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      Research and Application of Marine Microbial Enzymes: Status and Prospects

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          Abstract

          Over billions of years, the ocean has been regarded as the origin of life on Earth. The ocean includes the largest range of habitats, hosting the most life-forms. Competition amongst microorganisms for space and nutrients in the marine environment is a powerful selective force, which has led to evolution. The evolution prompted the marine microorganisms to generate multifarious enzyme systems to adapt to the complicated marine environments. Therefore, marine microbial enzymes can offer novel biocatalysts with extraordinary properties. This review deals with the research and development work investigating the occurrence and bioprocessing of marine microbial enzymes.

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          Most cited references56

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          Drugs from the deep: marine natural products as drug candidates.

          In recent years, marine natural product bioprospecting has yielded a considerable number of drug candidates. Most of these molecules are still in preclinical or early clinical development but some are already on the market, such as cytarabine, or are predicted to be approved soon, such as ET743 (Yondelis). Research into the ecology of marine natural products has shown that many of these compounds function as chemical weapons and have evolved into highly potent inhibitors of physiological processes in the prey, predators or competitors of the marine organisms that use them. Some of the natural products isolated from marine invertebrates have been shown to be, or are suspected to be, of microbial origin and this is now thought to be the case for the majority of such molecules. Marine microorganisms, whose immense genetic and biochemical diversity is only beginning to be appreciated, look likely to become a rich source of novel chemical entities for the discovery of more effective drugs.
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            Extremophiles as a source of novel enzymes for industrial application.

            Extremophilic microorganisms are adapted to survive in ecological niches such as at high temperatures, extremes of pH, high salt concentrations and high pressure. These microorganisms produce unique biocatalysts that function under extreme conditions comparable to those prevailing in various industrial processes. Some of the enzymes from extremophiles have already been purified and their genes successfully cloned in mesophilic hosts. In this review we will briefly discuss the biotechnological significance of extreme thermophilic (optimal growth 70-80 degrees C) and hyperthermophilic (optimal growth 85-100 degrees C) archaea and bacteria. In particular, we will focus on selected extracellular-polymer-degrading enzymes, such as amylases, pullulanases, cyclodextrin glycosyltransferases, cellulases, xylanases, chitinases, proteinases and other enzymes such as esterases, glucose isomerases, alcohol dehydrogenases and DNA-modifying enzymes with potential use in food, chemical and pharmaceutical industries and in environmental biotechnology.
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              Cold active microbial lipases: some hot issues and recent developments.

              Lipases are glycerol ester hydrolases that catalyze the hydrolysis of triglycerides to free fatty acids and glycerol. Lipases catalyze esterification, interesterification, acidolysis, alcoholysis and aminolysis in addition to the hydrolytic activity on triglycerides. The temperature stability of lipases has regarded as the most important characteristic for use in industry. Psychrophilic lipases have lately attracted attention because of their increasing use in the organic synthesis of chiral intermediates due to their low optimum temperature and high activity at very low temperatures, which are favorable properties for the production of relatively frail compounds. In addition, these enzymes have an advantage under low water conditions due to their inherent greater flexibility, wherein the activity of mesophilic and thermophilic enzymes are severely impaired by an excess of rigidity. Cold-adapted microorganisms are potential source of cold-active lipases and they have been isolated from cold regions and studied. Compared to other lipases, relatively smaller numbers of cold active bacterial lipases were well studied. Lipases isolated from different sources have a wide range of properties depending on their sources with respect to positional specificity, fatty acid specificity, thermostability, pH optimum, etc. Use of industrial enzymes allows the technologist to develop processes that closely approach the gentle, efficient processes in nature. Some of these processes using cold active lipase from C. antarctica have been patented by pharmaceutical, chemical and food industries. Cold active lipases cover a broad spectrum of biotechnological applications like additives in detergents, additives in food industries, environmental bioremediations, biotransformation, molecular biology applications and heterologous gene expression in psychrophilic hosts to prevent formation of inclusion bodies. Cold active enzymes from psychrotrophic microorganisms showing high catalytic activity at low temperatures can be highly expressed in such recombinant strains. Thus, cold active lipases are today the enzymes of choice for organic chemists, pharmacists, biophysicists, biochemical and process engineers, biotechnologists, microbiologists and biochemists.
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                Author and article information

                Journal
                Mar Drugs
                MD
                Marine Drugs
                Molecular Diversity Preservation International
                1660-3397
                2010
                23 June 2010
                : 8
                : 6
                : 1920-1934
                Affiliations
                [1 ] Department of Chemistry, Pukyong National University, Busan, 608-737, Korea
                [2 ] Key laboratory of Molecular Enzymology and Enzyme Engineering of Ministry Education, Jilin University, Changchun, 130023, China; E-Mail: ahxczc@ 123456yahoo.cn
                [3 ] Marine Bioprocess Research Center, Pukyong National University, Busan, 608-737, Korea
                Author notes
                *Author to whom correspondence should be addressed; E-Mail: sknkim@ 123456pknu.ac.kr ; Tel.: +82-51-629-7097; Fax: +82 -51-629-7099.
                Article
                marinedrugs-08-01920
                10.3390/md8061920
                2901830
                20631875
                5e4ef9d2-c28d-4afd-bc09-5e392f323f2a
                © 2008 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland

                This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                : 10 May 2010
                : 15 June 2010
                : 22 June 2010
                Categories
                Review

                Pharmacology & Pharmaceutical medicine
                lipase,protease,marine microbial enzymes,polysaccharide-degrading enzyme,extremozymes

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