Purification and partial characterization of an extracellular alginate lyase from Aspergillus oryzae isolated from brown seaweed

Singh, Ravindra; Gupta, Vishal; Kumari, Puja; Kumar, Manoj; Reddy, C. R. K.; Prasad, Kamalesh; Jha, Bhavanath

doi:10.1007/s10811-010-9576-9

Cited by 31 publications

(22 citation statements)

References 37 publications

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“…A double bond is then formed between nonreducing ends, namely C4 and C5, where the glycosidic bond is located, and an oligomeric oligosaccharide with a 4‐deoxy‐L‐erythro‐hex‐4‐enepyranosyluronate structure is simultaneously produced (Wong, Preston, & Schiller, ). Alginate lyases can be obtained from various sources, such as marine and terrestrial bacteria (Yu, Zhu, Wang, Tan, & Yin, ; Zhu, Ni, Sun, & Yao, ), fungus (Cao et al, ; Singh et al, ), virus (Ichiro et al, ), marine mollusks (Hata et al, ; Rahman, Inoue, Tanaka, & Ojima, ), and algae (Inoue et al, ). They can be classified into two groups, namely, polyG specific (polyG lyase, EC 4.2.2.11) and polyM specific (polyM lyase, EC 4.2.2.3), because of their different effects on substrates (Zhu & Yin, ).…”

Section: Introductionmentioning

confidence: 99%

Cloning, expression, and characterization of a new pH‐ and heat‐stable alginate lyase from Pseudoalteromonas carrageenovora ASY5

et al. 2019

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Alginate lyase is important in marine alginate degradation, and its enzymatic hydrolysates are excellent antioxidants. Here, we cloned a new alginate lyase, that is, Alg823, from the Gram‐negative marine bacterium Pseudoalteromonas carrageenovora ASY5. The optimal temperature and pH of Alg823 were 55°C and pH 8.0, respectively. After 30 min of incubation at 50°C, Alg823 could maintain over 75.0% of the maximum enzyme activity, suggesting its thermostability. The recombinant alginate lyase retained more than 80.0% of the maximum enzyme activity after it was treated at pH 6.0–10.0 and 4°C for 24 hr, indicating its excellent pH stability. Mg2+, Ca2+, Na+, and K+ could promote enzyme activity. Alginate oligosaccharides obtained by degradation with Alg823 displayed an excellent ability to scavenge ABTS, hydroxyl, and DPPH radicals. Alg823 showed potential for novel applications in alginate oligosaccharide production because of its pH tolerance and heat adaptation. Practical applications Alginate oligosaccharides produced by alginate degradation possess favorable properties, such as low molecular weight, high stability, and co‐dissolution with water. These oligosaccharides also have many biological activities. As such, they have been widely explored. Alginate oligosaccharides are prepared via three methods, namely, physical, chemical, and enzymatic methods. In chemical method, operational processes are difficult to thereby possibly damaging the unique structure of polysaccharides and causing environmental pollution. Although physical methods can overcome some of the shortcomings of chemical methods, their reaction is still difficult to control, and products are complicated. Conversely, enzymatic methods can has advantages of mild conditions, single product, and less pollution. Furthermore, oligosaccharides prepared by enzymatic methods are more biologically active than those prepared by other methods. Thus, finding novel alginate lyase with high activity and stability is important for research and commercial purposes.

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Section: Introductionmentioning

confidence: 99%

Cloning, expression, and characterization of a new pH‐ and heat‐stable alginate lyase from Pseudoalteromonas carrageenovora ASY5

et al. 2019

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“…The alginate lyases found in Pseudoalteromonas sp. SM0524 , Aspergillus oryzae , and Vibrio sp. YKW‐34 were preferable to hydrolyze poly (M) than poly (G).…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of a high salt‐tolerant alginate lyase from Cobetia sp. WG‐007

