Industrial enzyme applications

Kirk, Ole; Borchert, Torben V.; Fuglsang, Claus C.

doi:10.1016/s0958-1669(02)00328-2

Cited by 1,223 publications

(719 citation statements)

References 30 publications

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“…a-Amylase has at least six different industrial applications (including a part of the process for the production of ethanol from corn starch) (Kirk et al 2002). The heat-stable a-amylase protein that we used (from Bacillus licheniformis, and denoted BLA), is a single subunit protein with a molecular weight (MW) of 55 kDa; it has no disulfide bonds and has 28 lysine residues.…”

Section: Resultsmentioning

confidence: 99%

“…Enzymes are used as catalysts in various industrial, commercial, and pharmaceutical applications (Kirk et al 2002;Soetaert and Vandamme 2006); they are more selective, more efficient, and less toxic than many synthetic catalysts. Among their disadvantages (in commercial or industrial applications) are their low thermostability, their propensity to aggregate, their high cost, and their potential to act as allergens.…”

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confidence: 99%

“…The largest application of enzymes in industrial biotechnology, both in terms of quantity and cost, is the use of a-amylases, cellulases, lipases, and proteases in commercial cleaning solutions, e.g., fabric cleaners (Kirk et al 2002). Among the surfactants commonly used in commercial cleaners are the anionic surfactants sodium dodecyl sulfate (SDS, also known as sodium lauryl sulfate, or SLS), sodium lauryl ether sulfate (SLES), and the nonionic surfactant Triton X-100 (i.e., 4- [1,1,3,3-tetramethylbutyl]phenyl-polyethylene glycol).…”

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confidence: 99%

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Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation

et al. 2008

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This paper reports that the acetylation of lysine e-NH 3 + groups of a-amylase-one of the most important hydrolytic enzymes used in industry-produces highly negatively charged variants that are enzymatically active, thermostable, and more resistant than the wild-type enzyme to irreversible inactivation on exposure to denaturing conditions (e.g., 1 h at 90°C in solutions containing 100-mM sodium dodecyl sulfate). Acetylation also protected the enzyme against irreversible inactivation by the neutral surfactant TRITON X-100 (polyethylene glycol p-(1,1,3,3-tetramethylbutyl)phenyl ether), but not by the cationic surfactant, dodecyltrimethylammonium bromide (DTAB). The increased resistance of acetylated aamylase toward inactivation is attributed to the increased net negative charge of a-amylase that resulted from the acetylation of lysine ammonium groups (lysine e-NH 3 + ! e-NHCOCH 3 ). Increases in the net negative charge of proteins can decrease the rate of unfolding by anionic surfactants, and can also decrease the rate of protein aggregation. The acetylation of lysine represents a simple, inexpensive method for stabilizing bacterial a-amylase against irreversible inactivation in the presence of the anionic and neutral surfactants that are commonly used in industrial applications.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation

et al. 2008

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“…As a complement, a directed evolution strategy may be employed where mutations are semi-randomly introduced to create a large library of microorganisms with diverse phenotypes. 1,3,7 Subsequently, the microorganism library is screened for variants with a desired phenotype, e.g. improved production of an enzyme.…”

Section: Introductionmentioning

confidence: 99%

High-throughput screening for industrial enzyme production hosts by droplet microfluidics

et al. 2014

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A high-throughput method for single cell screening by microfluidic droplet sorting is applied to a whole-genome mutated yeast cell library yielding improved production hosts of secreted industrial enzymes. The sorting method is validated by enriching a yeast strain 14 times based on its α-amylase production, close to the theoretical maximum enrichment. Furthermore, a 10 5 member yeast cell library is screened yielding a clone with a more than 2-fold increase in α-amylase production. The increase in enzyme production results from an improvement of the cellular functions of the production host in contrast to previous droplet-based directed evolution that has focused on improving enzyme protein structure. In the workflow presented, enzyme producing single cells are encapsulated in 20 pL droplets with a fluorogenic reporter substrate. The coupling of a desired phenotype (secreted enzyme concentration) with the genotype (contained in the cell) inside a droplet enables selection of single cells with improved enzyme production capacity by droplet sorting. The platform has a throughput over 300 times higher than that of the current industry standard, an automated microtiter plate screening system. At the same time, reagent consumption for a screening experiment is decreased a million fold, greatly reducing the costs of evolutionary engineering of production strains.

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“…1 Apart from their function in living cells, since ancient times, enzymes have been used in preparation of food products such as cheese, beer, wine, vinegar, and in manufacture commodities such as linen, leather, and indigo. 2 Due to increasing progress in enzyme discovery, enzyme engineering, and biotechnology, enzymes have been used more often for in vitro applications, for example, as catalyst in enzymatic polymerizations. The use of enzymes as an in vitro catalyst offers many advantages such as high selectivity and specificity, preventing complicated step reactions, and reducing undesired byproducts.…”

Section: ■ Introductionmentioning

confidence: 99%

Lipase-Catalyzed Ring-Opening Copolymerization of ε-Caprolactone and β-Lactam

Stavila¹,

Ekenstein²,

Woortman³

et al. 2013

Biomacromolecules

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The enzymatic ring-opening copolymerization of ε-caprolactone (ε-CL) and β-lactam by using Candida antarctica lipase B (CAL-B) as catalyst was studied. Variation of the feed ratios of 25:75, 50:50, and 75:25 of ε-CL/β-lactam was performed. The products contain poly(ε-CL-co-β-lactam) and the homopolymers of poly(ε-CL) and poly(β-lactam). The structure of the copolymers was determined by MALDI-ToF MS. Poly(ε-CL-co-β-lactam) has an alternating and random structure consisting of alternating repeating units with oligo(ε-CL) or oligo(β-lactam). The highest fraction of the alternating copolymers resulted from the reaction with a feed ratio 50:50. The copolymer is a semicrystalline polymer with a T m at 124 °C and T g s at −15 and 50 °C. Interestingly, the copolymer also demonstrated cold crystallization at 29 and 74 °C, after quenching the sample from the melt in liquid nitrogen.

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Industrial enzyme applications

Cited by 1,223 publications

References 30 publications

Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation

Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation

High-throughput screening for industrial enzyme production hosts by droplet microfluidics

Lipase-Catalyzed Ring-Opening Copolymerization of ε-Caprolactone and β-Lactam

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