scholarly journals A novel Bacillus sp. isolated from rotten seaweed: Identification and characterization alginate lyase it is produced

2019 ◽  
Vol 20 (4) ◽  
pp. 1166-1172
Author(s):  
DEWI SESWITA ZILDA ◽  
YULIYANTI YULIANTI ◽  
RIZKY FAUZIYAH SHOLIHAH ◽  
SUBARYONO SUBARYONO ◽  
YUSRO NURI FAWZYA ◽  
...  
Keyword(s):  
Ethylenediaminetetraacetic Acid ◽  
Alginate Lyase ◽  
Maximum Activity ◽  
Bacillus Species ◽  
Bacillus Sp ◽  
16S Rdna Sequence ◽  
Bacillus Tequilensis ◽  
Bacterium Strain ◽  
Alginate Lyases ◽  
Identification And Characterization

Abstract. Zilda DS, Yulianti Y, Sholihah RF, Subaryono S, Fawzya YN, Irianto HE.2019. A novel Bacillus sp. isolated from rotten seaweed: identification and characterization alginate lyase it is produced. Biodiversitas 20: 1166-1172. Alginate lyase has been known as potential biocatalyst not only for industrial but also medicinal application especially for the production of oligosaccharides which have distinct bioactivities. An alginate lyase, AlgT513, has been isolated from rotten seaweed bacterium strain T513 and characterized. The bacterium showed low similarity (95%) with Bacillus tequilensis strain 10b based on 16S rDNA sequence indicating that Alg07 may be a novel Bacillus species. The bacterium forms a clear zone on solid medium with 0.5% sodium alginate addition. The optimum temperature and pH were 50ºC and 8 respectively. AlgT513 maintained stability at board pHs of 4-9 and temperature of 45ºC. Metal ions Mg2+, Ca2+ and K+ increase the activity of the enzyme while Zn2+, Co2+ and Li+ strongly inhibit it. NaCl inhibits AlgT513 activity where most of the alginate lyases need it to reach maximum activity. AlgT513 is suggested as a serine metalloenzyme due to inhibition of ethylenediaminetetraacetic acid (EDTA) and phenylmethylsulfonyl fluoride (PMSF).

scholarly journals Isolation and characterization of mannanase, xylanase, and cellulase from marine bacteria Bacillus sp.

2017 ◽  
Vol 15 (1) ◽  
pp. 15-20 ◽  
Author(s):  
YOPI YOPI ◽  
APRIDAH CAMELIAWATI DJOHAN ◽  
NANIK RAHMANI ◽  
ALIFAH MAFATIKHUL JANNAH
Keyword(s):  
Marine Bacteria ◽  
Bacillus Sp ◽  
16S Rdna Sequence ◽  
16S Rdna Sequence Analysis ◽  
Isolation And Characterization ◽  
Bacillus Tequilensis ◽  
Optimum Ph ◽  
Tlc Analysis ◽  
Identification And Characterization

Yopi, Djohan AC, Rahmani N, Jannah AM. 2017. Isolation and characterization of mannanase, xylanase, and cellulase from marine bacteria Bacillus sp. Biofarmasi (Rumphius J Nat Prod Biochem) 15: 15-20. Isolation, identification, and characterization of mannanase, xylanase and cellulase producing indigenous marine bacteria have been conducted from total 20 isolates. Based on 16S rDNA sequence analysis, three potential isolates are obtained and identified as Bacillus subtilis (M8), Bacillus tequilensis (X4) and Bacillus cereus (C9). The potential strains M8, X4 and C9 can produce mannanase, xylanase and cellulase activities such as 9.5 U/mL; 0.36U/mL;0.56U/mL with optimum pH and temperature 6.0;50oC, 5.5;70oC and 8;50oC, respectively. Based on the TLC analysis, mannanase from M8 and xylanase from X4 has potential to hydrolyzed mannan and xylan for producing oligosaccharides with size around tri-hexasaccharides as a main product.

scholarly journals Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium Alteromonas portus HB161718T

