Microbial communities inhabiting the Antarctic Ocean show extremophilic adaptations conferring interesting properties to their enzymes, which could be exploited for biotechnology and bioremediation. As use of cold- and salt-tolerant enzymes allows to limit costs, reduce contaminations, and minimize pretreatments[1], we recently screened our Antarctic strain collection, comprising 186 morphologically diverse microorganisms isolated from marine biofilms and seawater from Terra Nova Bay (Ross Sea, Antarctica). The screening highlighted proteolytic (52.2%), lipolytic (38.2%), amylolytic (28%), chitinolytic (8.6%) and laccase-like (13.4%) activities amongst the strains. In particular, a new protein (Ant laccase) belonging to the copper resistance system multicopper oxidase family was characterized, produced by seawater Halomonas sp. strain M68. Ant laccase oxidizes ABTS and 2,6-dimethoxy phenol, and shows good thermostability, maintaining more than 40% of its maximal activity at 10°C. Furthermore, it is salt- and organic solvent-tolerant, paving the way for its use in harsh conditions[2]. Meanwhile, a chitin deacetylaselike activity was identified in Acinetobacter sp. strain c33, isolated from marine biofilm. It proved able to quickly deacetylate para-nitroacetanilide as well as chitosan and colloidal chitin in under 24 hours at 37°C, and was not inhibited by salts. As chitin is currently considered a waste product of the seafood industry, this enzyme could be applied to valorise it by producing higher-value chitosan and chitooligosaccharides under mild conditions[3]. Our efforts show that bioprospecting Antarctic marine microbial biodiversity can lead to the identification of innovative enzymes with promising industrial applications.
Identification of new extremozymes for biomasses valorisation through bioprospecting of marine antarctic microbial communities
M. Bisaccia
;E. Binda;F. Berini;E. Rosini;L. Pollegioni;F. Marinelli
2023-01-01
Abstract
Microbial communities inhabiting the Antarctic Ocean show extremophilic adaptations conferring interesting properties to their enzymes, which could be exploited for biotechnology and bioremediation. As use of cold- and salt-tolerant enzymes allows to limit costs, reduce contaminations, and minimize pretreatments[1], we recently screened our Antarctic strain collection, comprising 186 morphologically diverse microorganisms isolated from marine biofilms and seawater from Terra Nova Bay (Ross Sea, Antarctica). The screening highlighted proteolytic (52.2%), lipolytic (38.2%), amylolytic (28%), chitinolytic (8.6%) and laccase-like (13.4%) activities amongst the strains. In particular, a new protein (Ant laccase) belonging to the copper resistance system multicopper oxidase family was characterized, produced by seawater Halomonas sp. strain M68. Ant laccase oxidizes ABTS and 2,6-dimethoxy phenol, and shows good thermostability, maintaining more than 40% of its maximal activity at 10°C. Furthermore, it is salt- and organic solvent-tolerant, paving the way for its use in harsh conditions[2]. Meanwhile, a chitin deacetylaselike activity was identified in Acinetobacter sp. strain c33, isolated from marine biofilm. It proved able to quickly deacetylate para-nitroacetanilide as well as chitosan and colloidal chitin in under 24 hours at 37°C, and was not inhibited by salts. As chitin is currently considered a waste product of the seafood industry, this enzyme could be applied to valorise it by producing higher-value chitosan and chitooligosaccharides under mild conditions[3]. Our efforts show that bioprospecting Antarctic marine microbial biodiversity can lead to the identification of innovative enzymes with promising industrial applications.
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