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Journal articles on the topic 'Agarases'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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1

Han, Wenjun, Yuanyuan Cheng, Dandan Wang, Shumin Wang, Huihui Liu, Jingyan Gu, Zhihong Wu, and Fuchuan Li. "Biochemical Characteristics and Substrate Degradation Pattern of a Novel Exo-Type β-Agarase from the Polysaccharide-Degrading Marine Bacterium Flammeovirga sp. Strain MY04." Applied and Environmental Microbiology 82, no. 16 (June 3, 2016): 4944–54. http://dx.doi.org/10.1128/aem.00393-16.

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ABSTRACTExo-type agarases release disaccharide units (3,6-anhydro-l-galactopyranose-α-1,3-d-galactose) from the agarose chain and, in combination with endo-type agarases, play important roles in the processive degradation of agarose. Several exo-agarases have been identified. However, their substrate-degrading patterns and corresponding mechanisms are still unclear because of a lack of proper technologies for sugar chain analysis. Herein, we report the novel properties of AgaO, a disaccharide-producing agarase identified from the genusFlammeovirga. AgaO is a 705-amino-acid protein that is unique to strain MY04. It shares sequence identities of less than 40% with reported GH50 β-agarases. Recombinant AgaO (rAgaO) yields disaccharides as the sole final product when degrading agarose and associated oligosaccharides. Its smallest substrate is a neoagarotetraose, and its disaccharide/agarose conversion ratio is 0.5. Using fluorescence labeling and two-stage mass spectrometry analysis, we demonstrate that the disaccharide products are neoagarobiose products instead of agarobiose products, as verified by13C nuclear magnetic resonance spectrum analysis. Therefore, we provide a useful oligosaccharide sequencing method to determine the patterns of enzyme cleavage of glycosidic bonds. Moreover, AgaO produces neoagarobiose products by gradually cleaving the units from the nonreducing end of fluorescently labeled sugar chains, and so our method represents a novel biochemical visualization of the exolytic pattern of an agarase. Various truncated AgaO proteins lost their disaccharide-producing capabilities, indicating a strict structure-function relationship for the whole enzyme. This study provides insights into the novel catalytic mechanism and enzymatic properties of an exo-type β-agarase for the benefit of potential future applications.IMPORTANCEExo-type agarases can degrade agarose to yield disaccharides almost exclusively, and therefore, they are important tools for disaccharide preparation. However, their enzymatic mechanisms and agarose degradation patterns are still unclear due to the lack of proper technologies for sugar chain analysis. In this study, AgaO was identified as an exo-type agarase of agarose-degradingFlammeovirgabacteria, representing a novel branch of glycoside hydrolase family 50. Using fluorescence labeling, high-performance liquid chromatography, and mass spectrum analysis technologies, we provide a useful oligosaccharide sequencing method to determine the patterns of enzyme cleavage of glycosidic bonds. We also demonstrate that AgaO produces neoagarobiose by gradually cleaving disaccharides from the nonreducing end of fluorescently labeled sugars. This study will benefit future enzyme applications and oligosaccharide studies.
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2

Flament, Didier, Tristan Barbeyron, Murielle Jam, Philippe Potin, Mirjam Czjzek, Bernard Kloareg, and Gurvan Michel. "Alpha-Agarases Define a New Family of Glycoside Hydrolases, Distinct from Beta-Agarase Families." Applied and Environmental Microbiology 73, no. 14 (May 18, 2007): 4691–94. http://dx.doi.org/10.1128/aem.00496-07.

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ABSTRACT The gene encoding the α-agarase from “Alteromonas agarilytica” (proposed name) has been cloned and sequenced. The gene product (154 kDa) is unrelated to β-agarases and instead belongs to a new family of glycoside hydrolases (GH96). The α-agarase also displays a complex modularity, with the presence of five thrombospondin type 3 repeats and three carbohydrate-binding modules.
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3

Liao, Li, Xue-Wei Xu, Xia-Wei Jiang, Yi Cao, Na Yi, Ying-Yi Huo, Yue-Hong Wu, Xu-Fen Zhu, Xin-qi Zhang, and Min Wu. "Cloning, Expression, and Characterization of a New β-Agarase fromVibriosp. Strain CN41." Applied and Environmental Microbiology 77, no. 19 (August 5, 2011): 7077–79. http://dx.doi.org/10.1128/aem.05364-11.

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ABSTRACTA new agarase, AgaACN41, cloned fromVibriosp. strain CN41, consists of 990 amino acids, with only 49% amino acid sequence identity with known β-agarases. AgaACN41belongs to the GH50 (glycoside hydrolase 50) family but yields neoagarotetraose as the end product. AgaACN41was expressed and characterized.
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4

Achudhan, Arunmozhi Bharathi, and Mahalakshmi Velrajan. "MOLECULAR CHARACTERIZATION OF β-AGARASE PRODUCED BY SPHINGOMONAS PAUCIMOBILIS, A MARINE BACTERIUM." Bacterial Empire 4, no. 2 (April 2, 2021): e159. http://dx.doi.org/10.36547/be.159.

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Agarases are enzymes that catalyze the hydrolysis of agar. The present study was carried out to isolate the agar degrading microorganisms from marine source. The characterization of agar degrading organism was done by VITEK 2.0 automated instrument, which confirmed the sample as Spinghomonas paucimobilis by a set of 64 biochemical tests. Production of agarase, an extracellular enzyme was done in mineral salt broth with agar and the enzyme was purified by ammonium sulphate precipitation and dialysis. The molecular weight of the enzyme was determined by SDS-PAGE method. Fourier transform infrared spectroscopy analysis was done to authenticate the degree of degradation of agar. The presence of agarase gene was targeted using the required primers and amplified by Polymerase chain reaction. Also the study addresses the problem of solid waste generation of agar waste by any microbiological laboratories and industries.
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5

Kawaroe, Mujizat, Dwi Setyaningsih, Bertoka Fajar SP Negara, and Dina Augustine. "Potential Marine Fungi Hypocreaceae sp. as Agarase Enzyme to Hydrolyze Macroalgae Gelidium latifolium (Potensi Jamur Hypocreaceae sp. sebagai Enzim Agarase untuk menghidrolisis Makroalga Gelidium latifolium)." ILMU KELAUTAN: Indonesian Journal of Marine Sciences 20, no. 1 (March 3, 2015): 45. http://dx.doi.org/10.14710/ik.ijms.20.1.45-51.