Marine Drugs ◽  
2021 ◽  
Vol 19 (3) ◽  
pp. 155
Author(s):  
Huiqin Huang ◽  
Shuang Li ◽  
Shixiang Bao ◽  
Kunlian Mo ◽  
Dongmei Sun ◽  
...  
Keyword(s):  
Marine Bacterium ◽  
Reducing Power ◽  
Alginate Lyase ◽  
Maximum Activity ◽  
Ionization Mass ◽  
Cold Adapted ◽  
Guluronic Acid ◽  
Type Activity ◽  
Alginate Oligosaccharides ◽  
Alginate Lyases

The alginate lyases have unique advantages in the preparation of alginate oligosaccharides and processing of brown algae. Herein, a gene alg2951 encoding a PL7 family alginate lyase with exo/endo-type activity was cloned from a novel marine bacterium Alteromonas portus HB161718T and then expressed in Escherichia coli. The recombinant Alg2951 in the culture supernatant reached the activity of 63.6 U/mL, with a molecular weight of approximate 60 kDa. Alg2951 exhibited the maximum activity at 25 °C and pH 8.0, was relatively stable at temperatures lower than 30 °C, and showed a special preference to poly-guluronic acid (polyG) as well. Both NaCl and KCl had the most promotion effect on the enzyme activity of Alg2951 at 0.2 M, increasing by 21.6 and 19.1 times, respectively. The TCL (Thin Layer Chromatography) and ESI-MS (Electrospray Ionization Mass Spectrometry) analyses suggested that Alg2951 could catalyze the hydrolysis of sodium alginate to produce monosaccharides and trisaccharides. Furthermore, the enzymatic hydrolysates displayed good antioxidant activity by assays of the scavenging abilities towards radicals (hydroxyl and ABTS+) and the reducing power. Due to its cold-adapted and dual exo/endo-type properties, Alg2951 can be a potential enzymatic tool for industrial production.

Isolation, identification and in silico study of native cellulase producing bacteria

2019 ◽  
Vol 17 ◽  
Author(s):  
Farzane Kargar ◽  
Mojtaba Mortazavi ◽  
Mahmood Maleki ◽  
Masoud Torkzadeh Mahani ◽  
Younes Ghasemi ◽  
...  
Keyword(s):  
Growth Rate ◽  
Bacillus Cereus ◽  
16S Rdna ◽  
Enzyme Production ◽  
Rational Design ◽  
Cellulase Production ◽  
Bacillus Species ◽  
Bacillus Sp ◽  
Chain Polymer ◽  
Bacillus Toyonensis

Aims: The purpose of this study was to screen the bacteria producing cellulase enzymes and their bioinformatics studies. Background: Cellulose is a long-chain polymer of glucose that hydrolyzes by cellulases to glucose molecules. In order to design the new biotechnological applications, some strategies have been used as increasing the efficiency of enzyme production, generating cost-effective enzymes, producing stable enzymes and identification of new strains. Objective: On the other hand, some bacteria special features have made them suitable candidates for the identification of the new source of enzymes. In this regard, some native strains of bacteria were screened. Method: These bacteria were grown on a culture containing the liquid M9 media containing CMC to ensure the synthesis of cellulase. The formation of a clear area in the culture medium indicated decomposition of cellulose. In the following, the DNA of these bacteria were extracted and their 16S rDNA genes were amplified. Result: The results show that nine samples were able to synthesize cellulase. In following, these strains were identified using 16S rDNA. The results show that these screened bacteria belonged to the Bacillus sp., Alcaligenes sp., Alcaligenes sp., and Enterobacter sp.conclusionThe enzyme activity analysis shows that the Bacillus toyonensis, Bacillus sp. strain XA15-411 Bacillus cereus have produced the maximum yield of cellulases. However, these amounts of enzyme production in these samples are not proportional to their growth rate. As the bacterial growth chart within 4 consecutive days shows that the Alcaligenes sp. Bacillus cereus, Bacillus toyonensis, Bacillus sp. strain XA15-411 have a maximum growth rate. The study of the phylogenetic tree also shows that Bacillus species are more abundant in the production of cellulase enzyme. These bioinformatics analyses show that the Bacillus species have different evolutionary relationships and evolved in different evolutionary time. Other: However, for maximum cellulase production by this bacteria, some information as optimum temperature, optimum pH, carbon and nitrogen sources are needed for the ideal formulation of media composition. The cellulase production is closely controlled in microorganisms and the cellulase yields appear to depend on a variety of factors. However, the further studies are needed for cloning, purification and application of these new microbial cellulases in the different commercial fields as in food, detergent, and pharmaceutical, paper, textile industries and also various chemical industries. However, these novel enzymes can be further engineered through rational design or using random mutagenesis techniques.

