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1.
Food Technol Biotechnol ; 56(3): 354-365, 2018 Sep.
Article in English | MEDLINE | ID: mdl-30510479

ABSTRACT

The aim of this research is to isolate and identify fungi with high lignin-degrading abilities that are autochthonous to southern Serbian region. Two novel fungal isolates identified as Trametes hirsuta F13 and Stereum gausapatum F28 were selected to assess their ligninolytic enzyme activities and the efficiency of lignin removal from beech wood sawdust. Obtained results show that both isolates are good sources of industrially valuable enzymes with a potential for application in various biotechnological and industrial processes. Both isolates showed laccase, manganese-dependent peroxidase, and versatile peroxidase activities, while only S. gausapatum F28 had lignin peroxidase activity. This is the first record of the ability of S. gausapatum species to produce lignin peroxidase. T. hirsuta F13 showed higher laccase activity than S. gausapatum F28, while S. gausapatum F28 had higher manganese peroxidase activity. Also, T. hirsuta F13 exhibited much higher laccase activity under submerged cultivation conditions than solid-state cultivation conditions, which is rare for fungi. This is important for industrial processes since the submerged fermentation is a dominant technique in industry. The test of the efficiency of lignin removal showed that both isolates are efficient lignin decomposers. After five weeks of incubation on beech wood sawdust, the total lignin losses were 33.84% with T. hirsuta F13 and 28.8% with S. gausapatum F28.

2.
Int J Biol Macromol ; 107(Pt B): 1856-1863, 2018 Feb.
Article in English | MEDLINE | ID: mdl-29032209

ABSTRACT

This study has explored the possibility to reuse the waste, spent coffee material for the cellulase enzyme immobilization. By the coffee surface modification with different activating agents, it was attempted to develop the convenient method for creation of a capable porous carrier for this purpose. Among the most common activating agents, glutaraldehyde, chlorine dioxide and hydrogen peroxide provided the most acceptable choice for the coffee surface modification. The changes that occurred on the coffee surface due to agents' treatment exposure were recorded by using of the FTIR spectra and SEM micrographs. The highest immobilization yield (55%) and immobilization efficiency (45%) were attained during 30min of the treatment time, by employing of 30% chlorine dioxide aqueous solution within 6mL/g activator/carrier ratio. The kinetic process was found to be predicted by the pseudo-second-order model. The cellulase immobilization onto the coffee surface provides an excellent base for increasing the enzyme availability to the substrate and enhancing the enzyme productivity, by offering the new perspectives to the industrial sector.


Subject(s)
Cellulase/metabolism , Coffee/chemistry , Enzyme Activators/pharmacology , Enzymes, Immobilized/metabolism , Trichoderma/enzymology , Adsorption , Kinetics , Spectroscopy, Fourier Transform Infrared , Temperature , Time Factors
3.
Heliyon ; 2(8): e00146, 2016 Aug.
Article in English | MEDLINE | ID: mdl-27626091

ABSTRACT

This study has explored the feasibility of using spent coffee grounds as a good supporting material for the Paenibacillus chitinolyticus CKS1 cellulase immobilization. An optimal operational conditions in a batch-adsorption system were found to be: carrier mass of 12 g/L, under the temperature of 45 °C and no pH adjustments. The immobilization yield reached about 71%. An equilibrium establishment between the cellulase and the carrier surface occurred within 45 min, whereas the process kinetics may be predicted by the pseudo-second-order model. An immobilized cellulase preparation expressed very good avicelase activity, this reached up to 2.67 U/g, and revealed an improved storage stability property, compared to free enzyme sample counterpart. The addition of metal ions, such as K(+) and Mg(2+) did not affect positively immobilization yield results, but on the contrary, contributed to an improved bio-activities of the immobilized cellulase, thus may be employed before each enzyme application. The method developed in this study offers a cheap and effective alternative for immediate enzyme isolation from the production medium and its stabilization, compared to other carriers used for the immobilization.

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