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Journal articles on the topic 'Agarase'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

Han, Wenjun, Yuanyuan Cheng, Dandan Wang та ін. "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, № 16 (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 uniq

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2

Jiang, Chengcheng, Zhen Liu, Jianan Sun, Changhu Xue та Xiangzhao Mao. "A Novel Route for Agarooligosaccharide Production with the Neoagarooligosaccharide-Producing β-Agarase as Catalyst". Catalysts 10, № 2 (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 agarohe

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3

Wang, Wenxin, Jianxin Wang, Ruihua Yan та ін. "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, № 8 (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 extensi

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4

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 (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 domain

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5

Flament, Didier, Tristan Barbeyron, Murielle Jam, et al. "Alpha-Agarases Define a New Family of Glycoside Hydrolases, Distinct from Beta-Agarase Families." Applied and Environmental Microbiology 73, no. 14 (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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6

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 (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

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7

Han, Zhang та Yang. "Biochemical Characterization of a New β-Agarase from Cellulophaga Algicola". International Journal of Molecular Sciences 20, № 9 (2019): 2143. http://dx.doi.org/10.3390/ijms20092143.

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Cellulophaga algicola DSM 14237, isolated from the Eastern Antarctic coastal zone, was found to be able to hydrolyze several types of polysaccharide materials. In this study, a predicted β-agarase (CaAga1) from C. algicola was heterologously expressed in Escherichia coli. The purified recombinant CaAga1 showed specific activities of 29.39, 20.20, 14.12, and 8.99 U/mg toward agarose, pure agar, and crude agars from Gracilaria lemaneiformis and Porphyra haitanensis, respectively. CaAga1 exhibited an optimal temperature and pH of 40 oC and 7, respectively. CaAga1 was stable over a wide pH range f

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8

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 (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

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9

Liao, Li, Xue-Wei Xu, Xia-Wei Jiang та ін. "Cloning, Expression, and Characterization of a New β-Agarase fromVibriosp. Strain CN41". Applied and Environmental Microbiology 77, № 19 (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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10

Burmeister, Margit, and Hans Lehrach. "Isolation of large DNA fragments from agarose gels using agarase." Trends in Genetics 5 (1989): 41. http://dx.doi.org/10.1016/0168-9525(89)90019-x.

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11

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 (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 ide

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12

Rochas, Cyrille, Philippe Potin та Bernard Kloareg. "NMR spectroscopic investigation of agarose oligomers produced by an α-agarase". Carbohydrate Research 253 (лютий 1994): 69–77. http://dx.doi.org/10.1016/0008-6215(94)80056-1.

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13

Rochas, C. "NMR spectroscopic investigation of agarose oligomers produced by an α-agarase". Carbohydrate Research 237, № 1 (1992): 69–77. http://dx.doi.org/10.1016/0008-6215(92)84234-j.

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14

JAM, Murielle, Didier FLAMENT, Julie ALLOUCH та ін. "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, № 3 (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

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15

Schroeder, Declan C., Mohamed A. Jaffer та 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, № 10 (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 gr

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16

Achudhan, Arunmozhi Bharathi, та Mahalakshmi Velrajan. "MOLECULAR CHARACTERIZATION OF β-AGARASE PRODUCED BY SPHINGOMONAS PAUCIMOBILIS, A MARINE BACTERIUM". Bacterial Empire 4, № 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 infrare

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17

Dong, Jinhua, Shinnosuke Hashikawa, Takafumi Konishi, Yutaka Tamaru та 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, № 9 (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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18

Lavín, Paris, Cristian Atala, Jorge Gallardo-Cerda, et al. "Isolation and characterization of an Antarctic Flavobacterium strain with agarase and alginate lyase activities." Polish Polar Research 37, no. 3 (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. Agar

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19

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

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20

Sambrook, Joseph, and David W. Russell. "Recovery of DNA from Low-melting-temperature Agarose Gels: Enzymatic Digestion with Agarase." Cold Spring Harbor Protocols 2006, no. 1 (2006): pdb.prot4026. http://dx.doi.org/10.1101/pdb.prot4026.

