a b s t r a c t ␥-Decalactone production from ricinoleic acid biotransformation by Yarrowia lipolytica has drawn the attention of many authors and, in the last years, molecular and physiological developments were made through the use of engineered strains in novel culture conditions.The purpose of this work was to monitor the performance of modified Y. lipolytica strains in their lipid metabolism specifically at the -oxidation pathway (MTLY40-2P strain, disrupted in the native genes POX2-5 and expressing an ectopic Aox2p-encoding gene) or at the triglyceride hydrolysis (JMY3010 strain, Lip2p overexpressed) using castor oil as substrate, in a lab-scale bioreactor. Using step-wise fedbatch cultures of MTLY40-2P strain, a ␥-decalactone concentration of 7 g L −1 was reached. ␥-Decalactone reconsumption was prevented and hydroxylactone production was reduced by Y. lipolytica MTLY40-2P strain. Moreover, substantial increase in the initial rate of aroma production was obtained with strain overexpressing LIP2 gene due to the fast hydrolysis of castor oil.
bIL41 and bIL170, virulent phages of Lactococcus lactis belonging to the 936 group, possess a late gene named l12, coding a putative fiber sharing partial similarity to diverse gene products of dairy phages, including host-range determinants, but whose function is unknown in this group. We observed that the full-size gpl12 gene product is a minor protein constitutive of both phage particles. A derivative of bIL41 deleted for part of this gene was constructed by homologous recombination. The recombinant bIL41DeltaL12 showed normal propagation on strain IL1403 and no altered head and tail structures, demonstrating its non-essential role under our laboratory conditions. bIL170 was investigated for major structural components. Tails were characterized by electron microscopy and image analysis, which indicated that the major repeat unit of the tail occupied a maximum volume of 18.5 nm3, corresponding to a size of 20 kDa for a globular protein. Total protein profiles and head-enriched fractions of bIL170 exhibited a major 38 kDa protein, identified by N-terminal sequence as the product of l13. This result questions some of the functional predictions deduced from synteny relationships assumed for the lambda-supergroup of the family Siphoviridae to which the 936-type phages were proposed to belong.
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