Optimized expression of the Starmerella bombicola lactone esterase in Pichia pastoris through temperature adaptation, codon-optimization and co-expression with HAC1

Waele, Stijn De; Vandenberghe, Isabel; Laukens, Bram; Planckaert, Sören; Verweire, Stijn; Bogaert, Inge Van; Soetaert, Wim; Devreese, Bart; Ciesielska, Katarzyna

doi:10.1016/j.pep.2017.10.016

Cited by 17 publications

(10 citation statements)

References 41 publications

(60 reference statements)

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“…The protein Hac1 is a transcription regulator involved in the unfolded protein response (UPR), which increases the synthesis of endoplasmic reticulum resident proteins required for protein folding, as well as components of the secretory pathway [74,82]. Overexpression of this transcription factor has proven to be a very important tool to increase the production yield of different recombinant proteins [81,85,86,[89][90][91][92][93][94]. Huang et al [93] evaluated the effect of HAC1p on a raw starch hydrolysing α-amylase (Gs4j-amyA) to improve heterologous production of the enzyme in K. phaffii, further evaluating the variation in copy number and promoter used in the overexpression of HAC1 [93].…”

Section: Transcription Factor Engineering In K Phaffii For Recombinan...mentioning

confidence: 99%

Advances in Cell Engineering of the Komagataella phaffii Platform for Recombinant Protein Production

et al. 2022

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Komagataella phaffii (formerly known as Pichia pastoris) has become an increasingly important microorganism for recombinant protein production. This yeast species has gained high interest in an industrial setting for the production of a wide range of proteins, including enzymes and biopharmaceuticals. During the last decades, relevant bioprocess progress has been achieved in order to increase recombinant protein productivity and to reduce production costs. More recently, the improvement of cell features and performance has also been considered for this aim, and promising strategies with a direct and substantial impact on protein productivity have been reported. In this review, cell engineering approaches including metabolic engineering and energy supply, transcription factor modulation, and manipulation of routes involved in folding and secretion of recombinant protein are discussed. A lack of studies performed at the higher-scale bioreactor involving optimisation of cultivation parameters is also evidenced, which highlights new research aims to be considered.

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Section: Transcription Factor Engineering In K Phaffii For Recombinan...mentioning

confidence: 99%

Advances in Cell Engineering of the Komagataella phaffii Platform for Recombinant Protein Production

et al. 2022

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“…Parekh et al [124] obtained similar SLs concentration (18.2 g/L) using S. bombicola NRRL Y-17069 and determining the optimal fermentation method to generate these surfactant compounds. Recently, a novel lactone esterase enzyme from S. bombicola, which catalyzes the intramolecular lactonization of acidic SLs in an aqueous environment, is being investigated to become an ecological tool in industry applications [127].…”

Section: Production Of Sophorolipids Biosurfactants By Candidamentioning

confidence: 99%

Advances in the Study of Candida stellata

García¹,

Esteve-Zarzoso

Cabellos³

et al. 2018

Fermentation

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Candida stellata is an imperfect yeast of the genus Candida that belongs to the order Saccharomycetales, while phylum Ascomycota. C. stellata was isolated originally from a must overripe in Germany but is widespread in natural and artificial habitats. C. stellata is a yeast with a taxonomic history characterized by numerous changes; it is either a heterogeneous species or easily confused with other yeast species that colonize the same substrates. The strain DBVPG 3827, frequently used to investigate the oenological properties of C. stellata, was recently renamed as Starmerella bombicola, which can be easily confused with C. zemplinina or related species like C. lactis-condensi. Strains of C. stellata have been used in the processing of foods and feeds for thousands of years. This species, which is commonly isolated from grape must, has been found to be competitive and persistent in fermentation in both white and red wine in various wine regions of the world and tolerates a concentration of at least 9% (v/v) ethanol. Although these yeasts can produce spoilage, several studies have been conducted to characterize C. stellata for their ability to produce desirable metabolites for wine flavor, such as acetate esters, or for the presence of enzymatic activities that enhance wine aroma, such as β-glucosidase. This microorganism could also possess many interesting technological properties that could be applied in food processing. Exo and endoglucosidases and polygalactosidase of C. stellata are important in the degradation of β-glucans produced by Botrytis cinerea. In traditional balsamic vinegar production, C. stellata shapes the aromatic profile of traditional vinegar, producing ethanol from fructose and high concentrations of glycerol, succinic acid, ethyl acetate, and acetoin. Chemical characterization of exocellular polysaccharides produced by non-Saccharomyces yeasts revealed them to essentially be mannoproteins with high mannose contents, ranging from 73–74% for Starmerella bombicola. Numerous studies have clearly proven that these macromolecules make multiple positive contributions to wine quality. Recent studies on C. stellata strains in wines made by co-fermentation with Saccharomyces cerevisiae have found that the aroma attributes of the individual strains were apparent when the inoculation protocol permitted the growth and activity of both yeasts. The exploitation of the diversity of biochemical and sensory properties of non-Saccharomyces yeast could be of interest for obtaining new products.

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“…SBLE was recombinantly produced in P. pastoris [ 15 , 27 ]. This rSBLE was used to assess catalytic activity and to determine specificity.…”

Section: Introductionmentioning

confidence: 99%

Revision of the sophorolipid biosynthetic pathway in Starmerella bombicola based on new insights in the substrate profile of its lactone esterase

Diao,

Roelants,

Luyten

et al. 2024

Biotechnol Biofuels

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Background Sophorolipids (SLs) are a class of natural, biodegradable surfactants that found their way as ingredients for environment friendly cleaning products, cosmetics and nanotechnological applications. Large-scale production relies on fermentations using the yeast Starmerella bombicola that naturally produces high titers of SLs from renewable resources. The resulting product is typically an extracellular mixture of acidic and lactonic congeners. Previously, we identified an esterase, termed Starmerella bombicola lactone esterase (SBLE), believed to act as an extracellular reverse lactonase to directly use acidic SLs as substrate. Results We here show based on newly available pure substrates, HPLC and mass spectrometric analysis, that the actual substrates of SBLE are in fact bola SLs, revealing that SBLE actually catalyzes an intramolecular transesterification reaction. Bola SLs contain a second sophorose attached to the fatty acyl group that acts as a leaving group during lactonization. Conclusions The biosynthetic function by which the Starmerella bombicola ‘lactone esterase’ converts acidic SLs into lactonic SLs should be revised to a ‘transesterase’ where bola SL are the true intermediate. This insights paves the way for alternative engineering strategies to develop designer surfactants.

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Optimized expression of the Starmerella bombicola lactone esterase in Pichia pastoris through temperature adaptation, codon-optimization and co-expression with HAC1

Cited by 17 publications

References 41 publications

Advances in Cell Engineering of the Komagataella phaffii Platform for Recombinant Protein Production

Advances in Cell Engineering of the Komagataella phaffii Platform for Recombinant Protein Production

Advances in the Study of Candida stellata

Revision of the sophorolipid biosynthetic pathway in Starmerella bombicola based on new insights in the substrate profile of its lactone esterase

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