Biotechnological Applications of Cold-Adapted Organisms by E. Remaut, C. Bliki, M. Iturriza-Gomara, K. Keymeulen

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By E. Remaut, C. Bliki, M. Iturriza-Gomara, K. Keymeulen (auth.), Professor Rosa Margesin, Professor Franz Schinner (eds.)

There is an expanding curiosity of biotechnologists within the capability of cold-adapted organisms, when you consider that they play an immense function within the procedures of nutrient turnover and first biomass construction in chilly ecosystems. crucial merits of the appliance of such organisms are the swift microbial metabolism at low temperatures, the low activation strength for enzymatic substrate hydrolysis and the low thermostability of enzymes from cold-adapted organisms. merits is usually deduced from the frost hardiness and frost resistance of cold-adapted vegetation and animals.

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Agric BioI Chern 1987; 51: 3201-3206. 63. Ashina Y, Watanabe I. Dramatic development of enzymatic process for acrylamide production. Kagaku to Kogyo 1990; 43:1098-1101 (in Japanese). 64. Sonomoto K, Tanaka A. Application of lipase in organic solvents for the preparation of optically active terpene alcohol esters. Ann NY Acad Sci 1988; 542:235-239. 65. Hoshino T, Yamane T, Shimizu S. Selective hydrolysis of fish oil by lipase to concentrate n-3 polyunsaturated fatty acids. Agric BioI Chern 1990; 54:1459-1467.

L 6 By the early 1980's over 25mesophile-derived enzymes and proteins had been studied at sub-zero temperatures. At such temperatures, enzyme reaction intermediates are more long-llved and therefore easier to characterizeP-21 The most common solvents for cryoenzymology are: 1. water-miscible organic co-solvent systems (I-phase systems), 2. water-in-oil micro emulsions or reverse micelles, 3. water-in-oil macro emulsions. 22,23 Water co-solvent miXtures containing about 50% (w/w) organic component can be cooled to between -44°C and -66°C without freezing.

51- 53 Effects on enzyme stability depend on the ratio of AOT to water and on the isoelectric point of the enzyme (or effective charge). Enzyme destabilization occurs when there is strong interaction with the anionic headgroups of the AOT. Enzymes that are negatively charged experience less structural perturbation as a result of being repulsed from the water-surfactant interface. R. K. Owusu Apenten 40 Cytochrome C (having a net charge of +8) was modified by acylation or succinylation to produce variants with net charges of -3 and -8.

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