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Agarase dapat mendegradasi agar ke oligosakarida dan memiliki banyak manfaat untuk makanan, kosmetik, dan lain-lain. Banyak spesies pendegradasi agar adalah organismelaut. Beberapa agarase telah diisolasi dari genera yang berbeda dari mikroorganisme yang ditemukan di air dan sedimen laut. Hypocreaceae sp. diisolasi dari air laut Pulau Pari, Kepulauan Seribu, Jakarta, Indonesia. Berdasarkan hasil identifikasi gen 16S rDNA dari 500 basis pasangan, isolat A10 memiliki 99% kesamaan dengan Hypocreaceae sp. Enzim agarase ekstraseluler dari Hypocreaceae sp. memiliki pH dan suhu optimum pada 8 TrisHCl (0,148 μ.mL-1) dan 50°C (0,182 μ.mL-1), masing-masing. Enzim Agarase dari Hypocreaceae sp. mencapai kondisi optimum pada aktivitas enzim tertinggi selama inkubasi dalam 24 jam (0,323 μ.mL-1). SDS page mengungkapkan bahwa ada dua band dari protein yang dihasilkan oleh agarase dari Hypocreaceae sp. yang berada di berat molekul 39 kDa dan 44 kDa dan hidrolisis Gelidium latifolium diperoleh 0,88% etanol. Kata kunci: enzim agarase, Hypocreaceae sp., hidrolisis, fungi, rDNA. Agarase can degradedagarto oligosaccharide and has a lot of benefits for food, cosmetics, and others. Many species of agar- degrader are marine-organism. Several agarases have been isolated from different genera of microorganisms found in seawater and marine sediments. Hypocreaceae sp. was isolated from sea water of Pari Islands, Seribu Islands, Jakarta, Indonesia. Based on the results of the 16S rDNA gene identification of 500 base pairs, A10 isolates had 99 % similarity toHypocreaceae sp. The extracellular agarase enzyme from Hypocreaceae sp. have optimum pH and temperature at 8 TrisHCl (0.148 µ.mL-1) and 50 °C (0.182 µ.mL-1), respectively. Agarase enzyme of Hypocreaceae sp. reach an optimum condition at the highest enzyme activity during incubation in 24 hours (0.323 µ.mL-1). SDS Page revealed that there are two bands of protein produced by agarase of Hypocreaceae sp. which are at molecular weight of 39 kDa and 44 kDa and hydrolisis of Gelidium latifolium obtained 0,88% ethanol. Key words: agarase enzym, Hypocreaceae sp., hydrolysis, marine fungi, rDNA
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6

Raut, Avinash A., and Shyam S. Bajekal. "An agar degrading diazotrophic actinobacteria from hyperalkaline meteoric lonar crater lake - a primary study." Microbiology Research 2, no. 1 (September 15, 2011): 10. http://dx.doi.org/10.4081/mr.2011.e10.

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There are very few reports on agarases being produced by actinobacteria, Streptomyces coelicolor being the only one known since decades for its agar degrading property. Here we report an agar degrading diazotrophic actinobacterium other than Streptomyces coelicolor, isolated from the littoral soil of Lonar Lake situated in Buldhana district of Maharashtra, India, a lake characterised by high alkalinity, carbonates, bicarbonates, and algal blooms. The lake has a mean diameter of 1800 meters. The Gram-positive filamentous rod grew in a simple medium of pH 10.5 containing agar as a sole source of carbon. The agar degrading property was detected by the appearance of depressions around each colony after 48 h of growth. The enzyme responsible for this degradation, agarase was also detected and estimated. The isolate also grew on Ashby’s Nitrogen free Mannitol Medium aerobically and fixed nitrogen. Morphological, physiological and biochemical characteristics of the isolate are presented in this paper.
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7

Wang, Wenxin, Jianxin Wang, Ruihua Yan, Runying Zeng, Yaqiang Zuo, Dingquan Wang, and Wu Qu. "Expression and Characterization of a Novel Cold-Adapted and Stable β-Agarase Gene agaW1540 from the Deep-Sea Bacterium Shewanella sp. WPAGA9." Marine Drugs 19, no. 8 (July 29, 2021): 431. http://dx.doi.org/10.3390/md19080431.

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The neoagaro-oligosaccharides, degraded from agarose by agarases, are important natural substances with many bioactivities. In this study, a novel agarase gene, agaW1540, from the genome of a deep-sea bacterium Shewanella sp. WPAGA9, was expressed, and the recombinant AgaW1540 (rAgaW1540) displayed the maximum activity under the optimal pH and temperature of 7.0 and 35 °C, respectively. rAgaW1540 retained 85.4% of its maximum activity at 0 °C and retained more than 92% of its maximum activity at the temperature range of 20–40 °C and the pH range of 4.0–9.0, respectively, indicating its extensive working temperature and pH values. The activity of rAgaW1540 was dramatically suppressed by Cu2+ and Zn2+, whereas Fe2+ displayed an intensification of enzymatic activity. The Km and Vmax of rAgaW1540 for agarose degradation were 15.7 mg/mL and 23.4 U/mg, respectively. rAgaW1540 retained 94.7%, 97.9%, and 42.4% of its maximum activity after incubation at 20 °C, 25 °C, and 30 °C for 60 min, respectively. Thin-layer chromatography and ion chromatography analyses verified that rAgaW1540 is an endo-acting β-agarase that degrades agarose into neoagarotetraose and neoagarohexaose as the main products. The wide variety of working conditions and stable activity at room temperatures make rAgaW1540an appropriate bio-tool for further industrial production of neoagaro-oligosaccharides.
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8

Xie, Zhangzhang, Weitie Lin, and Jianfei Luo. "Comparative Phenotype and Genome Analysis ofCellvibriosp. PR1, a Xylanolytic and Agarolytic Bacterium from the Pearl River." BioMed Research International 2017 (2017): 1–10. http://dx.doi.org/10.1155/2017/6304248.

