Exo‐inulinase production from <i>Aspergillus fumigatus</i> NFCCI 2426: purification, characterization, and immobilization for continuous fructose production

Rawat, Hemant Kumar; Soni, Hemant; Suryawanshi, Rahul Kumar; Choukade, Ritumbhara; Prajapati, Bhanu Pratap; Kango, Naveen

doi:10.1111/1750-3841.15681

Cited by 8 publications

(4 citation statements)

References 72 publications

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“…The more amount of reducing sugar produced is the higher the inulinase activity and vice versa [25]. The results of this study are different from the previous studies which found sources of inulinase from fungi such as the discovery of Aspergillus fumigatus [26], and Penicillium sp., as well as other sources of inulinase from bacteria such as Pseudomonas sp., Bacillus sp., and Arthrobacter sp, and source inulinase from yeasts such as Saccharomyces sp., Kluyveromyces sp., and Candida sp. [27].…”

Section: Discussioncontrasting

confidence: 97%

Isolation and Molecular Identification of Endophytic Mold Schizophillum commune in Red Dahlia (Dahlia sp. L) Tuber as Producing Inulinases

Sunarti

Ginting

2022

Open Access Maced J Med Sci

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BACKGROUND: Dahlia tuber as the source of isolates in endophytic mold produces Inulinases. Inulinase is used in industry to produce inulin to become fructose through an enzymatic reaction. Fructose from natural substances constitutes low calories used as diet in diabetes mellitus type 2 patients. An important phase is done obtain the inulinase enzyme through mold isolation. AIM: The objective of this research was to isolate and identify the molecular of endophytic mold from red dahlia tuber which had the optimum inulinase activity. METHODS: Mold isolation was done through the stage of surface sterilization and purification. Mold isolation which had the highest inulinase activity was identified in a molecular using the polymerase chain reaction technique with the Internal transcribed spacers ITS region. DNA amplification used primer ITS 1 and ITS 4. RESULTS: The result of the study showed that there was five-mold isolation with the result of screening high inulinase activity found in UD3 (++), UD4 (++), and UD5 (+++), the value of inulinase enzyme activity of UD3 was 0.582716049, UD4 was 0.330864198, and UD5 was 0.685185185. The result of identifying UD5 molecular in eight DNA tapes was successfully amplified with 660 pb. The result of identifying molecular based on BLAST analysis found Schizophillum commune species CONCLUSION: It was found that the highest inulinase activity was the species S. commune, which added new variants of inulinase enzyme from red dahlia tuber which could be used by industry to yield fructose through an enzymatic reaction.

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Section: Discussioncontrasting

confidence: 97%

Isolation and Molecular Identification of Endophytic Mold Schizophillum commune in Red Dahlia (Dahlia sp. L) Tuber as Producing Inulinases

Sunarti

Ginting

2022

Open Access Maced J Med Sci

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“…As for the characteristics of the enzyme, its optimum temperature (60 °C) is the same as that reported for Aspergillus fumigatus [ 19 ], Aspergillus niger [ 20 ], and Aspergillus tubingensis [ 21 ] inulinases. With an optimum pH of 4.0, the enzyme proved to be resistant to acidic conditions, a feature of great interest for high-fructose syrup (HFS) production, because it reduces the risk of microbial contamination especially during continuous operation [ 22 ].…”

Section: Discussionmentioning

confidence: 80%

Production, Biochemical Characterization, and Kinetic/Thermodynamic Study of Inulinase from Aspergillus terreus URM4658

Oliveira¹,

Silva²,

Converti

et al. 2022

Molecules

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Inulinases are enzymes involved in the hydrolysis of inulin, which can be used in the food industry to produce high-fructose syrups and fructo-oligosaccharides. For this purpose, different Aspergillus strains and substrates were tested for inulinase production by solid-state fermentation, among which Aspergillus terreus URM4658 grown on wheat bran showed the highest activity (15.08 U mL−1). The inulinase produced by this strain exhibited optimum activity at 60 °C and pH 4.0. A detailed kinetic/thermodynamic study was performed on the inulin hydrolysis reaction and enzyme thermal inactivation. Inulinase was shown to have a high affinity for substrate evidenced by very-low Michaelis constant values (0.78–2.02 mM), which together with a low activation energy (19.59 kJ mol−1), indicates good enzyme catalytic potential. Moreover, its long half-life (t1/2 = 519.86 min) and very high D-value (1726.94 min) at 60 °C suggested great thermostability, which was confirmed by the thermodynamic parameters of its thermal denaturation, namely the activation energy of thermal denaturation (E*d = 182.18 kJ mol−1) and Gibbs free energy (106.18 ≤ ΔG*d ≤ 111.56 kJ mol−1). These results indicate that A. terreus URM4658 inulinase is a promising and efficient biocatalyst, which could be fruitfully exploited in long-term industrial applications.

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“…Exoinulinase produces fructose as the main product by cleaving terminal units of fructose from inulin, whereas the inner linkages of inulin are hydrolyzed by endoinulinase into inulo-oligosaccharides [5,8]. Inulinase is a valuable enzyme used principally for fructose [10,11], ultrahigh fructose syrup [12,13], and ethanol [8,14] production.…”

Section: Introductionmentioning

confidence: 99%

Production, purification, and characterization of inulinase from Streptomyces anulatus

Beroigui

Ghadraoui

2023

J Basic Microbiol

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Inulinase is an enzyme that catalyzes inulin to D-fructose. This enzyme can be extracted from plants, but it is difficult to obtain it in large quantities, so its production cost is high. Therefore, microbial inulinase has great potential for industrial needs. In the last decade, there have been very few reports on actinobacterial inulinases, especially on purification and characterization of inulinase process extraction. This study aims to select actinomycetes that possess high inulinase activity from the soil. To screen inulinase-producing bacteria, modified Czapex-Dox agar supplemented with 1% inulin powder was used. The most effective isolate was Streptomyces sp. EFBO8, morphological and genotypic identification methods, confirmed that the strain is Streptomyces anulatus and that its nucleotide sequence has been deposited in GenBank under accession number OQ073700. To optimize inulinase production, kinetics were performed by using S. anulatus strain, which proved to be most productive with a value of 24,024 EU/mL. The enzyme was purified from the culture filtrate by precipitation with ammonium sulfate (NH 4 ) 2 SO 4 , followed by column chromatography Sephadex (G-50) separation. Purified protein has a molecular mass of 3331.83 Da.

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Exo‐inulinase production from Aspergillus fumigatus NFCCI 2426: purification, characterization, and immobilization for continuous fructose production

Cited by 8 publications

References 72 publications

Isolation and Molecular Identification of Endophytic Mold Schizophillum commune in Red Dahlia (Dahlia sp. L) Tuber as Producing Inulinases

Isolation and Molecular Identification of Endophytic Mold Schizophillum commune in Red Dahlia (Dahlia sp. L) Tuber as Producing Inulinases

Production, Biochemical Characterization, and Kinetic/Thermodynamic Study of Inulinase from Aspergillus terreus URM4658

Production, purification, and characterization of inulinase from Streptomyces anulatus

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