mg for polygalacturonase, 0.004 pmol/min.mg for exopolygalacturonase, 0.034 pmol/min.mg for pectinesterase and 0.005 pmol/min.mg for pectin lyase. The production of individual pectic enzymes was dependent on the C-source used in the cultivation medium (Tab. 1). [Pg.902]

AtCCD7 (Schwartz et al. 2004). Organic solvent addition (dioxane, DMSO, methanol or acetone) improved activity under low concentrations (Mathieu et al. 2007). Short chain aliphatic alcohols activated the enzymes although the reason for this activation is unclear (probably due to influences on substrate accessibility or micellar structure). An increase in activity was observed for all aliphatic alcohols tested, although the optimal concentration lessened with increasing log P values (Schilling etal. 2007). [Pg.410]

There are companies focused to the biocatalytic area for which the commercialization of enzymes constitutes the main business. Some of them also include R D activities in the whole range of areas concerning adding value to their product chain. The following sections describe some of those companies, for which their enzyme or protein business results relevant for the scope of the present book. [Pg.249]


See other pages where Enzyme value chains is mentioned: [Pg.343]    [Pg.391]    [Pg.1144]    [Pg.5]    [Pg.45]    [Pg.646]    [Pg.133]    [Pg.296]    [Pg.206]    [Pg.365]    [Pg.616]    [Pg.224]    [Pg.391]    [Pg.128]    [Pg.215]    [Pg.245]    [Pg.258]    [Pg.329]    [Pg.376]    [Pg.976]    [Pg.646]    [Pg.346]    [Pg.156]    [Pg.7]    [Pg.13]    [Pg.31]    [Pg.162]    [Pg.352]    [Pg.216]    [Pg.450]    [Pg.457]    [Pg.463]    [Pg.319]    [Pg.328]    [Pg.338]    [Pg.360]    [Pg.384]    [Pg.384]    [Pg.337]    [Pg.350]    [Pg.356]    [Pg.376]    [Pg.101]    [Pg.243]    [Pg.421]    [Pg.280]   
See also in sourсe #XX -- [ Pg.107 , Pg.110 , Pg.111 , Pg.112 ]




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Value chain

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