scholarly journals Purification and Characterization of A New Cold-Adapted and Thermo-Tolerant Chitosanase from Marine Bacterium Pseudoalteromonas sp. SY39

Molecules ◽  
2019 ◽  
Vol 24 (1) ◽  
pp. 183 ◽  
Author(s):  
Yu Zhou ◽  
Xuehong Chen ◽  
Xiao Li ◽  
Yantao Han ◽  
Yanan Wang ◽  
...  
Keyword(s):  
Enzymatic Degradation ◽  
Marine Bacterium ◽  
Degradation Products ◽  
Biological Activities ◽  
Apparent Molecular Weight ◽  
Maximal Activity ◽  
Purification And Characterization ◽  
Cold Adapted ◽  
Total Product

Chitosanases play an important role in chitosan degradation, forming enzymatic degradation products with several biological activities. Although many chitosanases have been discovered and studied, the enzymes with special characteristics are still rather rare. In this study, a new chitosanase, CsnM, with an apparent molecular weight of 28 kDa was purified from the marine bacterium Pseudoalteromonas sp. SY39. CsnM is a cold-adapted enzyme, which shows highest activity at 40 °C and exhibits 30.6% and 49.4% of its maximal activity at 10 and 15 °C, respectively. CsnM is also a thermo-tolerant enzyme that recovers 95.2%, 89.1% and 88.1% of its initial activity after boiling for 5, 10 and 20 min, respectively. Additionally, CsnM is an endo-type chitosanase that yields chitodisaccharide as the main product (69.9% of the total product). It’s cold-adaptation, thermo-tolerance and high chitodisaccharide yield make CsnM a superior candidate for biotechnological application to produce chitooligosaccharides.

scholarly journals Functional Characterization of a New GH107 Endo-α-(1,4)-Fucoidanase from the Marine Bacterium Formosa haliotis

Marine Drugs ◽  
2020 ◽  
Vol 18 (11) ◽  
pp. 562
Author(s):  
Marlene Vuillemin ◽  
Artem S. Silchenko ◽  
Hang Thi Thuy Cao ◽  
Maxim S. Kokoulin ◽  
Vo Thi Dieu Trang ◽  
...  
Keyword(s):  
Marine Bacterium ◽  
Divalent Cations ◽  
Recombinant Expression ◽  
Biological Activities ◽  
Functional Characterization ◽  
Maximal Activity ◽  
Brown Macroalgae ◽  
Pharmaceutical Uses ◽  
Enzymatic Depolymerization

Fucoidans from brown macroalgae are sulfated fucose-rich polysaccharides, that have several beneficial biological activities, including anti-inflammatory and anti-tumor effects. Controlled enzymatic depolymerization of the fucoidan backbone can help produce homogeneous, defined fucoidan products for structure-function research and pharmaceutical uses. However, only a few endo-fucoidanases have been described. This article reports the genome-based discovery, recombinant expression in Escherichia coli, stabilization, and functional characterization of a new bacterial endo-α-(1,4)-fucoidanase, Fhf1, from Formosa haliotis. Fhf1 catalyzes the cleavage of α-(1,4)-glycosidic linkages in fucoidans built of alternating α-(1,3)-/α-(1,4)-linked l-fucopyranosyl sulfated at C2. The native Fhf1 is 1120 amino acids long and belongs to glycoside hydrolase (GH) family 107. Deletion of the signal peptide and a 470 amino acid long C-terminal stretch led to the recombinant expression of a robust, minimized enzyme, Fhf1Δ470 (71 kDa). Fhf1Δ470 has optimal activity at pH 8, 37–40 °C, can tolerate up to 500 mM NaCl, and requires the presence of divalent cations, either Ca2+, Mn2+, Zn2+ or Ni2+, for maximal activity. This new enzyme has the potential to serve the need for controlled enzymatic fucoidan depolymerization to produce bioactive sulfated fucoidan oligomers.

scholarly journals Cloning, Expression, and Characterization of a New PL25 Family Ulvan Lyase from Marine Bacterium Alteromonas sp. A321

Marine Drugs ◽  
2019 ◽  
Vol 17 (10) ◽  
pp. 568 ◽  
Author(s):  
Jian Gao ◽  
Chunying Du ◽  
Yongzhou Chi ◽  
Siqi Zuo ◽  
Han Ye ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Amino Acid ◽  
Marine Bacterium ◽  
Apparent Molecular Weight ◽  
Maximal Activity ◽  
Amino Acid Residues ◽  
Polysaccharide Lyase ◽  
Sequence Identity

Ulvan lyases can degrade ulvan to oligosaccharides with potent biological activity. A new ulvan lyase gene, ALT3695, was identified in Alteromonas sp. A321. Soluble expression of ALT3695 was achieved in Escherichia coli BL21 (DE3). The 1314-bp gene encoded a protein with 437 amino acid residues. The amino acid sequence of ALT3695 exhibited low sequence identity with polysaccharide lyase family 25 (PL25) ulvan lyases from Pseudoalteromonas sp. PLSV (64.14% identity), Alteromonas sp. LOR (62.68% identity), and Nonlabens ulvanivorans PLR (57.37% identity). Recombinant ALT3695 was purified and the apparent molecular weight was about 53 kDa, which is different from that of other polysaccharide-degrading enzymes identified in Alteromonas sp. A321. ALT3695 exhibited maximal activity in 50 mM Tris-HCl buffer at pH 8.0 and 50 °C. ALT3695 was relatively thermostable, as 90% activity was observed after incubation at 40 °C for 3 h. The Km and Vmax values of ALT3695 towards ulvan were 0.43 mg·mL−1 and 0.11 μmol·min−1·mL−1, respectively. ESI-MS analysis showed that enzymatic products were mainly disaccharides and tetrasaccharides. This study reports a new PL25 family ulvan lyase, ALT3695, with properties that suggest its great potential for the preparation of ulvan oligosaccharides.

