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Article ; Online: Identification of a Novel Thermostable Alkaline Protease from Bacillus megaterium -TK1 for the Detergent and Leather Industry

Tamilvendan Manavalan / Arulmani Manavalan / Shiyamsundar Ramachandran / Klaus Heese

Biology, Vol 9, Iss 472, p

2020 Volume 472

Abstract: An increased need by the green industry for enzymes that can be exploited for eco-friendly industrial applications led us to isolate and identify a unique protease obtained from a proteolytic Bacillus megaterium -TK1 strain from a seawater source. The ... ...

Abstract	An increased need by the green industry for enzymes that can be exploited for eco-friendly industrial applications led us to isolate and identify a unique protease obtained from a proteolytic Bacillus megaterium -TK1 strain from a seawater source. The extracellular thermostable serine protease was processed by multiple chromatography steps. The isolated protease displayed a relative molecular weight (MW) of 33 kDa (confirmed by zymography), optimal enzyme performance at pH 8.0, and maximum enzyme performance at 70 °C with 100% substrate specificity towards casein. The proteolytic action was blocked by phenylmethylsulfonyl fluoride (PMSF), a serine hydrolase inactivator. Protease performance was augmented by several bivalent metal cations. The protease tolerance was studied under stringent conditions with different industrial dispersants and found to be stable with Surf Excel, Tide, or Rin detergents. Moreover, this protease could clean blood-stained fabrics and showed dehairing activity for cow skin with significantly reduced pollution loads. Our results suggest that this serine protease is a promising additive for various eco-friendly usages in both the detergent and leather industries.
Keywords	Bacillus megaterium ; detergent ; hydrolase ; protease ; thermostable ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2020-12-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Immunomodulatory zymosan/ι-carrageenan/ agarose hydrogel for targeting M2 to M1 macrophages (antitumoral).

Venkatachalam, Geetha / Giri, Jayant / Mallik, Saurav / Arumugam, Gandarvakottai Senthilkumar / Arulmani, Manavalan / Dewangan, Vimal Kumar / Doble, Mukesh / Zhao, Zhongming

RSC advances

2024 Volume 14, Issue 17, Page(s) 11694–11705

Abstract: Several studies have been performed on the immunomodulatory effects of yeast β-(1,3) glucan, but there is no proper evaluation of the thermal and immunomodulating properties of zymosan (ZM). Thermogravimetry analysis indicated a 54% weight loss of ZM at ... ...

Abstract	Several studies have been performed on the immunomodulatory effects of yeast β-(1,3) glucan, but there is no proper evaluation of the thermal and immunomodulating properties of zymosan (ZM). Thermogravimetry analysis indicated a 54% weight loss of ZM at 270 °C. Circular dichroism showed absorption peaks in the region of 250 to 400 nm, suggesting a helical coil β-sheet configuration. XRD showed a broad peak at 2
Language	English
Publishing date	2024-04-11
Publishing country	England
Document type	Journal Article
ISSN	2046-2069
ISSN (online)	2046-2069
DOI	10.1039/d3ra06978h
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Article ; Online: Compound Analysis of Jing Liqueur and nrf2 Activation by Jing Liqueur—One of the Most Popular Beverages in China

You-Sheng Cai / Jian Xu / Mosi Chen / Daoqing Wang / Yuejun Yang / Arulmani Manavalan / Xiaohua Wu / Yuancai Liu / Shugeng Cao

Beverages, Vol 6, Iss 1, p

2019 Volume 1

Abstract: The aim of this study is to identify the minor compounds in Jing liqueur, determine the concentration of metals, amino acids, and polysaccharides, and evaluate their Nrf2 activity and cytotoxicity. Jing liqueur that contains Chinese medicine is one of ... ...