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Cellvibriosp. PR1 is a xylanolytic and agarolytic bacterium isolated from the Pearl River. Strain PR1 is closely related toCellvibrio fibrivoransandC. ostraviensis(identity > 98%). The xylanase and agarase contents of strain PR1 reach up to 15.4 and 25.9 U/mL, respectively. The major cellular fatty acids consisted of C16:0 (36.7%), C18:0 (8.8%), C20:0 (6.8%), C15:0iso 2-OH or/and C16:1ω7c (17.4%), and C18:1ω7c or/and C18:1ω6c (6.7%). A total of 251 CAZyme modules (63 CBMs, 20 CEs, 128 GHs, 38 GTs, and 2 PLs) were identified from 3,730 predicted proteins. Genomic analysis suggested that strain PR1 has a complete xylan-hydrolyzing (5β-xylanases, 16β-xylosidases, 17α-arabinofuranosidases, 9 acetyl xylan esterases, 4α-glucuronidases, and 2 ferulic acid esterases) and agar-hydrolyzing enzyme system (2β-agarases and 2α-neoagarooligosaccharide hydrolases). In addition, the main metabolic pathways of xylose, arabinose, and galactose are established in the genome-wide analysis. This study shows that strain PR1 contains a large number of glycoside hydrolases.
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9

Ekborg, Nathan A., Larry E. Taylor, Atkinson G. Longmire, Bernard Henrissat, Ronald M. Weiner, and Steven W. Hutcheson. "Genomic and Proteomic Analyses of the Agarolytic System Expressed by Saccharophagus degradans 2-40." Applied and Environmental Microbiology 72, no. 5 (May 2006): 3396–405. http://dx.doi.org/10.1128/aem.72.5.3396-3405.2006.

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ABSTRACT Saccharophagus degradans 2-40 (formerly Microbulbifer degradans 2-40) is a marine gamma-subgroup proteobacterium capable of degrading many complex polysaccharides, such as agar. While several agarolytic systems have been characterized biochemically, the genetics of agarolytic systems have been only partially determined. By use of genomic, proteomic, and genetic approaches, the components of the S. degradans 2-40 agarolytic system were identified. Five agarases were identified in the S. degradans 2-40 genome. Aga50A and Aga50D include GH50 domains. Aga86C and Aga86E contain GH86 domains, whereas Aga16B carries a GH16 domain. Novel family 6 carbohydrate binding modules (CBM6) were identified in Aga16B and Aga86E. Aga86C has an amino-terminal acylation site, suggesting that it is surface associated. Aga16B, Aga86C, and Aga86E were detected by mass spectrometry in agarolytic fractions obtained from culture filtrates of agar-grown cells. Deletion analysis revealed that aga50A and aga86E were essential for the metabolism of agarose. Aga16B was shown to endolytically degrade agarose to release neoagarotetraose, similarly to a β-agarase I, whereas Aga86E was demonstrated to exolytically degrade agarose to form neoagarobiose. The agarolytic system of S. degradans 2-40 is thus predicted to be composed of a secreted endo-acting GH16-dependent depolymerase, a surface-associated GH50-dependent depolymerase, an exo-acting GH86-dependent agarase, and an α-neoagarobiose hydrolase to release galactose from agarose.
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10

Allouch, Julie, Murielle Jam, William Helbert, Tristan Barbeyron, Bernard Kloareg, Bernard Henrissat, and Mirjam Czjzek. "The Three-dimensional Structures of Two β-Agarases." Journal of Biological Chemistry 278, no. 47 (September 11, 2003): 47171–80. http://dx.doi.org/10.1074/jbc.m308313200.

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11

Naganuma, Takeshi, Daniel A. Coury, Miriam Polne-Fuller, Aharon Gibor, and Koki Horikoshi. "Characterization of Agarolytic Microscilla Isolates and their Extracellular Agarases." Systematic and Applied Microbiology 16, no. 2 (July 1993): 183–90. http://dx.doi.org/10.1016/s0723-2020(11)80466-2.

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12

Jahromi, Saeid Tamadoni, and Noora Barzkar. "Future direction in marine bacterial agarases for industrial applications." Applied Microbiology and Biotechnology 102, no. 16 (June 16, 2018): 6847–63. http://dx.doi.org/10.1007/s00253-018-9156-5.

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13

Li, Ren Kuan, Xi Juan Ying, Zhi Lin Chen, Tzi Bun Ng, Zhi Min Zhou, and Xiu Yun Ye. "Expression and Characterization of a GH16 Family β-Agarase Derived from the Marine Bacterium Microbulbifer sp. BN3 and Its Efficient Hydrolysis of Agar Using Raw Agar-Producing Red Seaweeds Gracilaria sjoestedtii and Gelidium amansii as Substrates." Catalysts 10, no. 8 (August 5, 2020): 885. http://dx.doi.org/10.3390/catal10080885.

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Agarases catalyze the hydrolysis of agarose to oligosaccharides which display an array of biological and physiological functions with important industrial applications in health-related fields. In this study, the gene encoding agarase (Aga-ms-R) was cloned from Microbulbifer sp. BN3 strain. Sequence alignment indicated that Aga-ms-R belongs to the GH16 family and contains one active domain and two carbohydrate binding module (CBM) domains. The mature Aga-ms-R was expressed successfully by employing the Brevibacillus system. Purified rAga-ms-R was obtained with a specific activity of 100.75 U/mg. rAga-ms-R showed optimal activity at 50 °C and pH 7.0, and the enzyme activity was stable at 50 °C and also over the pH range of 5.0–9.0. After exposure of rAga-ms-R to 70 °C for 30 min, only partial enzyme activity remained. Thin layer chromatographic analysis of the enzymatic hydrolysate of agar obtained using rAga-ms-R disclosed that the hydrolysate comprised, in a long intermediate-stage of the hydrolysis reaction, mainly neoagarotetraose (NA4) and neoagarohexaose (NA6) but ultimately, predominantly neoagarotetraose and trace amounts of neoagarobiose (NA2). Hydrolysates of the raw red seaweeds Gracilaria sjoestedtii and Gelidium amansii, produced by incubation with rAga-ms-R, were mainly composed of neoagarotetraose. The results demonstrate the high efficiency of rAga-ms-R in producing neoagaraoligosaccharide under low-cost conditions.
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14

JAM, Murielle, Didier FLAMENT, Julie ALLOUCH, Philippe POTIN, Laurent THION, Bernard KLOAREG, Mirjam CZJZEK, William HELBERT, Gurvan MICHEL, and Tristan BARBEYRON. "The endo-β-agarases AgaA and AgaB from the marine bacterium Zobellia galactanivorans: two paralogue enzymes with different molecular organizations and catalytic behaviours." Biochemical Journal 385, no. 3 (January 24, 2005): 703–13. http://dx.doi.org/10.1042/bj20041044.