Gong

Liu

Zhang

et al. 2017

Biotech and App Biochem

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An alginate lyase producing bacterial strain, Cobetia sp. WG-007, was isolated and identified from rotting seaweed. The alginate lyase, Aly-W02, was purified by procedures of ultrafiltration, Q-Sepharose Fast Flow, Phenyl Sepharose 6 Fast Flow, and Superdex-G100 with specific activity of 21,285.5 U/mg. Aly-W02 had an apparent molecular mass of 35 kDa. It exhibited maximum activity at 45 °C in 50 mM sodium phosphate buffer (pH 8.5). This alginate lyase was stable in the pH range of 6.0-8.5. Among the tested metal ions, the addition of K , Na , and Mg ions can enhance the enzyme activities, while Ba , Ni , Cu , Mn , Zn , Ag , and ethylenediaminetetraacetic acid decreased the activities. It displayed high salt-tolerant ability; 0.8 M NaCl or 1.5 M KCl significantly enhanced the enzyme activity. Furthermore, Aly-W02 mainly released disaccharide, trisaccharide, and tetrasaccharid from alginate. It showed potential in producing low molecular weight alginate oligosaccharides.

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“…The K m and V max values of the purified enzyme were found to be 1.07 mg alginate/ml and 128.2 U/mg protein. K m and V max values of alginate lyase from Aspergillus oryzae were 21.52 mg/ml and 222.68 U/mg proteins, respectively [21]. Several reports indicated that the optimum activity of alginate lyase was obtained between pH 7.0 and 8.0 from, Streptomyces species A5, and Microbulbifer sp.…”

Section: Discussionmentioning

confidence: 98%

“…Alginate lyase from Pseudomonas stutzeri MSEA04 can be considered more thermostable than the alginate lyase produced from Escherichia coli, which lost 50% of its activity after 10 min at 45 °C [14], and alginate lyase obtained from Aspergillus oryzae which lost completely its activity at 50 °C [21]. However, it was still considered to be less stable than the alginate lyase obtained from Bacillus species which retained 60% and 50% of its activity after treatment for 30 min at 20 °C and 60 °C, respectively [15].…”

Section: Discussionmentioning

confidence: 99%

“…The specific activity of the fractions from Sephadex-G100 column reached 116 U/mg. Purification of partially purified alginate lyase from Streptomyces species A5 and Aspergillus oryzae have been studied using DEAECellulose column and Sephadex G-100 column and the purified enzyme showed a specific activity of 101.6 U/mg and 67.24 U/mg, respectively [3,21]. In addition, purification of alginate lyase from Vibrio sp.…”

Section: Discussionmentioning

confidence: 99%

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Purification and characterization of alginate lyase from locally isolated marinePseudomonas stutzeriMSEA04

Beltagy

El-Borai

Lewiz

et al. 2016

Acta Biologica Hungarica

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An alginate lyase with high specific enzyme activity was purified from Pseudomonas stutzeri MSEA04, isolated from marine brown algae. The alginate lyase was purified by precipitation with ammonium sulphate, acetone and ethanol individually. 70% ethanol fraction showed maximum specific activity (133.3 U/mg). This fraction was re-purified by anion exchange chromatography DEAE-Cellulose A-52. The loaded protein was separated into 3 peaks. The second protein peak was the major one which contained 48.2% of the total protein recovered and 79.4% of the total recovered activity. The collected fractions of this peak were subjected to further purification by re-chromatography on Sephadex G-100. Alginate lyase activity was fractionated in the Sephadex column into one major peak, and the specific activity of this fraction reached 116 U/mg. The optimal substrate concentration, pH and temperature for alginate lyase activity were 8 mg/ml, pH 7.5 and 37 °C, respectively. While, K m and V max values were 1.07 mg alginate/ ml and 128.2 U/mg protein, respectively. The enzyme was partially stable below 50 °C, and the activity of the enzyme was strongly enhanced by K + , and strongly inhibited by Ba +2 , Cd +2 , Fe +2 and Zn +2 . The purified enzyme yielded a single band on SDS-PAGE with molecular weight (40.0 kDa).

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Purification and partial characterization of an extracellular alginate lyase from Aspergillus oryzae isolated from brown seaweed

Cited by 31 publications

References 37 publications

Cloning, expression, and characterization of a new pH‐ and heat‐stable alginate lyase from Pseudoalteromonas carrageenovora ASY5

Cloning, expression, and characterization of a new pH‐ and heat‐stable alginate lyase from Pseudoalteromonas carrageenovora ASY5

Purification and characterization of a high salt‐tolerant alginate lyase from Cobetia sp. WG‐007

Purification and characterization of alginate lyase from locally isolated marinePseudomonas stutzeriMSEA04

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