Abstract	The aim of this study is to identify the minor compounds in Jing liqueur, determine the concentration of metals, amino acids, and polysaccharides, and evaluate their Nrf2 activity and cytotoxicity. Jing liqueur that contains Chinese medicine is one of the best-selling liqueurs in China, which is also marketed in the United States. Totally, we have isolated 189 minor compounds including one new molecule ( 7 ) from a concentrated Jing liqueur, with the concentrations of most isolated compounds at micromolar levels. The structures of all these compounds were determined by using MS and NMR (1D and 2D) or by comparison of their chemical and physical data with reported values in the literatures. Besides, the concentrations of iron (0.52 mg/L), zinc (0.21 mg/L), calcium (11.0 mg/L), L -proline (2.33 mg/L), L -arginine (1.73 mg/L), total amino acids (9.84 mg/L), and total polysaccharides (337.4 mg/L) were determined. Jing liqueur, the five fractions and most of the compounds isolated from Jing liqueur were screened for their activities in the Nrf2-ARE and MTT assays. At 5.2 mg/mL the crude enhanced the Nrf2 activity. At 80 μg/mL, fraction IV weakly but fraction V strongly activated Nrf2. Among the compounds screened in the Nrf2 assay, eighteen activated Nrf2 at 40 μg/mL and compounds 51 and 126 from fraction V were the most active. The crude, all the five fractions, and Nrf2 activators were not cytotoxic toward HepG2 cells. In conclusion, Jing liqueur contains different classes of compounds including flavonoids, terpenoids, alkaloids, coumarins, cinnamic acid or coumaric acid, and phenyl ethanol (or acetic acid) derivatives, benzoquinone, naphthoquinone, anthraquinones or phenanphrene derivatives, xanthones, chromone, and γ-pyrone derivatives, lignans, other aromatic compounds, and others. Jing liqueur and the eighteen compounds, which were isolated from Jing liqueur, could activate Nrf2 without any cytotoxicity.
Keywords	jing liqueur ; traditional chinese medicine ; compounds ; nmr ; ms ; nrf2-are ; Nutrition. Foods and food supply ; TX341-641 ; Nutritional diseases. Deficiency diseases ; RC620-627
Subject code	540
Language	English
Publishing date	2019-12-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Identification of Anti-Inflammatory Compounds from Hawaiian Noni ( Morinda citrifolia L.) Fruit Juice

Dahae Lee / Jae Sik Yu / Peng Huang / Mallique Qader / Arulmani Manavalan / Xiaohua Wu / Jin-Chul Kim / Changhyun Pang / Shugeng Cao / Ki Sung Kang / Ki Hyun Kim

Molecules, Vol 25, Iss 4968, p

2020 Volume 4968

Abstract: Noni ( Morinda citrifolia L.) fruit juice has been used in Polynesia as a traditional folk medicine and is very popular worldwide as a functional food supplement. In this study, compounds present in Hawaiian Noni fruit juice, with anti-inflammatory ... ...

Abstract	Noni ( Morinda citrifolia L.) fruit juice has been used in Polynesia as a traditional folk medicine and is very popular worldwide as a functional food supplement. In this study, compounds present in Hawaiian Noni fruit juice, with anti-inflammatory activity in lipopolysaccharide (LPS)-stimulated RAW 264.7 cells were identified. Five compounds were isolated using a bioassay-driven technique and phytochemical analysis of noni fruit juice: asperulosidic acid ( 1 ), rutin ( 2 ), nonioside A ( 3 ), (2 E ,4 E ,7 Z )-deca-2,4,7-trienoate-2- O -β- d -glucopyranosyl-β- d -glucopyranoside ( 4 ), and tricetin ( 5 ). The structures of these five compounds were determined via NMR spectroscopy and LC/MS. In an anti-inflammatory assay, compounds 1 – 5 inhibited the production of nitric oxide (NO), which is a proinflammatory mediator, in LPS-stimulated macrophages. Moreover, the mechanisms underlying the anti-inflammatory effects of compounds 1 – 5 were investigated. Parallel to the inhibition of NO production, treatment with compounds 1 – 5 downregulated the expression of IKKα/β, I-κBα, and NF-κB p65 in LPS-stimulated macrophages. Furthermore, treatment with compounds 1 – 5 downregulated the expression of nitric oxide synthase and cyclooxygenase-2. Thus, these data demonstrated that compounds 1 – 5 present in noni fruit juice, exhibited potential anti-inflammatory activity; these active compounds may contribute preventively and therapeutically against inflammatory diseases.
Keywords	noni ; Morinda citrifolia ; anti-inflammation ; NO production ; RAW 264.7 cells ; Organic chemistry ; QD241-441
Language	English
Publishing date	2020-10-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Hidden Twins: SorCS Neuroreceptors Form Stable Dimers