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Two β-agarase genes, agaA and agaB, were functionally cloned from the marine bacterium Zobellia galactanivorans. The agaA and agaB genes encode proteins of 539 and 353 amino acids respectively, with theoretical masses of 60 and 40 kDa. These two β-agarases feature homologous catalytic domains belonging to family GH-16. However, AgaA displays a modular architecture, consisting of the catalytic domain (AgaAc) and two C-terminal domains of unknown function which are processed during secretion of the enzyme. In contrast, AgaB is composed of the catalytic module and a signal peptide similar to the N-terminal signature of prokaryotic lipoproteins, suggesting that this protein is anchored in the cytoplasmic membrane. Gel filtration and electrospray MS experiments demonstrate that AgaB is a dimer in solution, while AgaAc is a monomeric protein. AgaAc and AgaB were overexpressed in Escherichia coli and purified to homogeneity. Both enzymes cleave the β-(1→4) linkages of agarose in a random manner and with retention of the anomeric configuration. Although they behave similarly towards liquid agarose, AgaAc is more efficient than AgaB in the degradation of agarose gels. Given these organizational and catalytic differences, we propose that, reminiscent of the agarolytic system of Pseudoalteromonas atlantica, AgaA is specialized in the initial attack on solid-phase agarose, while AgaB is involved with the degradation of agarose fragments.
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15

Yang, Meng, Xiangzhao Mao, Nan Liu, Yongqian Qiu, and Changhu Xue. "Purification and characterization of two agarases from Agarivorans albus OAY02." Process Biochemistry 49, no. 5 (May 2014): 905–12. http://dx.doi.org/10.1016/j.procbio.2014.02.015.

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16

Aoki, Takahiko, Toshiyoshi Araki, and Manabu Kitamikado. "Purification and characterization of .BETA.-agarases from Vibrio sp. AP-2." NIPPON SUISAN GAKKAISHI 56, no. 5 (1990): 825–30. http://dx.doi.org/10.2331/suisan.56.825.

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17

Lee, Dong-Geun, and Sang-Hyeon Lee. "The Classification, Origin, Collection, Determination of Activity, Purification, Production, and Application of Agarases." Journal of Life Science 22, no. 2 (February 28, 2012): 266–80. http://dx.doi.org/10.5352/jls.2012.22.2.266.

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18

WU, Shao-Chi, and Chorng-Liang PAN. "Preparation of algal-oligosaccharide mixtures by bacterial agarases and their antioxidative properties." Fisheries Science 70, no. 6 (December 2004): 1164–73. http://dx.doi.org/10.1111/j.1444-2906.2004.00919.x.

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19

Michel, Gurvan, Pi Nyval-Collen, Tristan Barbeyron, Mirjam Czjzek, and William Helbert. "Bioconversion of red seaweed galactans: a focus on bacterial agarases and carrageenases." Applied Microbiology and Biotechnology 71, no. 1 (June 2006): 23–33. http://dx.doi.org/10.1007/s00253-006-0377-7.

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20

Kim, Hee Taek, Soo Rin Kim, Hee Jin Lee, Sae Young Lee, Kyoung Heon Kim, and In-Geol Choi. "Overexpression and characterization of recombinant agarases from Saccharophagus degradans strains 2–40." Journal of Biotechnology 136 (October 2008): S589. http://dx.doi.org/10.1016/j.jbiotec.2008.07.1188.

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21

Lemoine, Maud, and William Helbert. "Dégradation enzymatique en phase hétérogène des polysaccharides : exemple des agarases et des carraghénases." Journal de la Société de Biologie 201, no. 3 (2007): 291–96. http://dx.doi.org/10.1051/jbio:2007027.

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22

Fu, Wandong, Baoqin Han, Delin Duan, Wanshun Liu, and Changhong Wang. "Purification and characterization of agarases from a marine bacterium Vibrio sp. F-6." Journal of Industrial Microbiology & Biotechnology 35, no. 8 (May 14, 2008): 915–22. http://dx.doi.org/10.1007/s10295-008-0365-2.

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23

WU, Shao-Chi, Tuan-Nan WEN, and Chorng-Liang PAN. "Algal-oligosaccharide-lysates prepared by two bacterial agarases stepwise hydrolyzed and their anti-oxidative properties." Fisheries Science 71, no. 5 (October 2005): 1149–59. http://dx.doi.org/10.1111/j.1444-2906.2005.01075.x.

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Chen, Yu-Pei, Hong-Tan Wu, Guey-Horng Wang, Dai-Ying Wu, Ing-Er Hwang, Mei-Chih Chien, Hai-Yue Pang, Jong-Tar Kuo, and Li-Ling Liaw. "Inspecting the genome sequence and agarases of Microbulbifer pacificus LD25 from a saltwater hot spring." Journal of Bioscience and Bioengineering 127, no. 4 (April 2019): 403–10. http://dx.doi.org/10.1016/j.jbiosc.2018.10.001.

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25

FATURRAHMAN, FATURRAHMAN. "Isolation and identification of an agar, liquefying marine bacterium and some properties of its extracellular agarases." Biodiversitas, Journal of Biological Diversity 12, no. 4 (October 1, 2011): 192–97. http://dx.doi.org/10.13057/biodiv/d120402.

