Polyhydroxyalkanoates (PHAs) are polyesters of microbial origin that can be synthesized by prokaryotes from noble sugars or lipids and from complex renewable substrates. They are an attractive alternative to conventional plastics because they are biodegradable and can be produced from renewable resources, such as the surplus of whey from dairy companies. After an in silico screening to search for ß-galactosidase and PHA polymerase genes, several bacteria were identified as potential PHA producers from whey based on their ability to hydrolyse lactose. Among them, Caulobacter segnis DSM 29236 was selected as a suitable strain to develop a process for whey surplus valorization. This microorganism accumulated 31.5% of cell dry weight (CDW) of poly(3-hydroxybutyrate) (PHB) with a titre of 1.5 g l in batch assays. Moreover, the strain accumulated 37% of CDW of PHB and 9.3 g l in fed-batch mode of operation. This study reveals this species as a PHA producer and experimentally validates the in silico bioprospecting strategy for selecting microorganisms for waste re-valorization.
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http://dx.doi.org/10.1111/1751-7915.13371 | DOI Listing |
Chembiochem
November 2023
Department of Food, Environmental and Nutritional Sciences (DeFENS), University of Milan, via Celoria, 2, 20133, Milan, Italy.
Ozonolysis is a useful as well as dangerous reaction for performing alkene cleavage. On the other hand, enzymes are considered a more sustainable and safer alternative. Among them, Caulobacter segnis dioxygenase (CsO2) known so far for its ability to catalyze the coenzyme-free oxidation of vinylguaiacol into vanillin, was selected and its substrate scope evaluated towards diverse natural and synthetic stilbenoids.
View Article and Find Full Text PDFCurr Microbiol
August 2021
Department of Biological Sciences, University of South Carolina, Columbia, SC, 29208, USA.
Genomic sequencing has vastly expedited our understanding of bacterial functions. However, the genomes of many plant-growth-promoting bacteria (PGPB) have yet to be sequenced and contextualized. To this end, I report the sequenced genome of a PGPB-Caulobacter segnis CBR1-and contextualize its genomic features with the genomic features of sequenced Caulobacter strains.
View Article and Find Full Text PDFInt J Syst Evol Microbiol
July 2020
College of Biology and the Environment, Co-Innovation Centre for Sustainable Forestry in Southern China, Nanjing Forestry University, Nanjing 210037, PR China.
A Gram-stain-negative, yellow-pigmented, aerobic, non-spore-forming, motile with a single polar flagellum and rod-shaped bacterium, Ji-3-8, was isolated from a soil sample taken from Jiri Mountain, Republic of Korea. Comparative 16S rRNA gene sequence studies showed the isolate had clear affiliation with and the closest relatedness to KCTC 52515, ATCC 15253, ATCC 21756, THG-AG3.4, RHGG3 and CB51 showing 99.
View Article and Find Full Text PDFJ Biosci Bioeng
September 2020
Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, Tokyo 169-8555, Japan. Electronic address:
Vanillin is a well-known fragrant, flavoring compound. Previously, we established a method of coenzyme-independent vanillin production via an oxygenase from Caulobacter segnis ATCC 21756, called Cso2, that converts 4-vinylguaiacol to vanillin and formaldehyde using oxygen. In this study, we found that reactive oxygen species inhibited the catalytic activity of Cso2, and the addition of catalase increased vanillin production.
View Article and Find Full Text PDFAppl Microbiol Biotechnol
May 2020
Laboratory of Food Enzyme Engineering, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing, 100193, People's Republic of China.
Vanillin is a popular flavoring compound and an important food additive. Owing to the consumer preference for inexpensive natural aroma flavors, vanillin production through a biotechnological pathway has become of great interest and commercial value in recent years. In this study, an enzymatic synthetic system for vanillin using a coenzyme-independent decarboxylase (FDC) and oxygenase (CSO2) cascade was reconstituted and optimized.
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