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Relevant bibliographies by topics / Agarase

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Journal articles

Academic literature on the topic 'Agarase'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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Journal articles on the topic "Agarase"

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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