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Sugano, Yasushi, Hideki Nagae, Koji Inagaki, Takeshi Yamamoto, Ichiro Terada, and Yoshinari Yamazaki. "Production and characteristics of some new β-agarases from a marine bacterium, Vibrio sp. strain JT0107." Journal of Fermentation and Bioengineering 79, no. 6 (January 1995): 549–54. http://dx.doi.org/10.1016/0922-338x(95)94746-e.

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27

Chi, Won-Jae, Ju Won Seo, and Soon-Kwang Hong. "Characterization of Two Thermostable β-agarases from a Newly Isolated Marine Agarolytic Bacterium, Vibrio sp. S1." Biotechnology and Bioprocess Engineering 24, no. 5 (September 2019): 799–809. http://dx.doi.org/10.1007/s12257-019-0180-9.

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28

Czjzek, M., F. Thomas, E. Rebuffet, J. H. Hehemann, M. Jam, G. Correc, T. Barbeyron, and G. Michel. "Structural determinants for the specific recognition of algal cell wall polysaccharides: examples of agarases and alginate lyases." Acta Crystallographica Section A Foundations of Crystallography 68, a1 (August 7, 2012): s39. http://dx.doi.org/10.1107/s0108767312099254.

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29

Koti, Basawaraj A., M. Lakshmikanth, S. Manohar, and J. Lalitha. "AQUEOUS TWO-PHASE EXTRACTION FOR THE PURIFICATION OF ALKALINE AGARASES FROM CULTURE EXTRACTS OFPseudomonas aeruginosaAG LSL-11." Preparative Biochemistry and Biotechnology 42, no. 4 (July 2012): 364–77. http://dx.doi.org/10.1080/10826068.2011.623210.

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Lakshmikanth, M., S. Manohar, J. Patnakar, P. Vaishampayan, Y. Shouche, and J. Lalitha. "Optimization of Culture Conditions for the Production of Extracellular Agarases from Newly Isolated Pseudomonas Aeruginosa AG LSL-11." World Journal of Microbiology and Biotechnology 22, no. 5 (March 16, 2006): 531–37. http://dx.doi.org/10.1007/s11274-005-9068-2.

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31

Henshaw, Joanna, Ami Horne-Bitschy, Alicia Lammerts van Bueren, Victoria A. Money, David N. Bolam, Mirjam Czjzek, Nathan A. Ekborg, et al. "Family 6 Carbohydrate Binding Modules in β-Agarases Display Exquisite Selectivity for the Non-reducing Termini of Agarose Chains." Journal of Biological Chemistry 281, no. 25 (April 6, 2006): 17099–107. http://dx.doi.org/10.1074/jbc.m600702200.

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Lee, Chan Hyoung, Hee Taek Kim, Eun Ju Yun, Ah Reum Lee, Sa Rang Kim, Jae-Han Kim, In-Geol Choi, and Kyoung Heon Kim. "A Novel Agarolytic β-Galactosidase Acts on Agarooligosaccharides for Complete Hydrolysis of Agarose into Monomers." Applied and Environmental Microbiology 80, no. 19 (July 18, 2014): 5965–73. http://dx.doi.org/10.1128/aem.01577-14.

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ABSTRACTMarine red macroalgae have emerged to be renewable biomass for the production of chemicals and biofuels, because carbohydrates that form the major component of red macroalgae can be hydrolyzed into fermentable sugars. The main carbohydrate in red algae is agarose, and it is composed ofd-galactose and 3,6-anhydro-l-galactose (AHG), which are alternately bonded by β1-4 and α1-3 linkages. In this study, a novel β-galactosidase that can act on agarooligosaccharides (AOSs) to release galactose was discovered in a marine bacterium (Vibriosp. strain EJY3); the enzyme is annotated asVibriosp. EJY3 agarolytic β-galactosidase (VejABG). Unlike thelacZ-encoded β-galactosidase fromEscherichia coli,VejABG does not hydrolyze common substrates like lactose and can act only on the galactose moiety at the nonreducing end of AOS. The optimum pH and temperature ofVejABG on an agarotriose substrate were 7 and 35°C, respectively. Its catalytic efficiency with agarotriose was also similar to that with agaropentaose or agaroheptaose. Since agarotriose lingers as the unreacted residual oligomer in the currently available saccharification system using β-agarases and acid prehydrolysis, the agarotriose-hydrolyzing capability of this novel β-galactosidase offers an enormous advantage in the saccharification of agarose or agar in red macroalgae for its use as a biomass feedstock for fermentable sugar production.
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Yang, Ji Hye, Sae Kwang Ku, IL Je Cho, Je Hyeon Lee, Chang-Su Na, and Sung Hwan Ki. "Neoagarooligosaccharide Protects against Hepatic Fibrosis via Inhibition of TGF-β/Smad Signaling Pathway." International Journal of Molecular Sciences 22, no. 4 (February 18, 2021): 2041. http://dx.doi.org/10.3390/ijms22042041.

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Hepatic fibrosis occurs when liver tissue becomes scarred from repetitive liver injury and inflammatory responses; it can progress to cirrhosis and eventually to hepatocellular carcinoma. Previously, we reported that neoagarooligosaccharides (NAOs), produced by the hydrolysis of agar by β-agarases, have hepatoprotective effects against acetaminophen overdose-induced acute liver injury. However, the effect of NAOs on chronic liver injury, including hepatic fibrosis, has not yet been elucidated. Therefore, we examined whether NAOs protect against fibrogenesis in vitro and in vivo. NAOs ameliorated PAI-1, α-SMA, CTGF and fibronectin protein expression and decreased mRNA levels of fibrogenic genes in TGF-β-treated LX-2 cells. Furthermore, downstream of TGF-β, the Smad signaling pathway was inhibited by NAOs in LX-2 cells. Treatment with NAOs diminished the severity of hepatic injury, as evidenced by reduction in serum alanine aminotransferase and aspartate aminotransferase levels, in carbon tetrachloride (CCl4)-induced liver fibrosis mouse models. Moreover, NAOs markedly blocked histopathological changes and collagen accumulation, as shown by H&E and Sirius red staining, respectively. Finally, NAOs antagonized the CCl4-induced upregulation of the protein and mRNA levels of fibrogenic genes in the liver. In conclusion, our findings suggest that NAOs may be a promising candidate for the prevention and treatment of chronic liver injury via inhibition of the TGF-β/Smad signaling pathway.
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Tropeano, Mauro, Susana Vázquez, Silvia Coria, Adrián Turjanski, Daniel Cicero, Andrés Bercovich, and Walter Mac Cormack. "Extracellular hydrolytic enzyme production by proteolytic bacteria from the Antarctic." Polish Polar Research 34, no. 3 (June 1, 2013): 253–67. http://dx.doi.org/10.2478/popore-2013-0014.

