A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A3101, induced by histamine and its analogue betahistine

Abstract Biogenic amines (BAs) are low molecular weight organic bases formed by natural amino acids decarboxylation and trigger an array of toxicological effects in humans and animals. Bacterial amine oxidases enzymes are determined as practical tools to implement the rapid quantification of BAs in foods. Our study set out to obtain a new efficient, amine oxidase enzyme for developing new enzyme-based quantification of histamine. The soils from different sources were screened using histamine as sole carbon and nitrogen sources, and histamine oxidase producing bacteria were selected and identified using specific primers for histamine oxidase (HOD) gene. The HOD gene of six strains, out of 26 isolated histamine-utilizing bacteria, were amplified using our designed primers. The HOD enzyme from Glutamicibacter sp. N1A3101, isolated from nettle soil, was found to be thermostable and showed the highest substrate specificity toward the histamine and with no detected activity in the presence of putrescine, cadaverine, spermine, and spermidine. Its oxidation activity toward tyramine was lower than other HOD reported so far. The isolated enzyme was stable at 60 °C for 30 min and showed pH stability ranging from 6 to 9. Furthermore, we indicated the induction of identified HOD activity in the presence of betahistine as well, with nearly equal efficiency and without the consumption of the substrate.

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A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A310, induced by histamine and its analogue betahistine

10.21203/rs.3.rs-61063/v2 ◽

2020 ◽

Author(s):

Hossein Sadeghi ◽

Sareh Arjmand ◽

Seyed Omid Ranaei Siadat ◽

Jamshid Fooladi ◽

Gholamhossein Ebrahimipour

Keyword(s):

Amine Oxidase ◽

Nitrogen Sources ◽

Amine Oxidases ◽

Oxidation Activity ◽

Carbon And Nitrogen ◽

Toxicological Effects ◽

Organic Bases ◽

Oxidase Enzyme ◽

Natural Amino Acids ◽

Different Sources

Abstract Biogenic amines (BAs) are low molecular weight organic bases formed by natural amino acids decarboxylation and trigger an array of toxicological effects in humans and animals. Bacterial amine oxidases enzymes are determined as practical tools to implement the rapid quantification of BAs in foods. Our study set out to obtain a new efficient, amine oxidase enzyme for developing new enzyme-based quantification of histamine. The soils from different sources were screened using histamine as sole carbon and nitrogen sources, and histamine oxidase producing bacteria were selected and identified using specific primers for histamine oxidase (HOD) gene. The HOD gene of six strains, out of 26 isolated histamine-utilizing bacteria, were amplified using our designed primers. The HOD enzyme from Glutamicibacter sp. N1A3101, isolated from nettle soil, was found to be thermostable and showed the highest substrate specificity toward the histamine and with no detected activity in the presence of putrescine, cadaverine, spermine, and spermidine. Its oxidation activity toward tyramine was lower than other HOD reported so far. The isolated enzyme was stable at 60 °C for 30 min and showed pH stability ranging from 6-9. Furthermore, we indicated the induction of identified HOD activity in the presence of betahistine as well, with nearly equal efficiency and without the consumption of the substrate.

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A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A310, induced by histamine and its analogue betahistine

10.21203/rs.3.rs-61063/v1 ◽

2020 ◽

Author(s):

Hossein Sadeghi ◽

Sareh Arjmand ◽

Seyed Omid Ranaei Siadat ◽

Jamshid Fooladi ◽

Gholamhossein Ebrahimipour

Keyword(s):

Amine Oxidase ◽

Nitrogen Sources ◽

Amine Oxidases ◽

Oxidation Activity ◽

Carbon And Nitrogen ◽

Toxicological Effects ◽

Organic Bases ◽

Oxidase Enzyme ◽

Natural Amino Acids ◽

Different Sources

Abstract Biogenic amines (BAs) are low molecular weight organic bases formed by natural amino acids decarboxylation and trigger an array of toxicological effects in humans and animals. Bacterial amine oxidases enzymes are determined as practical tools to implement the rapid quantification of BAs in foods. Our study set out to obtain a new efficient, amine oxidase enzyme for developing new enzyme-based quantification of histamine. The soils from different sources were screened using histamine as sole carbon and nitrogen sources, and histamine oxidase producing bacteria were selected and identified using specific primers for histamine oxidase (HOD) gene. The HOD gene of six strains, out of 26 isolated histamine-utilizing bacteria, were amplified using our designed primers. The HOD enzyme from Glutamicibacter sp. N1A3101, isolated from nettle soil, was found to be thermostable and showed the highest substrate specificity toward the histamine and with no detected activity in the presence of putrescine, cadaverine, spermine, and spermidine. Its oxidation activity toward tyramine was lower than other HOD reported so far. The isolated enzyme was stable at 60 °C for 30 min and showed pH stability ranging from 6–9. Furthermore, we indicated the induction of identified HOD activity in the presence of betahistine as well, with nearly equal efficiency and without the consumption of the substrate.

