Identification and Characterization of α-Amylase and Endoxylanase, Produced by<i>Aspergillus</i>Mutant Strains

Evstatieva, Yana; Nikolova, Dilyana; Ilieva, Svetla; Getov, L.; Savov, V.

doi:10.1080/13102818.2010.10817908

Cited by 7 publications

(3 citation statements)

References 12 publications

(16 reference statements)

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“…According to (Wang et al,) 33 , who reported that low molecular weight xylanase is at the range of 21–34 kDa, this xylanase is considered to low molecular weight for xylanases. The low molecular weight of our purified xylanase was identical to the enzyme reported from an Aspergillus mutant strain 34 , Bacillus subtilis 35 , and Trichoderma inhamatum 9 . A higher molecular weight xylanase was reported for Bacillus pumilus 36 , for Bacillus sp.…”

Section: Resultssupporting

confidence: 73%

Paecilomyces variotii xylanase production, purification and characterization with antioxidant xylo-oligosaccharides production

Abdella

Ramadan

Hamouda

et al. 2021

Sci Rep

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Paecilomyces variotii xylanase was, produced in stirred tank bioreactor with yield of 760 U/mL and purified using 70% ammonium sulfate precipitation and ultra-filtration causing 3.29-fold purification with 34.47% activity recovery. The enzyme purity was analyzed on sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) confirming its monomeric nature as single band at 32 KDa. Zymography showed xylan hydrolysis activity at the same band. The purified enzyme had optimum activity at 60 °C and pH 5.0. The pH stability range was 5–9 and the temperature stability was up 70 °C. Fe2+and Fe3+ exhibited inhibition of xylanase enzyme while Cu2+, Ca2+, Mg2+ and Mn2+ stimulated its activity. Mercaptoethanol stimulated its activity; however, Na2-EDTA and SDS inhibited its activity. The purified xylanase could hydrolyze beechwood xylan but not carboxymethyl cellulose (CMC), avicel or soluble starch. Paecilomyces variotii xylanase Km and Vmax for beechwood were determined to be 3.33 mg/mL and 5555 U/mg, respectively. The produced xylanase enzyme applied on beech xylan resulted in different types of XOS. The antioxidant activity of xylo-oligosaccharides increased from 15.22 to 70.57% when the extract concentration was increased from 0.1 to 1.5 mg/mL. The enzyme characteristics and kinetic parameters indicated its high efficiency in the hydrolysis of xylan and its potential effectiveness in lignocellulosic hydrolysis and other industrial application. It also suggests the potential of xylanase enzyme for production of XOS from biomass which are useful in food and pharmaceutical industries.

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Section: Resultssupporting

confidence: 73%

Paecilomyces variotii xylanase production, purification and characterization with antioxidant xylo-oligosaccharides production

Abdella

Ramadan

Hamouda

et al. 2021

Sci Rep

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“…These differences were related to the optimum enzyme activity temperature ( Figure 1). The more marked effect on DON when α-amylase was present at 30 ºC was related to the activity of the α-amylase from Aspergillus oryzae (Evstatieva, Nikolova, Ilieva, Getov, & Savov, 2010 Chen, Chen, & Lin, 1997). The enzyme activity was also important because the breads with higher initial enzyme concentration (2.5 U/g initial concentration added, > 1. baking has been shown to be higher at higher initial toxin concentrations and not significant at lower initial DON concentrations (Vidal et al, 2014a(Vidal et al, , 2015.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Effect of xylanase and α-amylase on DON and its conjugates during the breadmaking process

Vidal

Sanchís

Ramos

et al. 2017

Food Research International

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Deoxynivalenol (DON) is one of the most frequently occurring mycotoxins in wheat crops worldwide and poses a risk to human and animal health due to its wide range of adverse effects. Deoxynivalenol-3-glucoside (DON-3-glucoside) is a DON plant conjugate that is widely found in cereal products. As DON accumulation in the field seems unavoidable, it is important to investigate all of the conditions that affect its stability during food processing. One of the most consumed cereal product around the world is bread, however the published information about DON stability in bread shows a large variability of results because a huge amount of factors affect DON and its modified forms. So, the aim of this research was to study the fate of DON and its modified forms through the breadmaking process with the addition of xylanase and α-amylase at different fermentation temperatures. Moreover, different α-amylase and xylanase concentrations were added to the dough to be fermented. To quantify DON and its derived forms in the samples, liquid chromatography with double mass spectrophotometer was used. DON was reduced during fermentation and baking; however, the reduction at each step was related to the fermentation temperature. The presence of α-amylase and xylanase caused increases in DON during fermentation and during early baking. DON-3-glucoside was slightly reduced after fermentation and was widely increased (>80%) after baking. Deepoxy-deoxynivalenol (DOM-1) increased during the breadmaking process. Breadmaking process can reduce DON concentration, however xylanase and α-amylase presence cause increases of DON.

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“…in solid state fermentation (SSF) ( Pal and Khanum, 2010 ). Many reports on xylanases from Bacillus spp., Streptomyces spp., Aspergillus spp., Trichoderma spp., and other microorganisms are available ( Krisana et al , 2005 ; Evstatieva et al , 2010 ). Trichoderma harzianum is present in all soil types and are the most prevalent culturable fungi.…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of a Xylanase-producing fungus isolated from fouled soil

Sakthiselvan¹,

Naveena²,

Partha³

2014

Braz. J. Microbiol.

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Xylanase (EC 3. 2. 1. 8), hydrolyzes xylo-oligosaccharides into D-xylose and required for complete hydrolysis of native cellulose and biomass conversion. It has broad range of applications in the pulp and paper, pharmaceutical and Agri-food industries. Fifty fungal species were isolated from the fouled soil around an oil refinery and screened for the production of xylanase enzyme by enrichment culture techniques. The isolated fungal strain was identified as Hypocrea lixii SS1 based on the results of biochemical tests and 18s rRNA sequencing. The phylogenetic tree was constructed using the MEGA 5 software. Further, Hypocrea lixii SS1 was tested for the ability to utilize the sunflower oil sludge (waste from the oil industry) as the sole carbon source for xylanase production. The growth characteristics of Hypocrea lixii SS1 were also studied and maximum growth was found on the 7th day of incubation. The fungus showed a remarkable xylanase production of 38.9 U/mL. Xylanase was purified using a combination of 0–50% NH4SO2 precipitation, DEAE-sepharose and Sephacryl S-200 chromatography. Single peak obtained in RP-HPLC confirms the purity of xylanase. Further the enzyme produced was affirmed as xylanase with its molecular weight (29 kDa) using SDS-PAGE.

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Identification and Characterization of α-Amylase and Endoxylanase, Produced byAspergillusMutant Strains

Abstract: ABSTRACT

Cited by 7 publications

References 12 publications

Paecilomyces variotii xylanase production, purification and characterization with antioxidant xylo-oligosaccharides production

Paecilomyces variotii xylanase production, purification and characterization with antioxidant xylo-oligosaccharides production

Effect of xylanase and α-amylase on DON and its conjugates during the breadmaking process

Molecular characterization of a Xylanase-producing fungus isolated from fouled soil

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