Journal Articles
- Production of an Endoinulinase from Aspergillus niger AUMC 9375, by Solid State Fermentation of Agricultural Wastes, with Purification and Characterization of the Free and Immobilized Enzyme
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Manal M. Housseiny
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J. Microbiol. 2014;52(5):389-398. Published online May 9, 2014
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DOI: https://doi.org/10.1007/s12275-014-3561-y
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Abstract
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Two different substrates, sunflower (Helianthus annuus L.) tubers and lettuce (Lactuca sativa) roots, were tested. Using a mixture of both wastes resulted in higher production of endoinulinase than either waste alone. Also, ten fungal spe-cies grown on these substrates as inexpensive, carbon sour-ces were screened for the best production of endoinulinase activities. Of these, Aspergillus niger AUMC 9375 was the most productive, when grown on the mixture using a 6:1 w/w ratio of sun flower: lettuce, and yielded the highest levels of inulinase at 50% moisture, 30°C, pH 5.0, with seven days of incubation, and with yeast extract as the best nitrogen source. Inulinase was purified to homogeneity by ion-exchange chro-matography and gel-filtration giving a 51.11 fold purification. The mixture of sunflower tubers and lettuce roots has poten-tial to be an effective and economical substrate for inulinase production. Inulinase was successfully immobilized with an immobilization yield of 71.28%. After incubation for 2 h at 60°C, the free enzyme activity decreased markedly to 10%, whereas that of the immobilized form decreased only to 87%. A reusability test demonstrated the durability of the immo-bilized inulinase for 10 cycles and in addition, that it could be stored for 32 days at 4°C. These results indicate that this inulinase, in the immobilized form, is a potential candidate for large-scale production of high purity fructose syrups.
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Citations
Citations to this article as recorded by

- Production of β-mannanase, inulinase, and oligosaccharides from coffee wastes and extracts
Selin Basmak, Irfan Turhan
International Journal of Biological Macromolecules.2024; 261: 129798. CrossRef - Sustainable inulinase enzyme production from novel strain Fusarium parceramosum with mixed biomass substrates of rice husk and banana shoot through solid-state fermentation
Shreya Hegde, Ramananda Bhat M, Subbalaxmi Selvaraj
Biomass Conversion and Biorefinery.2024;[Epub] CrossRef - Bio-utilization of agricultural residue banana plant shoot through solid state fermentation for production of inulinase using newly isolated Nothophoma anigozanthi JAM
Nisarga Tippanavar, Divya Bhat, Orline Rebello, Girisa Prabhu, Subbalaxmi Selvaraj, Ramananda M. Bhat
Biomass Conversion and Biorefinery.2024; 14(13): 14755. CrossRef - Aspergillus welwitschiae inulinase enzyme cocktails obtained on agro-material inducers for the purpose of fructooligosaccharides production
Sanja Stojanović, Marina Ristović, Jelena Stepanović, Aleksandra Margetić, Bojan Duduk, Zoran Vujčić, Biljana Dojnov
Food Research International.2022; 160: 111755. CrossRef - Solid-state fermentation enhances inulinase and invertase production by Aspergillus brasiliensis
C. Guerrero-Urrutia, T. Volke-Sepulveda, F. Figueroa-Martinez, E. Favela-Torres
Process Biochemistry.2021; 108: 169. CrossRef - Statistical optimization of solid-state fermentation for the production of fungal inulinase from apple pomace
Ram Sarup Singh, Kanika Chauhan, Karminder Kaur, Ashok Pandey
Bioresource Technology Reports.2020; 9: 100364. CrossRef - Optimization of inulinase production by a newly isolated strain Aspergillus flavus var. flavus by solid state fermentation of Saccharum arundinaceum
Deblina Das, Raja Selvaraj, M. Ramananda Bhat
Biocatalysis and Agricultural Biotechnology.2019; 22: 101363. CrossRef - Review of inulinase production using solid-state fermentation
Deblina Das, Ramananda Bhat M, Raja Selvaraj
Annals of Microbiology.2019; 69(3): 201. CrossRef - Immobilized inulinase: a new horizon of paramount importance driving the production of sweetener and prebiotics
Gerard Neeraj, Shobana Ravi, Ravindran Somdutt, ShriAishvarya Kaliyur Ravi, Vaidyanathan Vinoth Kumar
Critical Reviews in Biotechnology.2018; 38(3): 409. CrossRef - The cell wall anchored β-fructosidases of Lactobacillus paracasei : Overproduction, purification, and gene expression control
Petya Velikova, Kaloyan Petrov, Penka Petrova
Process Biochemistry.2017; 52: 53. CrossRef - Continuous generation of fructose from Taraxacum officinale tap root extract and inulin by immobilized inulinase in a packed-bed reactor
Hemant Kumar Rawat, Hemant Soni, Naveen Kango, C. Ganesh Kumar
