Use of Yarrowia lipolytica Lipase Immobilized in Cell Debris for the Production of Lipolyzed Milk Fat (LMF).

Jully L Fraga,Kelly A Silva,Adejanildo Da S Pereira,Emília Akil,Alexandre G Torres,Adrian C B Penha,Priscilla F F Amaral

doi:10.3390/ijms19113413

Jully L Fraga, Kelly A Silva + Show 5 more

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https://doi.org/10.3390/ijms19113413

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Abstract

Lipase immobilized on Yarrowia lipolytica cell debris after sonication of yeast cells (LipImDebri) was used in hydrolysis reaction as a novel strategy to produce lipolyzed milk fat (LMF). Extracellular (4732.1 U/L), intracellular (130.0 U/g), and cell debris (181.0 U/g) lipases were obtained in a 4 L bioreactor using residual frying oil as inducer in 24 h fermentation process. LipImDebri showed a good operational stability retaining 70% of lipolytic activity after the second cycle and 40% after the fourth. The highest degree of hydrolysis (28%) was obtained with 500 mg LipImDebri for 6 h of lipolysis of anhydrous milk fat. LMF produced with LipImDebri presented high contents of oleic (35.2%), palmitic (25.0%), and stearic (15.4%) acids and considerable amounts of odor-active short and medium chain fatty acids (C:4–C:10) (8.13%).

Highlights

For many years enzymes have been used in biotechnological processes as catalysts in several industrial sectors, mainly in food production [1]
Production of Lipase from Y. lipolytica Immobilized in Cell Debris Induced by Residual Frying Oil
The lipase that remained attached to cell debris after sonication (LipImDebri) showed a potential to be used as an immobilized enzyme that could be reused for four times with more than 40% residual hydrolytic activity

Summary

Introduction

For many years enzymes have been used in biotechnological processes as catalysts in several industrial sectors, mainly in food production [1]. The use of enzymes presents advantages in comparison to chemical catalysts such as mild reaction conditions and versatility [2]. Most lipases exhibit a catalytic mechanism that differentiates them from standard esterases, by the presence of two different conformations in equilibrium. A closed form (inactive) is observed when no hydrophobic surface is available and is characterized by a “lid” of helicoidal polypeptide chain that closes the catalytic site, making it inaccessible to the reaction medium. The open form (active), where this lid is entirely displaced, occurs in the presence of hydrophobic surfaces [4]

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