Characterization of an acid-tolerant β-1,4-glucosidase from Fusarium oxysporum and its potential as an animal feed additive

Zhao, Zhong; Ramachandran, Priyadharsini; Kim, Taesu; Chen, Zhilei; Jeya, Marimuthu; Lee, Jung-Kul

doi:10.1007/s00253-013-4767-3

Cited by 12 publications

(7 citation statements)

References 28 publications

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“…These changes along with viscosity reduction may result in better digestion and higher feed conversion ratio (FCR) in poultry. This is in agreement with the results of other researchers who observed that adding the enzyme to the poultry feed would improve digestion and eliminate digestive problems (Tervila-Wilo et al, 1996;Teymouri et al, 2018;Zhao et al, 2013).…”

Section: Effect Of the Enzyme On The Structure Of Cereal Grainssupporting

confidence: 93%

Investigation of the effects of fermented wheat bran extract containing beta‐glucanase on beta‐glucan of cereals used in animal feed

et al. 2021

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Background and objectives Beta‐glucan found in cereals is a non‐nutrient for poultry that would cause some digestion problems. Beta‐glucanase can break down the beta‐glucan. The aim was the production of beta‐glucanase from the fermentation of wheat bran and to investigate its effects on cereals. Findings Beta‐glucan contents of cereals, that is, wheat variety Pishtaz, hulless barley variety Loot, and a variety of medium maturity corn, were measured by direct extraction and beta‐glucan measurement kit. Beta‐glucanase was produced by solid‐state cultivation of five strains of Aspergillus on wheat bran. Aspergillus niger CCUG33991 was selected for the production of enzyme extract. Adding the extract enhanced the suspension viscosity reduction for the tested cereals. Barley had the highest amount of beta‐glucan and higher viscosity reduction that can be attributed to beta‐glucan content. Treatment of cereals with the enzyme extract modified their surfaces and made them more digestible. Conclusions The study demonstrated that beta‐glucanase can be a profitable animal feed additive especially for the feeds with high beta‐glucan content grains. Significance and novelty The effect of produced beta‐glucanase for the first time on the structure and solution viscosity of cereals showed that adding this enzyme is a suitable additive for digestive problems solving in animals.

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Section: Effect Of the Enzyme On The Structure Of Cereal Grainssupporting

confidence: 93%

Investigation of the effects of fermented wheat bran extract containing beta‐glucanase on beta‐glucan of cereals used in animal feed

et al. 2021

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“…The optimal temperature of the purified β‐glucosidase is 60 °C, which is similar to those of other known ones from some microorganisms, such as Fusarium oxysporum (60 °C) , Aspergillus fumigates (60 °C) , the protoplast fusant of Aspergillus oryzae and A. niger (65 °C) , and Colletotrichum graminicola (65 °C) . Compared to many acidic β‐glucosidases from Sporidiobolus pararoseus (pH 4.0) , A. niger (pH 4.0) , Penicillium aculeatum (pH 4.5) , Oenococcus oeni (pH 5.0–5.5) , and Endophytic fungi (pH 5.0 and 6.0) , the β‐glucosidase from Bacillus sp.…”

Section: Discussionsupporting

confidence: 53%

Optimization of a heat‐tolerant β‐glucosidase production by Bacillus sp. ZJ1308 and its purification and characterization

Zhang

2015

Biotech and App Biochem

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Response surface methodology was used to optimize the medium composition to improve the production of the heat-tolerant β-glucosidase from Bacillus sp. ZJ1308. Three significant factors were found to be corn cob, beef extract, and MnSO4 ·H2 O. The final medium compositions optimized were corn cob (51.8 g/L), beef extract (23.8 g/L), salicin (0.5 g/L), MnSO4 ·H2 O (0.363 g/L), MgSO4 ·7H2 O (0.4 g/L), and NaCl (5 g/L). Under the optimal conditions, the activity of β-glucosidase was up to 4.71 U/mL. β-Glucosidase was purified to homogeneity with a recovery rate of 5% and a specific activity of 110.47 U/mg. The optimal pH and temperature were 7.0 and 60 °C, respectively. β-Glucosidase was stable within a pH range of 6.0-8.0 and showed an extremely high thermostability at 80 and 90 °C, retaining 56% and 38% of its maximal activity, respectively. Ni(2+) and Ba(2+) heavily inhibited the β-glucosidase activity. The purified β-glucosidase showed a high substrate specificity. The kinetic parameters revealed that it had a high catalytic efficiency toward the substrate p-nitrophenyl-β-d-glucopyranoside (Kcat /Km = 700). It also showed a high catalytic activity toward the natural substrate salicin. This study provides a new insight into the future development and use of β-glucosidase from Bacillus sp. ZJ1308.

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“…Different Fusarium oxysporum species (more related to Fsh13) expressing different cellulases. The Fusarium oxysporum KCTC 16909 has one GH1, a β-glucosidase, [ 69 ] with 268 U/mg for the purified enzyme. Another Fusarium oxysporum [ 70 ] has at least two GH7, endoglucanases Cel7A [ 70 ] and Cel7B also known as endoglucanase I (PDB code 1OVW) [ 71 ].…”

Section: Discussionmentioning

confidence: 99%

A unique fungal strain collection from Vietnam characterized for high performance degraders of bioecological important biopolymers and lipids

et al. 2018

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Fungal strains are abundantly used throughout all areas of biotechnology and many of them are adapted to degrade complex biopolymers like chitin or lignocellulose. We therefore assembled a collection of 295 fungi from nine different habitats in Vietnam, known for its rich biodiversity, and investigated their cellulase, chitinase, xylanase and lipase activity. The collection consists of 70 isolates from wood, 55 from soil, 44 from rice straw, 3 found on fruits, 24 from oil environments (butchery), 12 from hot springs, 47 from insects as well as 27 from shrimp shells and 13 strains from crab shells. These strains were cultivated and selected by growth differences to enrich phenotypes, resulting in 211 visually different fungi. DNA isolation of 183 isolates and phylogenetic analysis was performed and 164 species were identified. All were subjected to enzyme activity assays, yielding high activities for every investigated enzyme set. In general, enzyme activity corresponded with the environment of which the strain was isolated from. Therefore, highest cellulase activity strains were isolated from wood substrates, rice straw and soil and similar substrate effects were observed for chitinase and lipase activity. Xylanase activity was similarly distributed as cellulase activity, but substantial activity was also found from fungi isolated from insects and shrimp shells. Seven strains displayed significant activities against three of the four tested substrates, while three degraded all four investigated carbon sources. The collection will be an important source for further studies. Therefore representative strains were made available to the scientific community and deposited in the public collection of the Leibniz-Institute DSMZ–German Collection of Microorganisms and Cell Cultures, Braunschweig.

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Characterization of an acid-tolerant β-1,4-glucosidase from Fusarium oxysporum and its potential as an animal feed additive

Cited by 12 publications

References 28 publications

Investigation of the effects of fermented wheat bran extract containing beta‐glucanase on beta‐glucan of cereals used in animal feed

Investigation of the effects of fermented wheat bran extract containing beta‐glucanase on beta‐glucan of cereals used in animal feed

Optimization of a heat‐tolerant β‐glucosidase production by Bacillus sp. ZJ1308 and its purification and characterization

A unique fungal strain collection from Vietnam characterized for high performance degraders of bioecological important biopolymers and lipids

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