Januliene, Dovile / Anders NykjÃ¦r / Arne Moeller / Arulmani Manavalan / Karen-Marie Pedersen / Peter Lund Ovesen / SÃ¸ren Thirup

Journal of Molecular Biology. 2017 Sept. 15, v. 429

2017

Abstract: SorCS1, SorCS2 and SorCS3 belong to the Vps10p-domain family of multiligand receptors. Genetic and functional studies have linked SorCS receptors to psychiatric disorders, Alzheimer's disease and type 2 diabetes, demonstrating critical roles in neuronal ... ...

Abstract	SorCS1, SorCS2 and SorCS3 belong to the Vps10p-domain family of multiligand receptors. Genetic and functional studies have linked SorCS receptors to psychiatric disorders, Alzheimer's disease and type 2 diabetes, demonstrating critical roles in neuronal functionality and metabolic control. Surprisingly, their structural composition has so far not been studied. Here we have characterized SorCS1, SorCS2 and SorCS3 using biochemical methods and electron microscopy. We found that their purified extracellular domains co-exist in stable dimeric and monomeric populations. This was supported by co-immunoprecipitation experiments, where membrane-bound dimers were successfully pulled down from cell lysate. While dimers were virtually unbreakable, dimerization of the monomeric population was promoted through enzymatic deglycosylation. We conclude that post-translational modifications, specifically the degree and pattern of glycosylation, regulate the oligomeric state of the protein. Hence, cells may dictate ligand specificity by controlling the ratio between monomers and dimers and, therefore, regulate the multiple functions of SorCS receptors.
Keywords	Alzheimer disease ; behavior disorders ; dimerization ; electron microscopy ; glycosylation ; ligands ; neurons ; noninsulin-dependent diabetes mellitus ; precipitin tests ; receptors ; twins
Language	English
Dates of publication	2017-0915
Size	p. 2907-2917.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2017.08.006
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Article ; Online: Quantitative iTRAQ secretome analysis of cellulolytic Thermobifida fusca.

Adav, Sunil S / Ng, Chee Sheng / Arulmani, Manavalan / Sze, Siu Kwan

Journal of proteome research

2010 Volume 9, Issue 6, Page(s) 3016–3024

Abstract: Thermobifida fusca, a thermophilic bacterium belonging to Actinobacteria, is a major degrader of plant cell walls. The protein profiles of the secretome produced by T. fusca grown in cellulose, lignin, and mixture of cellulose and lignin containing ... ...

Abstract	Thermobifida fusca, a thermophilic bacterium belonging to Actinobacteria, is a major degrader of plant cell walls. The protein profiles of the secretome produced by T. fusca grown in cellulose, lignin, and mixture of cellulose and lignin containing culture media, promoting production of respective substrate hydrolyzing enzymes, was explored using a proteomics approach with high throughput isobaric tag for relative and absolute quantification (iTRAQ) technique using liquid chromatography-tandem mass spectrometry (LC-MS/MS). The iTRAQ quantification of the secretome revealed unique extracellular enzyme system, including discrete multienzyme complexes of cellulases, hemicellulases, glycoside hydrolases, proteases, peroxidases, and protein translocating transporter proteins. When the strain was grown in these substrate conditions, proteins corresponding to cellulases, hemicellulases and transport proteins were highly up-regulated, while lignin degrading DyP-type peroxidase, novel nonheme peroxidases, catalase, cytochrome-c oxidase, and superoxide dismutase were also identified. Numerous proteins presumed to be involved in lignocellulose hydrolysis were expressed in response to these different culture conditions, and among these were several secreted hypothetical proteins that were not previously observed.
MeSH term(s)	Actinobacteria/chemistry ; Actinobacteria/enzymology ; Actinobacteria/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/secretion ; Cellulases/chemistry ; Cellulose/metabolism ; Glycoside Hydrolases/chemistry ; Hydrolysis ; Isotope Labeling/methods ; Lignin/metabolism ; Peptide Hydrolases/chemistry ; Proteome/chemistry ; Proteome/secretion ; Proteomics/methods ; Tandem Mass Spectrometry
Chemical Substances	Bacterial Proteins ; Proteome ; Cellulose (9004-34-6) ; Lignin (9005-53-2) ; Cellulases (EC 3.2.1.-) ; Glycoside Hydrolases (EC 3.2.1.-) ; hemicellulase (EC 3.2.1.-) ; Peptide Hydrolases (EC 3.4.-)
Language	English
Publishing date	2010-06-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/pr901174z
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Article: Purification and partial characterization of serine protease from thermostable alkalophilic Bacillus laterosporus-AK1