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21

Cui, Xin, Yuechen Jiang, Liuyi Chang, et al. "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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22

Gu, Wen Xue, Yu Lin Chen, Hui Na Niu, et al. "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-Behnk

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23

Cole, Kenneth D., and Björn Åkerman. "Enhanced Capacity for Electrophoretic Capture of Plasmid DNA by Agarase Treatment of Agarose Gels." Biomacromolecules 1, no. 4 (2000): 771–81. http://dx.doi.org/10.1021/bm005594c.

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24

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 (2016): 1–9. http://dx.doi.org/10.15433/ksmb.2016.8.1.001.

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25

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

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26

Han, Wen-Jun, Jing-Yan Gu, Hui-Hui Liu, Fu-Chuan Li, Zhi-Hong Wu та Yue-Zhong Li. "An Extra Peptide within the Catalytic Module of a β-Agarase Affects the Agarose Degradation Pattern". Journal of Biological Chemistry 288, № 13 (2013): 9519–31. http://dx.doi.org/10.1074/jbc.m112.412247.

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27

Koti, Basawaraj A., Manohar Shinde, and J. Lalitha. "Repeated batch production of agar-oligosaccharides from agarose by an amberlite IRA-900 immobilized agarase system." Biotechnology and Bioprocess Engineering 18, no. 2 (2013): 333–41. http://dx.doi.org/10.1007/s12257-012-0237-5.

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28

Pluvinage, Benjamin, Craig S. Robb, Roderick Jeffries, and Alisdair B. Boraston. "The structure of PfGH50B, an agarase from the marine bacterium Pseudoalteromonas fuliginea PS47." Acta Crystallographica Section F Structural Biology Communications 76, no. 9 (2020): 422–27. http://dx.doi.org/10.1107/s2053230x20010328.

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The recently identified marine bacterium Pseudoalteromonas fuliginea sp. PS47 possesses a polysaccharide-utilization locus dedicated to agarose degradation. In particular, it contains a gene (locus tag EU509_06755) encoding a β-agarase that belongs to glycoside hydrolase family 50 (GH50), PfGH50B. The 2.0 Å resolution X-ray crystal structure of PfGH50B reveals a rare complex multidomain fold that was found in two of the three previously determined GH50 structures. The structure comprises an N-terminal domain with a carbohydrate-binding module (CBM)-like fold fused to a C-terminal domain by a r

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29

Li, Ren Kuan, Xi Juan Ying, Zhi Lin Chen, Tzi Bun Ng, Zhi Min Zhou та 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, № 8 (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/m

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30

Zhong, Zhenping, Aresa Toukdarian, Donald Helinski, et al. "Sequence Analysis of a 101-Kilobase Plasmid Required for Agar Degradation by a MicroscillaIsolate." Applied and Environmental Microbiology 67, no. 12 (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, supportin

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31

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 (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 agaras

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

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33

Zhang, Lei, Xiaofang Guo, Yangyang Song, et al. "Bioadhesive immobilize agarase on magnetic ferriferous by polydopamine." Materials Science and Engineering: C 93 (December 2018): 218–25. http://dx.doi.org/10.1016/j.msec.2018.07.068.

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34

NOMURA, Kazuyo, Yukari NAITOH, Satsuki MURAMATSU та ін. "New Sulfated Oligosaccharides Produced byPseudomonasβ-Agarase fromGracilaria verrucosaPolysaccharide". Bioscience, Biotechnology, and Biochemistry 62, № 6 (1998): 1190–95. http://dx.doi.org/10.1271/bbb.62.1190.

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35

Parro, Victor, and Rafael P. Mellado. "Effect of glucose on agarase overproduction by Streptomyces." Gene 145, no. 1 (1994): 49–55. http://dx.doi.org/10.1016/0378-1119(94)90321-2.

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36

Kim, Byung-Chun, Haryoung Poo, Kang Hyun Lee, et al. "Simiduia areninigrae sp. nov., an agarolytic bacterium isolated from sea sand." International Journal of Systematic and Evolutionary Microbiology 62, Pt_4 (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

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37

Allouch, Julie, William Helbert, Bernard Henrissat та Mirjam Czjzek. "Parallel Substrate Binding Sites in a β-Agarase Suggest a Novel Mode of Action on Double-Helical Agarose". Structure 12, № 4 (2004): 623–32. http://dx.doi.org/10.1016/j.str.2004.02.020.

