Abstract:SummaryThe effect of a nonionic surfactant, polyoxyethylenesorbitan monolaurate (Tween 20), on the hen egg-white lysozyme catalyzed lysis of a dried cell suspension of Micrococcus lysodeikticus is analyzed. A rate enhancement of up to 70% is observed in the presence of surfactant a t concentrations above the critical micelle concentration. This activity increase may be explained by postulating the existence of a micelle-enzyme complex in which enzyme molecules are bound to micelles with preferential orientatio… Show more
“…Similar surface-dilution kinetics have been described for phospholipase A2 and phosphatidylserine carboxylase (Dennis, 1973;Warner & Dennis, 1975). Bernath & Vieth (1972) have described a similar enhancement in lysozyme activity in the presence of surfactant concentrations in excess of the critical micelle concentration. They believed that activation of the enzyme was due to an orientation effect inside the mixed micelle.…”
The physical properties and the methods used for interconversion of three forms of cholesterol oxidase extracted from Nocardia rhodochrous by treatment with Triton X-100, trypsin or buffer alone provide evidence that these forms differ chiefly in the possession or absence of a hydrophobic anchor region connected by a trypsin-sensitive region. The hydrophobic domain normally integrates the enzyme into the cell membrane and confers amphipathic properties on the solubilized enzyme, causing adsorption to hydrophobic resins, aggregation when detergent is removed and formation of mixed micelles with detergent and cholesterol resulting in surface-dilution kinetic behaviour and activation by relatively high concentrations of water-miscible solvents. By contrast, only the enzymic fragment is extracted with trypsin and it behaves as a conventional soluble enzyme and does not aggregate or interact with hydrophobic resins, detergents or water-miscible solvents. As no phospholipid could be detected in the enzyme extracts, the detergent appears to act as a substitute for the cell-membrane lipids that would normally interact with the hydrophobic region. This cholesterol oxidase is an example of a prokaryotic enzyme possessing two closely associated catalytic functions, dehydrogenase and isomerase activities, and an anchoring function.
“…Similar surface-dilution kinetics have been described for phospholipase A2 and phosphatidylserine carboxylase (Dennis, 1973;Warner & Dennis, 1975). Bernath & Vieth (1972) have described a similar enhancement in lysozyme activity in the presence of surfactant concentrations in excess of the critical micelle concentration. They believed that activation of the enzyme was due to an orientation effect inside the mixed micelle.…”
The physical properties and the methods used for interconversion of three forms of cholesterol oxidase extracted from Nocardia rhodochrous by treatment with Triton X-100, trypsin or buffer alone provide evidence that these forms differ chiefly in the possession or absence of a hydrophobic anchor region connected by a trypsin-sensitive region. The hydrophobic domain normally integrates the enzyme into the cell membrane and confers amphipathic properties on the solubilized enzyme, causing adsorption to hydrophobic resins, aggregation when detergent is removed and formation of mixed micelles with detergent and cholesterol resulting in surface-dilution kinetic behaviour and activation by relatively high concentrations of water-miscible solvents. By contrast, only the enzymic fragment is extracted with trypsin and it behaves as a conventional soluble enzyme and does not aggregate or interact with hydrophobic resins, detergents or water-miscible solvents. As no phospholipid could be detected in the enzyme extracts, the detergent appears to act as a substitute for the cell-membrane lipids that would normally interact with the hydrophobic region. This cholesterol oxidase is an example of a prokaryotic enzyme possessing two closely associated catalytic functions, dehydrogenase and isomerase activities, and an anchoring function.
“…To maintain proper surface tension, non-ionic surfactants are preferred for enzyme-based inks as they would cause less unwanted interaction with the protein conformation 14 . The concentration of surfactant used in the ink solution could also be a critical factor to influence enzymatic activity 26 . However, to our knowledge, there are no studies concerning the factor of surface tension on the activity of inkjetted enzyme.…”
Inkjet printing of enzymes can facilitate many novel applications where a small amount of materials need to be deposited in a precise and flexible manner. However, maintaining the satisfactory activity of inkjet printed enzyme is a challenging task due to the requirements of ink rheology and printhead parameters. Thus to find optimum inkjetting conditions we studied the effects of several ink formulation and jetting parameters on lysozyme activity using a piezoelectric printhead. Within linear activity range of protein concentrations ink containing 50 µg/mL lysozyme showed a satisfactory activity retention of 85%. An acceptable activity of jetted ink was found at pH 6.2 and ionic strength of 0.06 molar. Glycerol was found to be an effective viscosity modifier (10–15 mPa.s), humectant and protein structure stabilizer for the prepared ink. A non-ionic surfactant when used just below critical micelle concentration was found to be favourable for the jetted inks. An increase in activity retention was observed for inks jetted after 24 hours of room temperature incubation. However, no additional activity was seen for inkjetting above the room temperature. Findings of this study would be useful for formulating other protein-based inks and setting their inkjet printing parameters without highly compromising the functionality.
“…Pyricularia oryzae P 21) and Glomerella cingulata G 4-1-4 3 ) were used. Botrytis cinerea, Colletotrichum lagenalium and Alternaria kikuchiana Y -33 (Polyoxins tolerant strain) were supplied by Kumiai Chemical Industry Co., Ltd. Tokyo.…”
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