Purification and characterization of β-agarase from agar-liquefying soil bacterium, Acinetobacter sp., AG LSL-1

Mariyanna, Lakshmikanth; Shinde, Manohar; Lalitha, Junna

doi:10.1016/j.procbio.2009.04.025

Cited by 29 publications

(14 citation statements)

References 31 publications

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“…Online: 2014-06-30 ISSN: 2300 2014 SciPress Ltd., Switzerland effectiveness of NAOS with DP 4-12 has been confirmed both in vivo and in vitro. They showed augmented growth of Bifidobacterium and Lactobacillus [3].…”

Section: International Letters Of Natural Sciencesmentioning

confidence: 78%

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Optimization of Agrase Production by Alkaline <i>Pseudomonas aeruginosa</i> ZSL-2 Using Taguchi Experimental Design

Ziayoddin

Lalitha

Shinde

2014

ILNS

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The culture conditions for the production of extracellular agarase by Pseudomonas aeruginosa ZSL-2 were optimized using One-Factor-At-A-Time combined with orthogonal array design. OneFactor-At-A-Time method investigates the effect of time, temperature, NaCl, carbon sources, nitrogen sources and pH on agarase production. The optimized culture conditions obtained from the statistical analysis were temperature of 30 °C, pH 8.5, NH 4 NO 3 2 g L -1 and agar 3 g L -1 . The L 9 orthogonal array design was used to select the fermentation parameters influencing the yield of agarase. The order of the factors affecting the fermentation process was found to be NH 4 NO 3 > pH > agar > temperature, with temperature playing a significant role on the agarase production (p < 0.10). The higher yields than those in basal media culture were obtained in the final optimized medium with activity of 0.439 ± 0.013 U ml -1 . Extracellular agarase hydrolysed agar into a range of oligosaccharides which were analysed by LC-ESI-MS spectrometry as anhydrogalactose, galactose, agarobiose, agarotetrose and agarohexaose.

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Section: International Letters Of Natural Sciencesmentioning

confidence: 78%

“…β-Agarase from Acinetobacter sp. AG LSL-1 [40] has been reported to hydrolyse agarose into NA4, and NA6 and to NA2 as the only final product.…”

mentioning

confidence: 99%

Optimization of Agrase Production by Alkaline <i>Pseudomonas aeruginosa</i> ZSL-2 Using Taguchi Experimental Design

Ziayoddin

Lalitha

Shinde

2014

ILNS

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“…Some soil or marine isolates of Acinetobacter sp. produce an agarase able to degrade agarose (41,42). Similarly to degradation products of chitin that induce competence in Vibrio cholera (43), the degradation products of agarose could represent the trigger of competence in A. baumannii.…”

Section: Discussionmentioning

confidence: 99%

Fluorescence-based detection of natural transformation in drug resistant Acinetobacter baumannii

Godeux

Lupo

Haenni

et al. 2018

Preprint

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Acinetobacter baumannii is a nosocomial agent with a high propensity for developing resistance to antibiotics. This ability relies on horizontal gene transfer mechanisms occurring in the Acinetobacter genus, including natural transformation. To study natural transformation in bacteria, the most prevalent method uses selection for the acquisition of an antibiotic resistance marker in a target chromosomal locus by the recipient cell. Most clinical isolates of A. baumannii are resistant to multiple antibiotics limiting the use of such selection-based method. Here we report the development of a phenotypic and selection-free method based on flow cytometry to detect transformation events in multidrug resistant (MDR) clinical A. baumannii isolates. To this end, we engineered a translational fusion between the abundant and conserved A. baumannii nucleoprotein (HU) and the superfolder green fluorescent protein (sfGFP). The new method was benchmarked against the conventional antibiotic selection-based method. Using this new method, we investigated several parameters affecting transformation efficiencies and identified conditions of transformability one hundred times higher than those previously reported. Using optimized transformation conditions, we probed natural transformation in a set of MDR clinical and non-clinical animal A. baumannii isolates. Regardless of their origin, the majority of the isolates displayed natural transformability, indicative of a conserved trait in the species. Overall, this new method and optimized protocol will greatly facilitate the study of natural transformation in the opportunistic pathogen A. baumannii.

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“…최근에는 해조류가 바이오에 탄올 생산을 위한 발효용 기질로 각광을 받으면서 아가레이즈에 대 한 관심도 증가하고 있다 [13,14]. [6,8,16,17]. 순도를 향상시키기 위하여 친화성 크로마 토그래피(affinity chromatography)를 병행하여 사용하기도 한다 [6].…”

Section: 서 론unclassified

Optimization of Anion-exchange Chromatography for the Separation of Agarase from Culture Broth of Pseudoalteromonas sp.

Kim¹,

Kim

Kim³

et al. 2011

Korean Chemical Engineering Research

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− Degradation products of agarose are biologically active and thus used as an ingredient in pharmaceuticals or functional cosmetics. Furthermore, it has been strongly considered as a substrate for bio-ethanol fermentation. Recently, we isolated new agarase-producing microorganism, Pseudoalteromonas sp. from south sea of Korea. In this study, we aimed to separate and purify the agarase from culture broth of this strain. Separation of agarase was performed by ion-exchange chromatography on DEAE-Sepharose resin. Equilibrium pH and volume ratio of resin to the amount of protein were optimized for the efficient adsorption of protein. 410 µg of protein was completely adsorbed to 3 mL of resin at pH 7.5. The total amount of eluted protein increased as NaCl concentration increased to 400 mM at iso- †

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Purification and characterization of β-agarase from agar-liquefying soil bacterium, Acinetobacter sp., AG LSL-1

Cited by 29 publications

References 31 publications

Optimization of Agrase Production by Alkaline <i>Pseudomonas aeruginosa</i> ZSL-2 Using Taguchi Experimental Design

Optimization of Agrase Production by Alkaline <i>Pseudomonas aeruginosa</i> ZSL-2 Using Taguchi Experimental Design

Fluorescence-based detection of natural transformation in drug resistant Acinetobacter baumannii

Optimization of Anion-exchange Chromatography for the Separation of Agarase from Culture Broth of Pseudoalteromonas sp.

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