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38

Kim, Jung Hyun, Eun Ju Yun, Nari Seo та ін. "Enzymatic liquefaction of agarose above the sol–gel transition temperature using a thermostable endo-type β-agarase, Aga16B". Applied Microbiology and Biotechnology 101, № 3 (2016): 1111–20. http://dx.doi.org/10.1007/s00253-016-7831-y.

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39

Lee, Joo-Young, Dae-Geun Song, Jin-Ki Son, and Cheol-Ho Pan. "Effect of Agarase Signal Peptide from Agarivorans albus YKW-34 on Protein Secretion in Escherichia coli." Journal of Applied Biological Chemistry 53, no. 2 (2010): 105–7. http://dx.doi.org/10.3839/jabc.2010.019.

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40

Ohta, Yukari, Yuji Hatada, Yuichi Nogi, et al. "Thermostable .BETA.-Agarase from a Deep-sea Microbulbifer Isolate." Journal of Applied Glycoscience 51, no. 3 (2004): 203–10. http://dx.doi.org/10.5458/jag.51.203.

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41

Parro, Vı́ctor, Carme Vives, Francesc Godia, and Rafael P. Mellado. "Overproduction and purification of an agarase of bacterial origin." Journal of Biotechnology 58, no. 1 (1997): 59–66. http://dx.doi.org/10.1016/s0168-1656(97)00128-4.

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42

Yamaura, Izumi, Toshihiko Matsumoto, Masaru Funatsu, Hisaji Shigeiri, and Teruhiko Shibata. "Purification and Some Properties of Agarase fromPseudomonassp. PT-5." Agricultural and Biological Chemistry 55, no. 10 (1991): 2531–36. http://dx.doi.org/10.1080/00021369.1991.10871002.

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43

Parro, Victor, Rafael P. Mellado, and Colin R. Harwood. "Effects of phosphate limitation on agarase production byStreptomyces lividansTK21." FEMS Microbiology Letters 158, no. 1 (1998): 107–13. http://dx.doi.org/10.1111/j.1574-6968.1998.tb12808.x.

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Bannikova, G. E., S. A. Lopatin, V. P. Varlamov, et al. "The thermophilic bacteria hydrolyzing agar: Characterization of thermostable agarase." Applied Biochemistry and Microbiology 44, no. 4 (2008): 366–71. http://dx.doi.org/10.1134/s0003683808040054.

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Mei, Jianfeng, Zhongxiu Tang, Yu Yi, Hong Wang, Qi Wang та Guoqing Ying. "Purification and characterization of β-agarase from Paenibacillus sp." Food Science and Biotechnology 23, № 5 (2014): 1605–9. http://dx.doi.org/10.1007/s10068-014-0218-x.

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Lin, Bokun, Yandan Zheng, Jingxiao Huang, Junkang Shang, Yuli Yu, and Zhong Hu. "A new neoagarobiose-producing agarase from Vibrio sp. LA1." ScienceAsia 47, no. 4 (2021): 403. http://dx.doi.org/10.2306/scienceasia1513-1874.2021.045.

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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 (2011): 10. http://dx.doi.org/10.4081/mr.2011.e10.

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Abstract:

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

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

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Shi, X., M. Yu, S. Yan, S. Dong, and X. H. Zhang. "Genome Sequence of the Thermostable-Agarase-Producing Marine Bacterium Catenovulum agarivorans YM01T, Which Reveals the Presence of a Series of Agarase-Encoding Genes." Journal of Bacteriology 194, no. 19 (2012): 5484. http://dx.doi.org/10.1128/jb.01283-12.

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Jo, Jeong-Gwon, Sol-Ji Lee, Dong-Geun Lee, and Sang-Hyeon Lee. "Characterization of Agarase Produced from the Isolated Marine Bacterium Marinomonas sp. SH-2." Journal of Life Science 26, no. 2 (2016): 198–203. http://dx.doi.org/10.5352/jls.2016.26.2.198.

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