Arulmani, Manavalan / Aparanjini, Kalaichelvan / Vasanthi, Kalyanasundaram / Arumugam, Perumal / Arivuchelvi, Manavalan / Kalaichelvan, P. Thangavelu

World journal of microbiology & biotechnology. 2007 Apr., v. 23, no. 4

2007

Abstract: An extracellular thermostable alkaline protease isolated from Bacillus laterosporus-AK1 was purified by sephadex G-200 gel filtration and DEAE cellulose ion-exchange chromatography techniques. The purified protease showed a maximum relative activity of ... ...

Abstract	An extracellular thermostable alkaline protease isolated from Bacillus laterosporus-AK1 was purified by sephadex G-200 gel filtration and DEAE cellulose ion-exchange chromatography techniques. The purified protease showed a maximum relative activity of 100% on casein substrate and appeared as a single band on SDS-PAGE with the molecular mass of 86.29 kDa. The protease was purified to 11.1-folds with a yield of 34.3%. Gelatin zymogram also revealed a clear hydrolytic zone due to proteolytic activity, which corresponded to the band obtained with SDS-PAGE. The protease enzyme had on optimum pH of 9.0 and exhibited highest activity at 75°C. The enzyme activity was highly susceptible to the specific serine protease inhibitor PMSF, suggesting the presence of serine residues at the active sites. Enzyme activity strongly enhanced by the metal ions Ca²⁺ and Mg²⁺ and this enzyme compatible with aril detergent stability retained 75% even 1-h incubation. The purified protease remove bloodstain completely when used with Wheel detergent.
Keywords	Brevibacillus laterosporus ; purification
Language	English
Dates of publication	2007-04
Size	p. 475-481.
Publisher	Kluwer Academic Publishers
Publishing place	Dordrecht
Document type	Article
ZDB-ID	1499109-3
ISSN	1573-0972 ; 0959-3993
ISSN (online)	1573-0972
ISSN	0959-3993
DOI	10.1007/s11274-006-9249-7
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Article: Purification and characterization of laccase produced by a white rot fungus Pleurotus sajor-caju under submerged culture condition and its potential in decolorization of azo dyes.

Murugesan, Kumarasamy / Arulmani, Manavalan / Nam, In-Hyun / Kim, Young-Mo / Chang, Yoon-Seok / Kalaichelvan, P Thangavelu

Applied microbiology and biotechnology

2006 Volume 72, Issue 5, Page(s) 939–946

Abstract: An extracellular laccase was isolated and purified from Pleurotus sajor-caju grown in submerged culture in a bioreactor, and used to investigate its ability to decolorize three azo dyes. The extracellular laccase production was enhanced up to 2.5-fold in ...