scholarly journals Identification and characterization of a novel 2R,3R-Butanediol dehydrogenase from Bacillus sp. DL01

2021 ◽  
Vol 49 ◽  
pp. 56-63
Author(s):  
Mostafa Elmahmoudy ◽  
Nora Elfeky ◽  
Pu Zhongji ◽  
Yue Zhang ◽  
Yongming Bao
Keyword(s):  
Bacillus Sp ◽  
Identification And Characterization ◽  
Butanediol Dehydrogenase

scholarly journals Specificities and Synergistic Actions of Novel PL8 and PL7 Alginate Lyases from the Marine Fungus Paradendryphiella salina

2021 ◽  
Vol 7 (2) ◽  
pp. 80
Author(s):  
Bo Pilgaard ◽  
Marlene Vuillemin ◽  
Jesper Holck ◽  
Casper Wilkens ◽  
Anne S. Meyer
Keyword(s):  
Alginate Lyase ◽  
Marine Fungus ◽  
Brown Macroalgae ◽  
Polysaccharide Lyases ◽  
Alginate Lyases ◽  
Encoding Genes ◽  
Substrate Affinities ◽  
Alginate Degradation ◽  
Insight Into

Alginate is an anionic polysaccharide abundantly present in the cell walls of brown macroalgae. The enzymatic depolymerization is performed solely by alginate lyases (EC 4.2.2.x), categorized as polysaccharide lyases (PLs) belonging to 12 different PL families. Until now, the vast majority of the alginate lyases have been found in bacteria. We report here the first extensive characterization of four alginate lyases from a marine fungus, the ascomycete Paradendryphiella salina, a known saprophyte of seaweeds. We have identified four polysaccharide lyase encoding genes bioinformatically in P. salina, one PL8 (PsMan8A), and three PL7 alginate lyases (PsAlg7A, -B, and -C). PsMan8A was demonstrated to exert exo-action on polymannuronic acid, and no action on alginate, indicating that this enzyme is most likely an exo-acting polymannuronic acid specific lyase. This enzyme is the first alginate lyase assigned to PL8 and polymannuronic acid thus represents a new substrate specificity in this family. The PL7 lyases (PsAlg7A, -B, and -C) were found to be endo-acting alginate lyases with different activity optima, substrate affinities, and product profiles. PsAlg7A and PsMan8A showed a clear synergistic action for the complete depolymerization of polyM at pH 5. PsAlg7A depolymerized polyM to mainly DP5 and DP3 oligomers and PsMan8A to dimers and monosaccharides. PsAlg7B and PsAlg7C showed substrate affinities towards both polyM and polyG at pH 8, depolymerizing both substrates to DP9-DP2 oligomers. The findings elucidate how P. salina accomplishes alginate depolymerization and provide insight into an efficient synergistic cooperation that may provide a new foundation for enzyme selection for alginate degradation in seaweed bioprocessing.

Growth enhancement of black pepper (Piper nigrum) by a newly isolated Bacillus tequilensis NII-0943

Biologia ◽  
2011 ◽  
Vol 66 (5) ◽  
Author(s):  
Syed Dastager ◽  
C. Deepa ◽  
Ashok Pandey
Keyword(s):  
Sequence Similarity ◽  
Black Pepper ◽  
Piper Nigrum ◽  
Bacillus Species ◽  
Rrna Gene ◽  
Growth Enhancement ◽  
Nitrogen And Phosphorus ◽  
Bacillus Tequilensis ◽  
Plant Growth Promoting ◽  
The Western Ghats

