Microbial lipases and their industrial applications: a comprehensive review

Chandra, Prem; Enespa,; Singh, Ramandeep; Arora, Pankaj

doi:10.1186/s12934-020-01428-8

Cited by 422 publications

(169 citation statements)

References 667 publications

(601 reference statements)

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“…Cold active/adapted enzymes are useful biotechnological tools due to their optimal activity at lower temperatures (1)(2)(3)(4). Esterase enzymes are particularly useful as they catalyse the hydrolysis of a wide variety of esters into their constituent alcohol and acid (5)(6)(7)(8)(9). Cold-adapted esterases are important for temperature sensitive applications such as synthesising fragile chiral compounds (10,11), cold washing laundry (12), environmental bioremediation (13) and the food industry (14).…”

Section: Introductionmentioning

confidence: 99%

Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation

Noby

Auhim

Winter

et al. 2021

Preprint

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Cold-active esterases hold great potential for undertaking useful biotransformations at low temperatures. Here, we determined the structure of a cold active family IV esterase (EstN7) cloned from Bacillus cohnii strain N1, which has an apparent melting temperature of 26°C. EstN7 is a dimer with a classical α/β hydrolase fold. It has an acidic surface that is thought to play a role in cold-adaption by retaining solvation under changed water solvent entropy at lower temperatures. However, dynamics do not appear to play a major role in cold adaption. Comparison of B-factors with the closest related mesophilic and thermophilic esterases suggests there is little difference in dynamics with the catalytically important N-terminal cap comprising the main dynamic element. Molecular dynamics, rigidity analysis, normal mode analysis and geometric simulations of motion confirm the flexibility of the cap region but suggest that the rest of the protein is largely rigid. Rigidity analysis indicates the distribution of hydrophobic tethers is appropriate to colder conditions, where the hydrophobic effect is weaker than in mesophilic conditions due to reduced water entropy. The conformation of the cap region is significantly different to EstN7′s closest relatives, forming a bridge-like structure with reduced helical content providing more than one access tunnel through to the active site. Thus, it is likely that increased substrate accessibility and tolerance to changes in water entropy are the main drivers of EstN7′s cold adaptation rather than changes in dynamics.

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Section: Introductionmentioning

confidence: 99%

Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation

Noby

Auhim

Winter

et al. 2021

Preprint

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“…(3)(4)(5). Esterases are especially useful as they can utilise a variety of ester substrates, catalysing their hydrolysis into their constituent alcohol and acid (6)(7)(8). Cold active/adapted enzymes are attracting particular attention as their optimal activity at lower temperatures can be applied to temperature sensitive processes (9)(10)(11)(12)(13)(14) such as: the pharmaceutical industry for synthesising fragile chiral compounds (15,16); detergent industry for cold washing (17); environmental bioremediation (18).…”

Section: Introductionmentioning

confidence: 99%

Structure guided engineering of a cold active esterase expands substrate range though a stabilisation mutation that allows access to a buried water chamber

Noby

Johnson

Tyzack

et al. 2021

Preprint

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Cold active esterases represent an important class of enzymes capable of undertaking useful chemical transformations at low temperatures. EstN7 from Bacillus cohnii represents a true psychrophilic esterase with a temperature optimum below 20°C. We have recently determined the structure of EstN7 and have used this knowledge to understand substrate specificity and expands its substrate range through protein engineering. Substrate range is determined by a plug at the end of acyl binding pocket that blocks access to a buried water filled cavity, so limiting EstN7 to turnover of C2 and C4 substrates. Data mining revealed a potentially important commercial reaction, conversion of triacetin to only the 1,2-glyceryl diacetate isomer, which the EstN7 was capable of achieving. Residues M187, N211 and W206 were identified as plug residues. M187 was identified as the key plug residue but mutation to alanine destabilised the structure as whole. Another plug mutation, N211A had a stabilising effect on EstN7 and suppressed the destabilising M187A mutation. The M187A-N211A variant had the broadest substrate range, capable of hydrolysing a C8 substrate. Thus, the structure of EstN7 together with focused engineering has provided new insights into the structural stability and substrate specificity that allowed expansion of substrate range.

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“…Microbial lipases include fungal, yeast, and bacterial lipases. The classification of bacterial lipases, in particular, can be divided into intracellular (glycoproteins) and extracellular (lipoproteins), and they are constitutive [5]. Bacterial lipases are reported to be more often substrate nonspecific and thermostable in addition to being abundant [3].…”

Section: Introductionmentioning

confidence: 99%

“…Bacterial lipases often originate from Streptomyces sp., Alcaligenes sp., Arthrobacter, Pseudomonas sp., Chromobacterium, and Achromobacter sp. [5]. Among all these, bacterial lipases from Staphylococcus sp.…”

Section: Introductionmentioning

confidence: 99%

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Effect of inoculum size, inducer and metal ion on lipase production by Rhodococcus strain UCC 0009

et al. 2020

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Lipases are critical enzymes for industrial applications such as in the food and pharmaceutical fields. Therefore, the discovery of new lipases with enhanced characteristics are always encouraged. Thus, the present study explored the ability of a novel bacterial strain isolated from a tropical climate for lipase production. The optimization method using the one-variable-at-a-time approach was adopted to obtain increased production of lipase. The strain identified as Rhodococcus strain UCC 0009 was able to generate specific lipase activity of 11.67a ± 0.00 mU/mg at optimized conditions of 8 % (v/v) inoculum concentration, 1 % (v/v) olive oil as the inducer, and the addition of Ca2+ions. The specific lipase activity increased by 162 % when the optimization using a one-variable-ata-time approach was adopted compared to that of the non-optimized counterpart, signifying this experimental phase’s importance. The present study’s findings revealed the potential of utilizing Rhodococcus strain UCC 0009 as a green lipase producer for application in bioremediation and biotransformation at an industrial scale. Further study concentrating on enzyme characterization and improving culture conditions for conducive production of lipase via statistical optimization using response surface methodology (RSM) will be attempted to elucidate further the superiority of lipase obtained from local resources.

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Microbial lipases and their industrial applications: a comprehensive review

Cited by 422 publications

References 667 publications

Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation

Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation

Structure guided engineering of a cold active esterase expands substrate range though a stabilisation mutation that allows access to a buried water chamber

Effect of inoculum size, inducer and metal ion on lipase production by Rhodococcus strain UCC 0009

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