Adaptational properties and applications of cold-active lipases from psychrophilic bacteria

Maiangwa, Jonathan; Ali, Mohd Shukuri Mohamad; Salleh, Abu Bakar; Rahman, Raja Noor Zaliha Raja Abdul; Shariff, Fairolniza Mohd; Leow, Adam Thean Chor

doi:10.1007/s00792-014-0710-5

Cited by 57 publications

(30 citation statements)

References 144 publications

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“…These features make these hydrolytic enzymes potential biocatalysts for use in several industrial fields . Studies have revealed the strong potency of cold‐active lipases for the organic synthesis of valuable short‐chain esters such as flavors used in food and pharmaceuticals . Amylases are essential in the conversion of starches into oligosaccharides and they are used in the production of maltodextrin, glucose or fructose syrups and in different sectors like textile, paper, and detergent industries .…”

Section: Discussionmentioning

confidence: 99%

Bioprospecting around Arctic islands: Marine bacteria as rich source of biocatalysts

Santi

Altermark

Pascale

et al. 2015

J. Basic Microbiol.

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We have investigated the biotechnological potential of Arctic marine bacteria for their ability to produce a broad spectrum of cold-active enzymes. Marine bacteria exhibiting these features are of great interest for both fundamental research and industrial applications. Macrobiota, water and sediment samples have been collected during 2010 and 2011 expeditions around the Lofoten and Svalbard islands. Bacteria were isolated from this material and identified through 16S rRNA gene sequence analysis for the purpose of establishing a culture collection of marine Arctic bacteria. Herein, we present the functional screening for different extracellular enzymatic activities from 100 diversely chosen microbial isolates incubated at 4 and 20 °C. The production of esterase/lipase, DNase, and protease activities were revealed in 67, 53, and 56% of the strains, respectively, while 41, 23, 9, and 7% of the strains possessed amylase, chitinase, cellulase, and xylanase activities, respectively. Our findings show that phylogenetically diverse bacteria, including many new species, could be cultured from the marine arctic environment. The Arctic polar environment is still an untapped reservoir of biodiversity for bioprospecting.

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Section: Discussionmentioning

confidence: 99%

Bioprospecting around Arctic islands: Marine bacteria as rich source of biocatalysts

Santi

Altermark

Pascale

et al. 2015

J. Basic Microbiol.

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“…However, these organisms, through evolutionary processes, developed metabolic capabilities that enable them to survive and multiply at low temperatures [ 3 , 4 ]. Cold-active biocatalysts from psychrophilic microbial strains are attractive with respect to applications that profit from low-temperature reaction conditions, for example due to thermal instability of products and reactants, like in the food processing industry, or the need to efficiently inactivate the biocatalysts during downstream processes, as exemplified by enzymes for bio-chemical synthesis or molecular research [ 5 – 8 ]. Advantages of such enzymes are their often high rates of catalytic activity at low temperature, low temperature optima and less resistance to thermal inactivation as compared to their mesophilic counterparts.…”

Section: Introductionmentioning

confidence: 99%

Isolation and genome sequencing of four Arctic marine Psychrobacter strains exhibiting multicopper oxidase activity