scholarly journals Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01

Marine Drugs ◽  
2019 ◽  
Vol 17 (3) ◽  
pp. 185 ◽  
Author(s):  
Yangtao Fang ◽  
Suxiao Yang ◽  
Xiaodan Fu ◽  
Wancui Xie ◽  
Li Li ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Marine Bacterium ◽  
Specific Activity ◽  
Degradation Products ◽  
Purification And Characterization ◽  
Promising Candidate ◽  
Functional Activities ◽  
Action Mode ◽  
Low Degrees

Chondroitinase (ChSase), a type of glycosaminoglycan (GAG) lyase, can degrade chondroitin sulfate (CS) to unsaturate oligosaccharides, with various functional activities. In this study, ChSase AC II from a newly isolated marine bacterium Arthrobacter sp. CS01 was cloned, expressed in Pichia pastoris X33, purified, and characterized. ChSase AC II, with a molecular weight of approximately 100 kDa and a specific activity of 18.7 U/mg, showed the highest activity at 37 °C and pH 6.5 and maintained stability at a broad range of pH (5–7.5) and temperature (below 35 °C). The enzyme activity was increased in the presence of Mn2+ and was strongly inhibited by Hg2+. Moreover, the kinetic parameters of ChSase AC II against CS-A, CS-C, and HA were determined. TLC and ESI-MS analysis of the degradation products indicated that ChSase AC II displayed an exolytic action mode and completely hydrolyzed three substrates into oligosaccharides with low degrees of polymerization (DPs). All these features make ChSase AC II a promising candidate for the full use of GAG to produce oligosaccharides.

scholarly journals Cloning and Characterization of a Cold-adapted Chitosanase from Marine Bacterium Bacillus sp. BY01

Molecules ◽  
2019 ◽  
Vol 24 (21) ◽  
pp. 3915 ◽  
Author(s):  
Yue Yang ◽  
Zhou Zheng ◽  
Yifei Xiao ◽  
Jiaojiao Zhang ◽  
Yu Zhou ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Marine Bacterium ◽  
Volume Concentration ◽  
Biological Activities ◽  
Maximum Activity ◽  
Bacillus Sp ◽  
Cold Adapted ◽  
Encoding Gene ◽  
Bacterium Bacillus

Chitosanase plays an important role in the production of chitooligosaccharides (CHOS), which possess various biological activities. Herein, a glycoside hydrolase (GH) family 46 chitosanase-encoding gene, csnB, was cloned from marine bacterium Bacillus sp. BY01 and heterologously expressed in Escherichia coli. The recombinant chitosanase, CsnB, was optimally active at 35 °C and pH 5.0. It was also revealed to be a cold-adapted enzyme, maintaining 39.5% and 40.4% of its maximum activity at 0 and 10 °C, respectively. Meanwhile, CsnB showed wide pH-stability within the range of pH 3.0 to 7.0. Then, an improved reaction condition was built to enhance its thermostability with a final glycerol volume concentration of 20%. Moreover, CsnB was determined to be an endo-type chitosanase, yielding chitosan disaccharides and trisaccharides as the main products. Overall, CsnB provides a new choice for enzymatic CHOS production.

scholarly journals Purification and Characterization of a Novel Alginate Lyase from the Marine Bacterium Bacillus sp. Alg07

Marine Drugs ◽  
2018 ◽  
Vol 16 (3) ◽  
pp. 86 ◽  
Author(s):  
Peng Chen ◽  
Yueming Zhu ◽  
Yan Men ◽  
Yan Zeng ◽  
Yuanxia Sun
Keyword(s):  
Marine Bacterium ◽  
Alginate Lyase ◽  
Bacillus Sp ◽  
Purification And Characterization ◽  
Bacterium Bacillus

scholarly journals Partial purification and characterization of xylanase from Bacillus cereus X3

2014 ◽  
Vol 11 (2) ◽  
pp. 1056-1061
Author(s):  
Baghdad Science Journal
Keyword(s):  
Bacillus Cereus ◽  
Maximal Activity ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Xylanase Production ◽  
Optimum Activity ◽  
Biology Department ◽  
Characterization Study ◽  
Quantitative Screening

Three strain of Bacillus cereus were obtained from soil sours Laboratories of Biology Department/ College of Science/ University of Baghdad. The bacteria secreted extracellular xylanase in liquid cultur the test ability of xylanase production from these isolates was studied semi quantitative and quantitative screening appeared that Bacillus cereus X3 was the highest xylanase producer. The enzyme was partial purification 191 fold from cultur by reached step by 4 U/mg proteins by ammonium sulfat precipitation 80%, Ion exchang DEAE-cellulos chromatography Characterization study of the partial purifation enzyme revealed that the enzyme had a optimum activity pH8 and activity was stable in the pH rang (8-10) for 30min. maximal activity was attained at 50C

scholarly journals Purification and Characterization of a Biofilm-Degradable Dextranase from a Marine Bacterium

Marine Drugs ◽  
2018 ◽  
Vol 16 (2) ◽  
pp. 51 ◽  
Author(s):  
Wei Ren ◽  
Ruanhong Cai ◽  
Wanli Yan ◽  
Mingsheng Lyu ◽  
Yaowei Fang ◽  
...  
Keyword(s):  
Marine Bacterium ◽  
Purification And Characterization
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