Abstract	An extracellular laccase was isolated and purified from Pleurotus sajor-caju grown in submerged culture in a bioreactor, and used to investigate its ability to decolorize three azo dyes. The extracellular laccase production was enhanced up to 2.5-fold in the medium amended with xylidine (1 mM). Purification was carried out using ammonium sulfate (70% w/v), DEAE-cellulose, and Sephadex G-100 column chromatography. The enzyme was purified up to 10.3-fold from the initial protein preparation with an overall yield of 53%. The purified laccase was monomeric with an apparent molecular mass of 61.0 kDa. The purified enzyme exerted its optimal activity with 2,2-azino-bis(3-ethylbenzo-thiazoline-6-sulfonate (ABTS) and oxidized various lignin-related phenols. The catalytic efficiencies kcat/Km determined for ABTS and syringaldazine were 9.2x10(5) and 8.7x10(5), respectively. The optimum pH and temperature for the purified enzyme was 5.0 and 40 degrees C, respectively. Sodium azide completely inhibited the laccase activity. The absorption spectrum revealed type 1 and type 3 copper signals. The purified enzyme decolorized azo dyes such as acid red 18, acid Black 1, and direct blue 71 up to 90, 87, and 72%, respectively. Decolorization ability of P. sajor-caju laccase suggests that this enzyme could be used for decolorization of industrial effluents.
MeSH term(s)	Azo Compounds/chemistry ; Azo Compounds/metabolism ; Coloring Agents/chemistry ; Coloring Agents/metabolism ; Hydrogen-Ion Concentration ; Laccase/metabolism ; Pleurotus/enzymology ; Temperature ; Time Factors
Chemical Substances	Azo Compounds ; Coloring Agents ; Laccase (EC 1.10.3.2)
Language	English
Publishing date	2006-10
Publishing country	Germany
Document type	Journal Article
ZDB-ID	392453-1
ISSN	1432-0614 ; 0175-7598 ; 0171-1741
ISSN (online)	1432-0614
ISSN	0175-7598 ; 0171-1741
DOI	10.1007/s00253-006-0403-9
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Article: Purification and characterization of laccase produced by a white rot fungus Pleurotus sajor-caju under submerged culture condition and its potential in decolorization of azo dyes

Murugesan, Kumarasamy / Arulmani, Manavalan / Nam, In-Hyun / Kim, Young-Mo / Chang, Yoon-Seok / Kalaichelvan, P. Thangavelu

Applied microbiology and biotechnology. 2006 Oct., v. 72, no. 5

2006

Abstract	An extracellular laccase was isolated and purified from Pleurotus sajor-caju grown in submerged culture in a bioreactor, and used to investigate its ability to decolorize three azo dyes. The extracellular laccase production was enhanced up to 2.5-fold in the medium amended with xylidine (1 mM). Purification was carried out using ammonium sulfate (70% w/v), DEAE-cellulose, and Sephadex G-100 column chromatography. The enzyme was purified up to 10.3-fold from the initial protein preparation with an overall yield of 53%. The purified laccase was monomeric with an apparent molecular mass of 61.0 kDa. The purified enzyme exerted its optimal activity with 2,2-azino-bis(3-ethylbenzo-thiazoline-6-sulfonate (ABTS) and oxidized various lignin-related phenols. The catalytic efficiencies k cat/K m determined for ABTS and syringaldazine were 9.2x10⁵ and 8.7x10⁵, respectively. The optimum pH and temperature for the purified enzyme was 5.0 and 40 °C, respectively. Sodium azide completely inhibited the laccase activity. The absorption spectrum revealed type 1 and type 3 copper signals. The purified enzyme decolorized azo dyes such as acid red 18, acid Black 1, and direct blue 71 up to 90, 87, and 72%, respectively. Decolorization ability of P. sajor-caju laccase suggests that this enzyme could be used for decolorization of industrial effluents.
Keywords	Pleurotus sajor-caju ; absorption ; ammonium sulfate ; azo dyes ; chromatography ; decolorization ; fungi ; industrial effluents ; laccase ; molecular weight ; pH ; phenols ; sodium azide ; temperature
Language	English
Dates of publication	2006-10
Size	p. 939-946.
Publisher	Springer-Verlag
Publishing place	Berlin/Heidelberg
Document type	Article
ZDB-ID	392453-1
ISSN	1432-0614 ; 0171-1741 ; 0175-7598
ISSN (online)	1432-0614
ISSN	0171-1741 ; 0175-7598
DOI	10.1007/s00253-006-0403-9
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