et al. 2016

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BackgroundMarine cold-temperature environments are an invaluable source of psychrophilic microbial life for new biodiscoveries. An Arctic marine bacterial strain collection was established consisting of 1448 individual isolates originating from biota, water and sediment samples taken at a various depth in the Barents Sea, North of mainland Norway, with an all year round seawater temperature of 4 °C. The entire collection was subjected to high-throughput screening for detection of extracellular laccase activity with guaiacol as a substrate.ResultsIn total, 13 laccase-positive isolates were identified, all belonging to the Psychrobacter genus. From the most diverse four strains, based on 16S rRNA gene sequence analysis, all originating from the same Botryllus sp. colonial ascidian tunicate sample, genomic DNA was isolated and genome sequenced using a combined approach of whole genome shotgun and 8 kb mate-pair library sequencing on an Illumina MiSeq platform. The genomes were assembled and revealed genome sizes between 3.29 and 3.52 Mbp with an average G + C content of around 42 %, with one to seven plasmids present in the four strains. Bioinformatics based genome mining was performed to describe the metabolic potential of these four strains and to identify gene candidates potentially responsible for the observed laccase-positive phenotype. Up to two different laccase-like multicopper oxidase (LMCO) encoding gene candidates were identified in each of the four strains. Heterologous expression of P11F6-LMCO and P11G5-LMCO2 in Escherichia coli BL21 (DE3) resulted in recombinant proteins exhibiting 2,2'-azino-bis-3-ethylbenzothiazoline-6-sulphonic acid (ABTS) and guaiacol oxidizing activity.ConclusionsThirteen Psychrobacter species with laccase-positive phenotype were isolated from a collection of Arctic marine bacteria. Four of the isolates were genome sequenced. The overall genome features were similar to other publicly available Psychrobacter genome sequences except for P11G5 harboring seven plasmids. However, there were differences at the pathway level as genes associated with degradation of phenolic compounds, nicotine, phenylalanine, styrene, ethylbenzene, and ethanolamine were detected only in the Psychrobacter strains reported in this study while they were absent among the other publicly available Psychrobacter genomes. In addition, six gene candidates were identified by genome mining and shown to possess T1, T2 and T3 copper binding sites as the main signature of the three-domain laccases. P11F6-LMCO and P11G5-LMCO2 were recombinantly expressed and shown to be active when ABTS and guaiacol were used as substrates.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-016-2445-4) contains supplementary material, which is available to authorized users.

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“…Lipases or triacylglycerol acyl ester hydrolases belong to the serine hydrolase family; they are called carboxylic acid esterases, numbered as EC 3.1.1.3, and are a group of Sources of lipase A Review on Geotrichum Lipases: Production, Purification, Immobilization and Applications 18 Advances in Candida (C.) rugosa lipases covering production, purification and structure and activity 19 Overview on Rhizopus lipases with a focus on their structure, protein engineering and their biotechnological applications 20 Yeast and fungal lipases and their cellular physiology and biotechnological applications 21 Cold-evolved lipases from psychrophilic bacteria and their peculiar properties along with their potential biotechnological applications 22 Role of microbial lipases in green chemistry and eco-friendly processes 23 Medical and pharmaceutical application…”

Section: Lipase Structurementioning

confidence: 99%

Recent advances on sources and industrial applications of lipases

Sarmah

Revathi

Sheelu

et al. 2017

Biotechnology Progress

273

148

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Lipases are the industrially important biocatalysts, which are envisioned to have tremendous applications in the manufacture of a wide range of products. Their unique properties such as better stability, selectivity and substrate specificity position them as the most expansively used industrial enzymes. The research on production and applications of lipases is ever growing and there exists a need to have a latest review on the research findings of lipases. The present review aims at giving the latest and broadest overall picture of research and development on lipases by including the current studies and progressions not only in the diverse industrial application fields of lipases, but also with regard to its structure, classification and sources. Also, a special emphasis has been made on the aspects such as process optimization, modeling, and design that are very critical for further scale-up and industrial implementation. The detailed tabulations provided in each section, which are prepared by the exhaustive review of current literature covering the various aspects of lipase including its production and applications along with example case studies, will serve as the comprehensive source of current advancements in lipase research. This review will be very useful for the researchers from both industry as well as academia in promoting lipolysis as the most promising approaches to intensified, greener and sustainable processes. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 34:5-28, 2018.

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Adaptational properties and applications of cold-active lipases from psychrophilic bacteria

Cited by 57 publications

References 144 publications

Bioprospecting around Arctic islands: Marine bacteria as rich source of biocatalysts

Bioprospecting around Arctic islands: Marine bacteria as rich source of biocatalysts

Isolation and genome sequencing of four Arctic marine Psychrobacter strains exhibiting multicopper oxidase activity

Recent advances on sources and industrial applications of lipases

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