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AbstractCold−adapted marine bacteria producing extracellular hydrolytic enzymes are important for their industrial application and play a key role in degradation of particulate organic matter in their natural environment. In this work, members of a previously−obtained protease−producing bacterial collection isolated from different marine sources from Potter Cove (King George Island, South Shetlands) were taxonomically identified and screened for their ability to produce other economically relevant enzymes. Eighty−eight proteolytic bacterial isolates were grouped into 25 phylotypes based on their Amplified Ribosomal DNA Restriction Analysis profiles. The sequencing of the 16S rRNA genes from representative isolates of the phylotypes showed that the predominant culturable protease−producing bacteria belonged to the class Gammaproteobacteria and were affiliated to the genera Pseudomonas, Shewanella, Colwellia, and Pseudoalteromonas, the latter being the predominant group (64% of isolates). In addition, members of the classes Actinobacteria, Bacilli and Flavobacteria were found. Among the 88 isolates screened we detected producers of amylases (21), pectinases (67), cellulases (53), CM−cellulases (68), xylanases (55) and agarases (57). More than 85% of the isolates showed at least one of the extracellular enzymatic activities tested, with some of them producing up to six extracellular enzymes. Our results confirmed that using selective conditions to isolate producers of one extracellular enzyme activity increases the probability of recovering bacteria that will also produce additional extracellular enzymes. This finding establishes a starting point for future programs oriented to the prospecting for biomolecules in Antarctica.
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Jiang, Chengcheng, Zhen Liu, Jianan Sun, Changhu Xue, and Xiangzhao Mao. "A Novel Route for Agarooligosaccharide Production with the Neoagarooligosaccharide-Producing β-Agarase as Catalyst." Catalysts 10, no. 2 (February 10, 2020): 214. http://dx.doi.org/10.3390/catal10020214.

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Enzymes are catalysts with high specificity. Different compounds could be produced by different enzymes. In case of agaro-oligosaccharides, agarooligosaccharide (AOS) can be produced by α-agarase through cleaving the α-1,3-glycosidic linkages of agarose, while neoagarooligosaccharide (NAOS) can be produced by β-agarase through cleaving the β-1,4-glycosidic linkages of agarose. However, in this study, we showed that β-agarase could also be used to produce AOSs with high purity and yield. The feasibility of our route was confirmed by agarotriose (A3) and agaropentaose (A5) formation from agaroheptaose (A7) and agarononoses (A9) catalyzed by β-agarase. Agarose was firstly liquesced by citric acid into a mixture of AOSs. The AOSs mixture was further catalyzed by β-agarase. When using the neoagarotetraose-forming β-agarase AgWH50B, agarotriose could be produced with the yield of 48%. When using neoagarotetraose, neoagarohexaose-forming β-agarase DagA, both agarotriose and agaropentaose could be produced with the yield of 14% and 13%, respectively. Our method can be used to produce other value-added agaro-oligosaccharides from agarose by different agarolytic enzymes.
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Dong, Jinhua, Shinnosuke Hashikawa, Takafumi Konishi, Yutaka Tamaru, and Toshiyoshi Araki. "Cloning of the Novel Gene Encoding β-Agarase C from a Marine Bacterium, Vibrio sp. Strain PO-303, and Characterization of the Gene Product." Applied and Environmental Microbiology 72, no. 9 (September 2006): 6399–401. http://dx.doi.org/10.1128/aem.00935-06.

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ABSTRACT The β-agarase C gene (agaC) of a marine bacterium, Vibrio sp. strain PO-303, consisted of 1,437 bp encoding 478 amino acid residues. β-Agarase C was identified as the first β-agarase that cannot hydrolyze neoagarooctaose and smaller neoagarooligosaccharides and was assigned to a novel glycoside hydrolase family.
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Ziayoddin, M., Junna Lalitha, and Manohar Shinde. "Optimization of Agrase Production by Alkaline Pseudomonas aeruginosa ZSL-2 Using Taguchi Experimental Design." International Letters of Natural Sciences 17 (June 2014): 180–93. http://dx.doi.org/10.18052/www.scipress.com/ilns.17.180.

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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. One-Factor-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, NH4NO3 2 g L-1 and agar 3 g L-1. The L9 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 NH4NO3 > 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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Gu, Wen Xue, Yu Lin Chen, Hui Na Niu, Xiao Lu, Xiang Zhao Mao, Zong Jun Du, and Xin Li Liu. "Enhanced Activity of Intracellular Agarase from a Novel Marine Strain Agarivorans gilvus WH0801." Advanced Materials Research 554-556 (July 2012): 1227–32. http://dx.doi.org/10.4028/www.scientific.net/amr.554-556.1227.

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A marine bacterium strain Agarivorans gilvus WH0801 with the efficient agar degradation ability isolated from fresh seaweed samples of Weihai coast was found to be potential in producing agarase. We studied on the optimal medium composition and culture conditions of Agarivorans gilvus WH0801 by statistical methods in shake flasks. First, several more important factors influencing agarase activity were selected by Plackett-Burman design. They are agar concentration, yeast extract concentration and seed age. Then the optimum levels of these three variables were further determined using Box-Behnken design. The highest agarase activity is obtained in the medium consisting of 2.49 g L-1 agar and 0.88 g L-1 yeast extract when the seed age is 25.64 h. The levels of other factors are 1 g L-1 peptone, 0.01 g L-1 ironic citrate at initial pH 7.0 and 28 °C. The whole optimization strategy results in the activity of agarase reaches 1.158 U mL-1, which is about 6.2-fold increase compares with the control.
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Zhang, Wei-wei, and Li Sun. "Cloning, Characterization, and Molecular Application of a Beta-Agarase Gene from Vibrio sp. Strain V134." Applied and Environmental Microbiology 73, no. 9 (March 2, 2007): 2825–31. http://dx.doi.org/10.1128/aem.02872-06.