Biocatalysis and Agricultural Biotechnology.2017; 9: 134. CrossRef - Biotechnological potential of microbial inulinases: Recent perspective
Hemant Kumar Rawat, Hemant Soni, Helen Treichel, Naveen Kango
Critical Reviews in Food Science and Nutrition.2017; 57(18): 3818. CrossRef - Development of heterogeneous preparation with inulinase for tubular reactor systems
M.G. Holyavka, M.P. Evstigneev, V.G. Artyukhov, V.V. Savin
Journal of Molecular Catalysis B: Enzymatic.2016; 129: 1. CrossRef - Recent insights in enzymatic synthesis of fructooligosaccharides from inulin
Ram Sarup Singh, Rupinder Pal Singh, John F. Kennedy
International Journal of Biological Macromolecules.2016; 85: 565. CrossRef - Production of inulinase, fructosyltransferase and sucrase from fungi on low-value inulin-rich substrates and their use in generation of fructose and fructo-oligosaccharides
Hemant Kumar Rawat, Mohd Anis Ganaie, Naveen Kango
Antonie van Leeuwenhoek.2015; 107(3): 799. CrossRef
- Purification and Characterization of a New L-Methioninase from Solid Cultures of Aspergillus flavipes
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Ashraf S. A. El-Sayed
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J. Microbiol. 2011;49(1):130-140. Published online March 3, 2011
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DOI: https://doi.org/10.1007/s12275-011-0259-2
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Abstract
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L-Methioninase was purified to electrophoretic homogeneity from cultures of Aspergillus flavipes using anionexchange and gel filtration chromatography by 12.1 fold compared to the crude enzyme preparation. The purified enzyme had a molecular mass of 47 kDa under denaturing conditions and an isoelectric point
of 5.8 with no structural glycosyl residues. The enzyme had optimum activity at pH 7.8 and pH stability from 6.8-8.0 at 35°C. The enzyme appeared to be catalytically stable below 40°C. The enzyme activity was strongly inhibited by DL-propargylglycine, hydroxylamine, PMSF, 2-mercaptoethanol, Hg2+, Cu2+, and
Fe2+, with slight inhibition by Triton X-100. A. flavipes L-methioninase has a higher catalytic affinity towards L-methionine (Km, 6.5 mM and Kcat, 14.1 S-1) followed by a relative demethiolating activity to L-homocysteine (Km, 12 mM and Kcat, 9.3 S-1). The enzyme has two absorption maxima at 280 and 420 nm, typical of other PLP-enzymes. Apo-L-methioninase has the ability to reconstitute its structural catalytic
state completely upon addition of 0.15 mM PLP. L-Methioninase has neither an appreciable effect on liver function, platelet aggregation, nor hemolysis of human blood. The purified L-methioninase from solid cultures of A. flavipes displayed unique biochemical and catalytic properties over the currently applied Pseudomonad
enzyme.
Research Support, Non-U.S. Gov't
- Production, Partial Characterization, and Immobilization in Alginate Beads of an Alkaline Protease from a New Thermophilic Fungus Myceliophthora sp.
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Letícia Maria Zanphorlin , Fernanda Dell Antonio Facchini , Filipe Vasconcelos , Rafaella Costa Bonugli-Santos , André Rodrigues , Lara Durães Sette , Eleni Gomes , Gustavo Orlando Bonilla-Rodriguez
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J. Microbiol. 2010;48(3):331-336. Published online June 23, 2010
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DOI: https://doi.org/10.1007/s12275-010-9269-8
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38
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34
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Abstract
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Thermophilic fungi produce thermostable enzymes which have a number of applications, mainly in biotechnological processes. In this work, we describe the characterization of a protease produced in solidstate (SSF) and submerged (SmF) fermentations by a newly isolated thermophilic fungus identified as a putative new species in the genus Myceliophthora. Enzyme-production rate was evaluated for both fermentation processes, and in SSF, using a medium composed of a mixture of wheat bran and casein, the proteolytic output was 4.5-fold larger than that obtained in SmF. Additionally, the peak of proteolytic activity was obtained after 3 days for SSF whereas for SmF it was after 4 days. The crude enzyme obtained by both
SSF and SmF displayed similar optimum temperature at 50°C, but the optimum pH shifted from 7 (SmF) to 9 (SSF). The alkaline protease produced through solid-state fermentation (SSF), was immobilized on beads of calcium alginate, allowing comparative analyses of free and immobilized proteases to be carried out. It was
observed that both optimum temperature and thermal stability of the immobilized enzyme were higher than for the free enzyme. Moreover, the immobilized enzyme showed considerable stability for up to 7 reuses.