Biocatalysis in organic media using enzymes from extremophiles

Sellek, Gerard Alexander; Chaudhuri, Julian B.

doi:10.1016/s0141-0229(99)00075-7

Cited by 208 publications

(97 citation statements)

References 145 publications

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“…Mechanisms of protein stability in aqueous and nonaqueous environments 1,2 , the links between conformational mobility, structural integrity and activity 3,4 , and the complexities of substrate specificity have all succumbed to the onslaught of advanced molecular methods, including crystallography 5-7 , site-specific mutagenesis, gene shuffling, and protein evolution [8][9][10][11] . Scientists are now in a position to visualize, if not design, catalytic systems that approach the functional "ideal".…”

Section: Introductionmentioning

confidence: 99%

The search for the ideal biocatalyst

2002

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While the use of enzymes as biocatalysts to assist in the industrial manufacture of fine chemicals and pharmaceuticals has enormous potential, application is frequently limited by evolution-led catalyst traits. The advent of designer biocatalysts, produced by informed selection and mutation through recombinant DNA technology, enables production of process-compatible enzymes. However, to fully realize the potential of designer enzymes in industrial applications, it will be necessary to tailor catalyst properties so that they are optimal not only for a given reaction but also in the context of the industrial process in which the enzyme is applied.The past two decades have led to major advances in our understanding of the subtleties of protein structure-function interrelationships. Mechanisms of protein stability in aqueous and nonaqueous environments 1,2 , the links between conformational mobility, structural integrity and activity 3,4 , and the complexities of substrate specificity have all succumbed to the onslaught of advanced molecular methods, including crystallography 5-7 , site-specific mutagenesis, gene shuffling, and protein evolution [8][9][10][11] . Scientists are now in a position to visualize, if not design, catalytic systems that approach the functional "ideal".The "ideal" catalyst is typically considered by the biochemist in terms of turnover number (k cat ) or, for a given process, in terms of maximum specificity constant (A cat /KM). However, from a bioprocess viewpoint, each bioprocess is constrained by a set of conditions dictated by the specific properties of the substrates, products, and the bioconversion reaction. Thus, while for any given bioprocess it is clearly possible to specify a set of catalyst properties that would constitute the ideal for that process, only broad generalizations for ideality may otherwise be identified.In this review, we discuss molecular properties of enzymes from a bioprocess viewpoint. A paradigm for design based on the ideal process determining the desired features of the catalyst is presented. "Ideal" characteristics (generic and process-specific) and methodologies for seeking or engineering these are discussed. We then review the extent to which significant changes in protein functional properties have been achieved by application of these methods, together with issues that require more research and/or development. Ideal processesBioprocess engineers develop processes not only against fixed capital and operating expenditure, but also rapid, and often, very aggressive timelines. This is particularly the case for pharmaceutical products where patent expiry on the product demands a robust and scalable process with short development times 12 . Conventionally, once a synthetic route is fixed and the biocatalytic step defined, bioprocess design and operation are centered on the properties of the

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Section: Introductionmentioning

confidence: 99%

The search for the ideal biocatalyst

2002

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“…Dramatic residual activity depletion which occurred at 60% v/v could signify a point of transition to either denaturation or molten globule MG formation. Some proteins showed transitions from preferential exclusion to preferential binding as DMSo concentration was increased (4,36). Stabilization results from compaction of the enzyme structures by the exclusion of the solvent molecules from the enzyme hydration layer.…”

Section: Resultsmentioning

confidence: 99%

The Role of Lid in Protein-Solvent Interaction of the Simulated Solvent Stable Thermostable Lipase fromBacillusStrain 42 in Water-Solvent Mixtures

Hamid¹,

Rahman²,

Salleh³

et al. 2009

Biotechnology & Biotechnological Equipment

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“…Halophilic microorganisms generally produce salt requiring enzymes as a result of adaptation to high salt conditions. Since salt reduces water activity (a feature in common with organic solvent systems), halophilic enzymes are considered to be valuable tools as biocatalysts in aqueous-organic media [195,230,231]. A summary of organic solvent stability profile of some alkaline proteases is listed in Table 4.…”

Section: Alkaline Proteases From Organic Solvent Tolerant Microbesmentioning

confidence: 99%

Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

Garg¹,

Singh²

2015

Enz Eng

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Since the advent and release of Bio 40 (the first detergent with bacterial alkaline protease) in 1959, exploration of the microbial alkaline proteases has been exploited beyond expectations. The inventory of microbial alkaline proteases is difficult to draft as it is increasing daily. Most of these proteases are the result of studies in which one or a few isolates were targeted for an alkali-stable enzyme. Although, the worldwide research on microbial alkaline proteases has been widely performed, we still need an improved enzyme capable of catalyzing reactions under extreme conditions (also called as extremozymes), e.g., high alkalinity and salinity, anhydrous environment, cold and hot environment, etc. As the search for extremozymes is in progress, it is imperative to explore the extreme environments to get some novel microbial strains (extremophiles) for alkali-stable proteases. This review article is an effort to compile the scattered information on some extremophiles and their alkali-stable proteases, which may have better specific industrial applications. It includes: (i) various extreme environments relevant to industrial biocatalysts, (ii) strategies of extremophilic microbes and enzymes which make them able to tolerate such conditions, and (iii) an overview of some important work done so far to explore industrially relevant extremophilic enzymes from extremophiles.

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Biocatalysis in organic media using enzymes from extremophiles

Cited by 208 publications

References 145 publications

The search for the ideal biocatalyst

The search for the ideal biocatalyst

The Role of Lid in Protein-Solvent Interaction of the Simulated Solvent Stable Thermostable Lipase fromBacillusStrain 42 in Water-Solvent Mixtures

Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

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