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ABSTRACT V134, a marine isolate of the Vibrio genus, was found to produce a new beta-agarase of the GH16 family. The relevant agarase gene agaV was cloned from V134 and conditionally expressed in Escherichia coli. Enzyme activity analysis revealed that the optimum temperature and pH for the purified recombinant agarase were around 40°C and 7.0. AgaV was demonstrated to be useful in two aspects: first, as an agarolytic enzyme, the purified recombinant AgaV could be employed in the recovery of DNA from agarose gels; second, as a secretion protein, AgaV was explored at the genetic level and used as a reporter in the construction of a secretion signal trap which proved to be a simple and efficient molecular tool for the selection of genes encoding secretion proteins from both gram-positive and gram-negative bacteria.
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40

Zhong, Zhenping, Aresa Toukdarian, Donald Helinski, Vic Knauf, Sean Sykes, Jane E. Wilkinson, Colleen O'Bryne, Terry Shea, Craig DeLoughery, and Ron Caspi. "Sequence Analysis of a 101-Kilobase Plasmid Required for Agar Degradation by a MicroscillaIsolate." Applied and Environmental Microbiology 67, no. 12 (December 1, 2001): 5771–79. http://dx.doi.org/10.1128/aem.67.12.5771-5779.2001.

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ABSTRACT An agar-degrading marine bacterium identified as aMicroscilla species was isolated from coastal California marine sediment. This organism harbored a single 101-kb circular DNA plasmid designated pSD15. The complete nucleotide sequence of pSD15 was obtained, and sequence analysis indicated a number of genes putatively encoding a variety of enzymes involved in polysaccharide utilization. The most striking feature was the occurrence of five putative agarase genes. Loss of the plasmid, which occurred at a surprisingly high frequency, was associated with loss of agarase activity, supporting the sequence analysis results.
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Negara, Bertoka Fajar SP, Mujizat Kawaroe Kawaroe, and Dwi Setyaningsih Setyaningsih. "IDENTIFIKASI POTENSI ENZIM AGARASE YANG DIHASILKAN OLEH KAPANG HASIL ISOLASI DARI Caulerpa sp." JURNAL ENGGANO 1, no. 1 (May 1, 2016): 1–7. http://dx.doi.org/10.31186/jenggano.1.1.1-7.

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Kapang adalah mikroorganisme yang dapat diisolasi dari beberapa sumber seperti sedimen, air, serasah, rumput laut dan masih banyak lagi. Kapang dapat menghasilkan enzim yang memiliki banyak fungsi dan keuntungan. Tujuan dari penelitian ini adalah untuk mengisolasi kapang dari sedimen, serasah, dan air yang berasal dari sekitar lingkungan Caulerpa sp. Dan mengidentifikasi potensi enzim agarase yang dihasilkan. Sebanyak 41 isolat berhasil diisolasi. 5 isolat memiliki aktivitas enzim yang potensial (A10, A11, A13, SUC 7 dan SEC 8). Isolat A13 adalah isolat terbaik karena memiliki aktivitas agarase tertinggi dan waktu pertumbuhan yang lebih cepat daripada yang lain.
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42

Schroeder, Declan C., Mohamed A. Jaffer, and Vernon E. Coyne. "Investigation of the role of a β(1–4) agarase produced by Pseudoalteromonas gracilis B9 in eliciting disease symptoms in the red alga Gracilaria gracilis." Microbiology 149, no. 10 (October 1, 2003): 2919–29. http://dx.doi.org/10.1099/mic.0.26513-0.

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Gracilaria species are an important source of agar. The South African Gracilaria industry has experienced a number of setbacks over the last decade in the form of complete or partial die-offs of the agarophyte growing in Saldanha Bay, which may be attributed to bacterial infection. Since a positive correlation was observed between the presence of agarolytic epiphytes and bacterial pathogenicity, we investigated the role of an agarase in the virulence mechanism employed by a bacterium that elicits disease in Gracilaria gracilis. The recombinant plasmid pDA1, isolated from a Pseudoalteromonas gracilis B9 genomic library, was responsible for the agarolytic activity exhibited by Escherichia coli transformants when grown on solid medium. A blast search of the GenBank database showed that an 873 bp ORF (aagA) located on pDA1 had 85 % identity to the β-agarase (dagA) from Pseudoalteromonas atlantica ATCC 19262T (or IAM 12927T) at the amino acid level. AagA was purified from the extracellular medium of an E. coli transformant harbouring pDA1 by using a combination of gel filtration and ion-exchange chromatography. AagA has an M r of 30 000 on SDS-PAGE. TLC of the digestion products of AagA showed that the enzyme cleaves the β-(1,4) linkages of agarose to yield predominately neoagarotetraose. Western hybridization confirmed that the cloned agarase was in fact the extracellular β-agarase of P. gracilis B9. The observed relationship between disease symptoms of G. gracilis and the agarolytic phenotype of P. gracilis B9 was confirmed. Transmission electron microscope examination of cross sections of both healthy G. gracilis and G. gracilis infected with P. gracilis, revealed a weakening of the cell structure in the latter plants. Immunogold-labelled antibodies localized the agarase in situ to the cell walls of bleached G. gracilis. Thus, the weakening observed in the cell structure of G. gracilis infected with P. gracilis can be attributed to degradation of the mucilaginous component of the cell wall of the bleached thalli.
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43

Bien, Thanh T. L. "Isolation of agarase-producing bacteria from seawater and examination of the enzyme activity." Journal of Agriculture and Development 19, no. 02 (April 29, 2020): 50–58. http://dx.doi.org/10.52997/jad.7.02.2020.

