Literature DB >> 30333947

Recombinant β-agarases: insights into molecular, biochemical, and physiochemical characteristics.

Sneeha Veerakumar1, Ramesh Pathy Manian1.   

Abstract

Agarases (agarose 4-glycanohydrolase; EC 3.2.1.81) are class of enzymes that belong to glycoside hydrolase (GH) family capable of hydrolyzing agar. Their classification depends on hydrolysis pattern and product formation. Among all the agarases, β-agarases and the oligosaccharides formed by its action have fascinated quite a lot of industries. Ample of β-agarase genes have been endowed from marine sources such as algae, sea water, and marine sediments, and the expression of these genes into suitable host gives rise to recombinant β-agarases. These recombinant β-agarases have wide range of industrial applications due to its improved catalytic efficiency and stability in tough environments with ease of production on large scale. In this review, we have perused different types of recombinant β-agarases in consort with their molecular, physiochemical, and kinetic properties in detail and the significant features of those agarases are spotlighted. From the literature reviewed after 2010, we have found that the recombinant β-agarases belonged to the families GH16, GH39, GH50, GH86, and GH118. Among that, GH39, GH50, and GH86 belonged to clan GH-A, while the GH16 family belonged to clan GH-B. It was observed that GH16 is the largest polyspecific glycoside hydrolase family with ample number of β-agarases and the families GH50 and GH118 were found to be monospecific with only β-agarase activity. And, out of 84 non-catalytic carbohydrate-binding modules (CBMs), only CBM6 and CBM13 were professed in β-agarases. We witnessed a larger heterogeneity in molecular, physiochemical, and catalytic characteristics of the recombinant β-agarases including molecular mass: 32-132 kDa, optimum pH: 4.5-9, optimum temperature 16-60 °C, K M: 0.68-59.8 mg/ml, and V max: 0.781-11,400 U/mg. Owing to this extensive range of heterogeneity, they have lion's share in the multibillion dollar enzyme market. This review provides a holistic insight to a few aspects of recombinant β-agarases which can be referred by the upcoming explorers to this area.

Entities:  

Keywords:  Glycoside hydrolase; Kinetic properties; Molecular characteristics; Physiochemical properties; Recombinant β-agarases

Year:  2018        PMID: 30333947      PMCID: PMC6177356          DOI: 10.1007/s13205-018-1470-1

Source DB:  PubMed          Journal:  3 Biotech        ISSN: 2190-5738            Impact factor:   2.406


  55 in total

1.  Biochemical and structural characterization of the complex agarolytic enzyme system from the marine bacterium Zobellia galactanivorans.

Authors:  Jan-Hendrik Hehemann; Gaëlle Correc; François Thomas; Thomas Bernard; Tristan Barbeyron; Murielle Jam; William Helbert; Gurvan Michel; Mirjam Czjzek
Journal:  J Biol Chem       Date:  2012-07-09       Impact factor: 5.157

2.  Characterization and overexpression of a novel β-agarase from Thalassomonas agarivorans.

Authors:  S-S Liang; Y-P Chen; Y-H Chen; S-H Chiu; L-L Liaw
Journal:  J Appl Microbiol       Date:  2013-12-05       Impact factor: 3.772

3.  Cloning, expression, and biochemical characterization of a GH16 β-agarase AgaH71 from Pseudoalteromonas hodoensis H7.

Authors:  Da Yeon Park; Won-Jae Chi; Jae-Seon Park; Yong-Keun Chang; Soon-Kwang Hong
Journal:  Appl Biochem Biotechnol       Date:  2014-10-24       Impact factor: 2.926

4.  Overexpression and biochemical characterization of DagA from Streptomyces coelicolor A3(2): an endo-type β-agarase producing neoagarotetraose and neoagarohexaose.

Authors:  Uyangaa Temuujin; Won-Jae Chi; Soon-Youl Lee; Yong-Keun Chang; Soon-Kwang Hong
Journal:  Appl Microbiol Biotechnol       Date:  2011-06-08       Impact factor: 4.813

5.  Gene cloning, expression and characterisation of a new β-agarase, AgWH50C, producing neoagarobiose from Agarivorans gilvus WH0801.

Authors:  Nan Liu; Xiangzhao Mao; Meng Yang; Bozhong Mu; Dongzhi Wei
Journal:  World J Microbiol Biotechnol       Date:  2014-01-07       Impact factor: 3.312

6.  Expression and Characterization of a Novel Thermostable and pH-Stable β-Agarase from Deep-Sea Bacterium Flammeovirga Sp. OC4.

Authors:  Xing-Lin Chen; Yan-Ping Hou; Min Jin; Run-Ying Zeng; He-Tong Lin
Journal:  J Agric Food Chem       Date:  2016-09-19       Impact factor: 5.279

7.  Genomic and proteomic analyses of the agarolytic system expressed by Saccharophagus degradans 2-40.

Authors:  Nathan A Ekborg; Larry E Taylor; Atkinson G Longmire; Bernard Henrissat; Ronald M Weiner; Steven W Hutcheson
Journal:  Appl Environ Microbiol       Date:  2006-05       Impact factor: 4.792

8.  Identification and biochemical characterization of Sco3487 from Streptomyces coelicolor A3(2), an exo- and endo-type β-agarase-producing neoagarobiose.

Authors:  Uyangaa Temuujin; Won-Jae Chi; Yong-Keun Chang; Soon-Kwang Hong
Journal:  J Bacteriol       Date:  2011-10-21       Impact factor: 3.490

9.  Overexpression and molecular characterization of Aga50D from Saccharophagus degradans 2-40: an exo-type beta-agarase producing neoagarobiose.

Authors:  Hee Taek Kim; Saeyoung Lee; Dongho Lee; Hyun-Soo Kim; Won-Gi Bang; Kyoung Heon Kim; In-Geol Choi
Journal:  Appl Microbiol Biotechnol       Date:  2009-10-03       Impact factor: 4.813

10.  Purification and characterization of a new agarase from a marine bacterium, Vibrio sp. strain JT0107.

Authors:  Y Sugano; I Terada; M Arita; M Noma; T Matsumoto
Journal:  Appl Environ Microbiol       Date:  1993-05       Impact factor: 4.792

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  3 in total

1.  The structure of PfGH50B, an agarase from the marine bacterium Pseudoalteromonas fuliginea PS47.

Authors:  Benjamin Pluvinage; Craig S Robb; Roderick Jeffries; Alisdair B Boraston
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2020-08-19       Impact factor: 1.056

2.  Overexpression and characterization of a novel GH16 β-agarase (Aga1) from Cellulophaga omnivescoria W5C.

Authors:  Kristine Rose M Ramos; Kris Niño G Valdehuesa; Angelo B Bañares; Grace M Nisola; Won-Keun Lee; Wook-Jin Chung
Journal:  Biotechnol Lett       Date:  2020-06-09       Impact factor: 2.461

3.  Characterization of Agarolytic Pathway in a Terrestrial Bacterium Cohnella sp. LGH.

Authors:  Gen Li; Rui Guo; Shuqi Wu; Si Cheng; Jiaqi Li; Zhenzhen Liu; Wangliang Xie; Xiaolin Sun; Qiuyi Zhang; Zihan Li; JiaZheng Xu; Jun Wu; Zhong Wei; Feng Hu
Journal:  Front Microbiol       Date:  2022-03-31       Impact factor: 5.640

  3 in total

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