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Growth responses of aquatic hyphomycetes to different sources of carbon and nitrogen

Journal of Applied and Natural Science ◽

10.31018/jans.v5i2.323 ◽

2013 ◽

Vol 5 (2) ◽

pp. 313-317 ◽

Cited By ~ 3

Author(s):

Saraswati Bisht

Keyword(s):

Carbon Sources ◽

Nitrogen Sources ◽

Dry Weight ◽

Maximum Growth ◽

Fungal Species ◽

Aquatic Hyphomycetes ◽

Growth Responses ◽

Carbon And Nitrogen ◽

Fungal Isolates ◽

Different Sources

Assessment of different sources of carbon and nitrogen in terms of dry weight biomass of four selected aquatic hyphomycetes viz; Flagellospora penicilloides Ingold, Pestalotiopsis submersus Sati and Tiwari, Tetrachaetum elegans Ingold and Tetracladium marchalianum De Wildeman was made for their nutritional requirements. Eight carbon sources and ten nitrogen sources were singly added to the basal media in order to provide 4g of carbon and 1g of nitrogen per litre of distilled water. Among carbon compounds glucose and sucrose were found to be most suitable sources of carbon for all the four fungal isolates, where as fructose proved good for T. marchalianum, P. submersus and F.penicilloides fairly. Cellulose was found a poor source of carbon for the growth of all these isolates. The inorganic sources of nitrogen were found as good nitrogen sources with preference for ammonium ions. Suitability of amino acids was found variable from species to species for nitrogen. T.elegans and T.marchalianum had their maximum growth in asparagines, whereas, P. submersus had their highest growth in proline. Cysteine was observed as a good source of nitrogen for almost all the fungal isolates used. Anova calculated for these observed data showed significant variations in the dry weight production of different fungal species grown in different sources of carbon and nitrogen(P<0.01).

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Nutritional requirements for growth of fungal endophytes of grasses

Canadian Journal of Microbiology ◽

10.1139/w98-004 ◽

1998 ◽

Vol 44 (3) ◽

pp. 231-237 ◽

Cited By ~ 6

Author(s):

Walid Naffaa ◽

Catherine Ravel ◽

Jean-Jacques Guillaumin

Keyword(s):

Rapid Growth ◽

Fungal Endophytes ◽

Carbon Sources ◽

Nitrogen Sources ◽

Sensu Stricto ◽

Poor Growth ◽

Carbon And Nitrogen ◽

High Concentrations ◽

Different Sources ◽

Previous Group

Fifteen isolates of fungal endophytes of grasses were studied for their ability to metabolize different sources of carbon and nitrogen. These endophytes had been isolated from 12 different species of Poaceae and included Clavicipitaceae with or without a teleomorph (genera Epichloë and Neotyphodium, respectively) and species belonging to the genus Acremonium sensu stricto (Acremonium chilense-like). Pectin and cellulose as carbon sources and tryptophan and methionine as nitrogen sources appeared to support poorly the growth of most isolates. Hexoses, disaccharides, complex nitrogen sources, asparagine, and glutamine supported growth of all isolates. The isolates of genus Neotyphodium were characterized by limited growth whatever the substrate, the inhibition of their growth by high concentrations of glucose and fructose, and their inability to assimilate pentoses (xylose, arabinose) and nitrates. The isolates of genus Epichloë showed better growth than those of the previous group and their growth was not inhibited by high concentrations of glucose, but they were also unable to use pentoses. The Acremonium chilense-like isolates showed rapid growth and were distinguished by their ability to use the pentoses and nitrates. In contrast, they showed relatively poor growth on methionine and alanine as nitrogen sources. They showed the most rapid growth on high concentrations of glucose or fructose.Key words: carbon sources, nitrogen sources, Neotyphodium, Epichloë, Acremonium, grass endophytes.

