Name: JULIO PANSIERE ZAVARISE
Publication date: 09/11/2021
Advisor:
Name |
Role |
|---|---|
| LAURA MARINA PINOTTI | Advisor * |
Examining board:
| Name |
Role |
|---|---|
| JAIRO PINTO DE OLIVEIRA | Advisor * |
| LAURA MARINA PINOTTI | Advisor * |
| PAULO SÉRGIO DA SILVA PORTO | Advisor * |
Summary: Lipases are common enzymes that catalyze hydrolysis reactions or synthesis of
long-chain acylglycerols. These enzymes can be obtained from plants, animals,
and microorganisms such as bacteria and filamentous fungi. The production of
lipases by filamentous fungi is widely described in the literature and it is known
that they can produce extracellular and intracellular lipases (mycelium -bound
lipases) and that these lipases may present distinct characteristics. Fungal
biomass and broth fermented with lipasic activity can be biocatalysts in
applications such as biodiesel synthesis and in the treatment of fatty effluents.
The greatest advantage of the afore mentioned enzymes in the face of purified
enzymes is the low relative cost of obtaining, by eliminating complex purification
steps. Therefore, the objective of this work is to study the production potential of
intracellular and extracellular lipases from three fungal strains (Aspergillus niger,
Penicillium spp. and Trichoderma koningii) and to perform biochemical
characterization of the lipases produced. The results obtained indicate that T.
koningii presented the maximum intracellular lipasic activity (81.5 IU/g of dry
biomass), while the maximum extracellular lipasic activity (10.6 IU/mL of
fermented broth) was found for A. niger, both activities attained after 96 h of
fermentation. The analysis of specific activities (ratio between lipase activity and
dry biomass concentration) indicated that Trichoderma presented a differentiated
behavior in relation to the other microorganisms studied, with indications that
there is a strong retention of lipases in mycelium. The values of the kinetic
parameters determined for the lipases produced, with the emulsion of commercial
olive oil as substrate, ranged from 68.24 to 469.04 mM for Km and from 5.58 to
37.88 IU for Vmax. Statistical analysis of the effects of the factors (temperature
and pH) on lipasic activity indicated that the effect of pH on the lipasic activity of
the mycelia of T. koningii was about 13 times greater than the effect of
temperature. It was noted that the reactional temperatures in the range of 37°C
to 44°C and the pH from 7.8 to 8.0 favored the lipase strain activity of lipases
produced by T. koningii.
Keywords: Filamentous fungi. Lipases. Mycelia. Biochemical Characterization