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This study aimed to isolate agarase-producing bacteria from seawater, and then determine activity of the agarase. Eight coastal surface seawater samples were collected from Ba Ria - Vung Tau province. Twenty-one bacterial strains that are capable of liquefying agar were isolated. These isolates produced disintegration zones around their colonies on agar plates with diameters ranging from 4.0 to 7.0 cm after an incubation period of 2 days at room temperature. Five bacterial strains (M1, M5, M7, M62B, and M71) that produced large halos on plates were identified belonging to Vibrio genus with identity > 96%. The crude enzyme activities of these strains ranged from 0.15 to 0.22 U/mL in reaction with agarose as substrate. Among isolated strains, the strain M71 showed the highest agarase activity, and was used to examine the degradation of seaweed. The hydrolysis of dried Gracilaria seaweed by the crude enzyme of M71 at concentration of 5% (v/v) released 915 μM/mL reducing sugar after a 24-h incubation period at 40oC.
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44

Kim, Byung-Chun, Haryoung Poo, Kang Hyun Lee, Mi Na Kim, Doo-Sang Park, Hyun Woo Oh, Jin Man Lee, and Kee-Sun Shin. "Simiduia areninigrae sp. nov., an agarolytic bacterium isolated from sea sand." International Journal of Systematic and Evolutionary Microbiology 62, Pt_4 (April 1, 2012): 906–11. http://dx.doi.org/10.1099/ijs.0.031153-0.

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During a study intended to screen for agar-degrading bacteria, strain M2-5T was isolated from black sand off the shore of Jeju Island, Republic of Korea. Strain M2-5T exhibited agarase activity; the β-agarase gene of the isolate had 62 % amino acid sequence identity to the β-agarase gene of Microbulbifer thermotolerans JAMB A94T. The isolate was closely related to members of the genus Simiduia but was clearly discernible from reported Simiduia species, based on a polyphasic analysis. Cells of strain M2-5T were Gram-negative, catalase- and oxidase-positive, motile rods. The DNA G+C content was 53.3 mol%. The predominant isoprenoid quinone was Q-8. The major cellular fatty acids were C17 : 1ω8c (25.9 %), summed feature 3 (iso-C15 : 0 2-OH and/or C16 : 1ω7c; 17.2 %) and C17 : 0 (15.0 %). Phylogenetic analysis using 16S rRNA gene sequences showed that strain M2-5T had 96.6 % gene sequence similarity to Simiduia agarivorans SA1T, the most closely related type strain of the genus Simiduia . These results suggest that strain M2-5T represents a novel species in the genus Simiduia , for which the name Simiduia areninigrae sp. nov. is proposed; the type strain is M2-5T ( = KCTC 23293T = NCAIM B 02424T).
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Cui, Xin, Yuechen Jiang, Liuyi Chang, Lei Meng, Junhong Yu, Chun Wang, and Xiaolu Jiang. "Heterologous expression of an agarase gene in Bacillus subtilis, and characterization of the agarase." International Journal of Biological Macromolecules 120 (December 2018): 657–64. http://dx.doi.org/10.1016/j.ijbiomac.2018.07.118.

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46

Lee, Sol-Ji, Da-Young Shin, Jae-Deog Kim, Dong-Geun Lee, and Sang-Hyeon Lee. "Characterization of α-agarase from Alteromonas sp. SH-1." KSBB Journal 31, no. 2 (June 30, 2016): 113–19. http://dx.doi.org/10.7841/ksbbj.2016.31.2.113.

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Jang, Min-Kyung, Ok-Hee Lee, Ki-Hwan Yoo, Dong-Geun Lee, and Sang-Hyeon Lee. "Secretory Overexpression of β-Agarase in Bacillus subtilis and Antibacterial Activity of Enzymatic Products." Journal of Life Science 17, no. 11 (November 30, 2007): 1601–4. http://dx.doi.org/10.5352/jls.2007.17.11.1601.

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48

Kim, Jae-Deog, Sol-Ji Lee, Jeong-Gwon Jo, Dong-Geun Lee, and Sang-Hyeon Lee. "Characterization of β-agarase from Isolated Simiduia sp. SH-4." Journal of Life Science 26, no. 4 (April 30, 2016): 453–59. http://dx.doi.org/10.5352/jls.2016.26.4.453.

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49

Lavín, Paris, Cristian Atala, Jorge Gallardo-Cerda, Marcelo Gonzalez-Aravena, Rodrigo De La Iglesia, Rómulo Oses, Cristian Torres-Díaz, Nicole Trefault, Marco A. Molina-Montenegro, and H. Dail Laughinghouse IV. "Isolation and characterization of an Antarctic Flavobacterium strain with agarase and alginate lyase activities." Polish Polar Research 37, no. 3 (September 1, 2016): 403–19. http://dx.doi.org/10.1515/popore-2016-0021.

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AbstractSeveral bacteria that are associated with macroalgae can use phycocolloids as a carbon source. Strain INACH002, isolated from decomposing Porphyra (Rhodophyta), in King George Island, Antarctica, was screened and characterized for the ability to produce agarase and alginate-lyase enzymatic activities. Our strain INACH002 was identified as a member of the genus Flavobacterium, closely related to Flavobacterium faecale, using 16S rRNA gene analysis. The INACH002 strain was characterized as psychrotrophic due to its optimal temperature (17ºC) and maximum temperature (20°C) of growth. Agarase and alginate-lyase displayed enzymatic activities within a range of 10°C to 50°C, with differences in the optimal temperature to hydrolyze agar (50°C), agarose (50°C) and alginate (30°C) during the first 30 min of activity. Strain Flavobacterium INACH002 is a promising Antarctic biotechnological resource; however, further research is required to illustrate the structural and functional bases of the enzymatic performance observed during the degradation of different substrates at different temperatures.
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Kim, Se Won, Chae-Hwan Hong, Na Kyong Yun, and Hyun-Jae Shin. "Production and Application of Recombinant Agarase." Journal of Marine Bioscience and Biotechnology 8, no. 1 (June 30, 2016): 1–9. http://dx.doi.org/10.15433/ksmb.2016.8.1.001.

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