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Enhanced production of β- glucosidase by locally isolated fungal strain employing submerged fermentation

Bioscience Journal ◽

10.14393/bj-v35n5a2019-47943 ◽

2019 ◽

Vol 35 (5) ◽

Cited By ~ 1

Author(s):

Roheena Abdullah ◽

Sobia Nazir Chudhary ◽

Afshan Kaleem ◽

Mehwish Iqtedar ◽

Kinza Nisar ◽

...

Keyword(s):

Submerged Fermentation ◽

Wide Spectrum ◽

Nitrogen Sources ◽

Fermentation Medium ◽

Fungal Strain ◽

Carbon And Nitrogen Sources ◽

Carbon And Nitrogen ◽

Enhanced Production ◽

Different Sources ◽

Fermentation Media

β-glucosidase has wide spectrum of biotechnological applications in different industries including food, textile, laundry detergents, pulp and paper, pharmaceutical and biofuel industry. The present investigation related to isolation, screening, and process optimization of fungal strain for enhanced production of β-glucosidase (BGL). For this purpose, different fungal stains were isolated from different sources including soil, fruits, bark of tree as well as from the compost. The screening of fungal strain for BGL production was carried out via submerged fermentation. All the tested strains were identified on the basis of micro and macroscopic features. The fungal strain having greater ability for BGL synthesis among tested ones was identified as Aspergillus niger and given the code SBT-15. The process parameter including fermentation media, temperature, pH, rate of fermentation, carbon and nitrogen sources, volume of media were optimized. Five different fermentation media were evaluated M3 medium gave maximum production. The optimal conditions for BGL production was 72 hours of incubation at 40°C, pH 6 and 50 ml fermentation medium. Glucose (1%) and ammonium sulphate (3%) were optimized as best carbon and nitrogen sources, respectively.

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THE STUDY OF ETHANOL PRODUCTION BY NEW STRAIN OF YEASTS "HANSENIASPORA OPUNTIAE MK 460485", INVESTIGATION OF ITS ETHANOL PRODUCTION IN PRESENCE OF DIFFERENT CARBON AND NITROGEN SOURCES, AND OPTIMAL CONDITIONS

Journal of Critical Reviews ◽

10.31838/jcr.07.04.94 ◽

2020 ◽

Vol 7 (04) ◽

Keyword(s):

Ethanol Production ◽

Nitrogen Sources ◽

Optimal Conditions ◽

Carbon And Nitrogen Sources ◽

Carbon And Nitrogen

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A highly thermotolerant laccase produced by Cerrena unicolor strain CGMCC 5.1011 for complete and stable malachite green decolorization

AMB Express ◽

10.1186/s13568-020-01118-z ◽

2020 ◽

Vol 10 (1) ◽

Author(s):

Yanhua Yao ◽

Guimei Zhou ◽

Yonghui Lin ◽

Xinqi Xu ◽

Jie Yang

Keyword(s):

Malachite Green ◽

Fermentation Broth ◽

Nitrogen Sources ◽

Life Time ◽

Industrial Applications ◽

Dynamics Simulation ◽

Carbon And Nitrogen ◽

Cdna Sequences ◽

Cerrena Unicolor ◽

Future Work

Abstract Laccases are a class of multi-copper oxidases with important industrial values. A thermotolerant laccase produced by a basidiomycete fungal strain Cerrena unicolor CGMCC 5.1011 was studied. With glycerin and peptone as the carbon and nitrogen sources, respectively, a maximal laccase activity of 121.7 U/mL was attained after cultivation in the shaking flask for 15 days. Transcriptomics analysis revealed an expressed laccase gene family of 12 members in C. unicolor strain CGMCC 5.1011, and the gene and cDNA sequences were cloned. A glycosylated laccase was purified from the fermentation broth of Cerrena unicolor CGMCC 5.1011 and corresponded to Lac2 based on MALDI-TOF MS/MS identification. Lac2 was stable at pH 5.0 and above, and was resistant to organic solvents. Lac2 displayed remarkable thermostability, with half-life time of 1.67 h at 70 ºC. Consistently, Lac2 was able to completely decolorize malachite green (MG) at high temperatures, whereas Lac7 from Cerrena sp. HYB07 resulted in accumulation of colored MG transformation intermediates. Molecular dynamics simulation of Lac2 was conducted, and possible mechanisms underlying Lac2 thermostability were discussed. The robustness of C. unicolor CGMCC 5.1011 laccase would not only be useful for industrial applications, but also provide a template for future work to develop thermostable laccases.

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