AbstractA Gram positive, rod-shaped potential strain was selected from the pool of bacterial isolates obtained from the Western Ghats forest (India) on the basis of zone of P-solubilization activity. Identification based on 16S rRNA gene sequence revealed that the strain is of Bacillus species, sharing highest sequence similarity to Bacillus tequilensis NRRL B-41771T (99.5%). Strain NII-0943 was able to produce good amount of indole acetic acid (IAA) and was positive for siderophore production. In addition to IAA and siderophore attributes, strain NII-0943 also possessed the characteristics like Ca3(PO4)2 solubilization and growth in nitrogen-free medium. Seed inoculation with the strain NII-0943 resulted in significantly higher root initiation in black pepper cuttings grown under pots. The contents of nitrogen and phosphorus in both soil and plant were also enhanced significantly in treatments inoculated with these bacterial inocula. Hence, based on this evidence it is proposed that strain NII-0943 could be deployed as a plant growth-promoting inoculant to attain the desired results of bacterization.

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

Purification, Properties and Mass Spectrometry Analysis of Two Novel Thermotolerant Endoglucanases from Bacillus akibai I-2

2011 ◽  
Vol 393-395 ◽  
pp. 911-915
Author(s):  
Sen Lin Liu ◽  
Miao Xing
Keyword(s):  
Mass Spectrometry ◽  
Soda Lakes ◽  
Maximum Activity ◽  
Mass Spectrometry Analysis ◽  
16S Rrna Sequence ◽  
Spectrometry Analysis ◽  
16S Rrna Sequence Analysis ◽  
Bacterium Strain ◽  
Terminal Amino ◽  
Alkaliphilic Bacterium

The alkaliphilic bacterium strain Ⅰ-2, which was isolated from soda lakes, was identified as Bacillus akibai by 16S rRNA sequence analysis and suggested to be a new subspecies of genus Bacillus. Two novel thermotolerant alkaline endoglucanases Ⅰ-2-A and Ⅰ-2-B were produced by this alkaliphilic strain. The purified Ⅰ-2-A and Ⅰ-2-B had molecular mass of approximately 60 and 90 kDa, respectively. The optimum pH of Ⅰ-2-A was about 9.0, while that of Ⅰ-2-B was about 8.0. Both enzymes exhibited maximum activity at around 50 °C and were stable up to 50 °C.The two enzymes were resistant to most metal ions and reagents examined. Mass spectrometry analysis indicated that Ⅰ-2-A was probably different from the endoglucanases reported. Ⅰ-2-B showed homology with those of family A5 endoglucanases but low similarity was found in C-terminal amino acid sequence.

scholarly journals Structure Characteristics, Biochemical Properties, and Pharmaceutical Applications of Alginate Lyases

Marine Drugs ◽  
2021 ◽  
Vol 19 (11) ◽  
pp. 628
Author(s):  
Shu-Kun Gao ◽  
Rui Yin ◽  
Xiao-Chen Wang ◽  
Hui-Ning Jiang ◽  
Xiao-Xiao Liu ◽  
...  
Keyword(s):  
Brown Algae ◽  
Catalytic Mechanism ◽  
Degradation Products ◽  
Structural Characteristics ◽  
Catalytic Efficiency ◽  
Alginate Lyase ◽  
Biochemical Properties ◽  
Structure And Property ◽  
Alginate Oligosaccharides ◽  
Alginate Lyases

Alginate, the most abundant polysaccharides of brown algae, consists of various proportions of uronic acid epimers α-L-guluronic acid (G) and β-D-mannuronic acid (M). Alginate oligosaccharides (AOs), the degradation products of alginates, exhibit excellent bioactivities and a great potential for broad applications in pharmaceutical fields. Alginate lyases can degrade alginate to functional AOs with unsaturated bonds or monosaccharides, which can facilitate the biorefinery of brown algae. On account of the increasing applications of AOs and biorefinery of brown algae, there is a scientific need to explore the important aspects of alginate lyase, such as catalytic mechanism, structure, and property. This review covers fundamental aspects and recent developments in basic information, structural characteristics, the structure–substrate specificity or catalytic efficiency relationship, property, molecular modification, and applications. To meet the needs of biorefinery systems of a broad array of biochemical products, alginate lyases with special properties, such as salt-activated, wide pH adaptation range, and cold adaptation are outlined. Withal, various challenges in alginate lyase research are traced out, and future directions, specifically on the molecular biology part of alginate lyases, are delineated to further widen the horizon of these exceptional alginate lyases.

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