Synergistic action of Penicillium camemberti and Yarrowia lipolytica lipases in milk fat hydrolysis

Jully Lacerda Fraga

ORCID iD Universidade Federal do Rio de Janeiro (UFRJ) Brasil

Adrian Bezerra Penha

Universidade Federal do Rio de Janeiro (UFRJ) Brasil

Kelly Alencar Silva

ORCID iD Universidade Federal Fluminense (UFF) Brasil

Priscilla Filomena Fonseca Amaral

ORCID iD Universidade Federal do Rio de Janeiro (UFRJ) Brasil

Resumo

Lipolyzed Milk Fat (LMF) is a very important ingredient in food industry by acting as an additive (taste and aroma) in bakery, dairy and candy products. LMF can be produced by enzymatic route using lipases. Lipases from microorganisms are capable of promoting the hydrolysis of milk fat and can be obtained by fermenting processes with yeasts, such as Yarrowia lipolytica. In the present work, a commercial lipase obtained from Penicillium camemberti was tested for LMF production, as well as the enzyme extract produced in a 3L-bioreactor by Y. lipolytica. The highest lipase activity detected during Y. lipolytica growth was 6.278 U/L in 51 h. Different esters chain length were hydrolyzed by the lipases of Y. lipolytica (LipYl) and P. camemberti (LipPc) in two distinct type-emulsions (Arabic gum or Tween 20). Higher activity (5.890 U/L) was observed in the hydrolysis promoted by Y. lipolytica in milk fat emulsion with Arabic gum. The combination of both enzymes was effective in promoting hydrolysis in Arabic gum (1.77 Mol of LMF). The aim of this study was to evaluate a possible synergistic action between the lipases of P. Camemberti and Y. lipolytica in the hydrolysis of milk fat, in order to generate a LMF with a greater variety of fatty acids short chain. Thus, through this work it was possible to estimate a possible complementary action of lipases that can generate a greater range of fatty acids during the production of LMF.

Palavras-chave


Enzymes; Lipolytic activity; Lipolyzed Milk Fat; Biotechnology; Microorganisms


Texto completo:

Referências


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DOI: http://dx.doi.org/10.18265/1517-03062015v1n50p47-53

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