@article {2147,
	title = {Identification of the wax ester synthase/acyl-coenzyme A: Diacylglycerol acyltransferase WSD1 required for stem wax ester biosynthesis in Arabidopsis},
	journal = {Plant Physiology},
	volume = {148},
	number = {1},
	year = {2008},
	note = {ISI Document Delivery No.: 344SMTimes Cited: 16Cited Reference Count: 52Li, Fengling Wu, Xuemin Lam, Patricia Bird, David Zheng, Huanquan Samuels, Lacey Jetter, Reinhard Kunst, Ljerka},
	month = {Sep},
	pages = {97-107},
	type = {Article},
	abstract = {Wax esters are neutral lipids composed of aliphatic alcohols and acids, with both moieties usually long-chain (C-16 and C-18) or very-long-chain (C-20 and longer) carbon structures. They have diverse biological functions in bacteria, insects, mammals, and terrestrial plants and are also important substrates for a variety of industrial applications. In plants, wax esters are mostly found in the cuticles coating the primary shoot surfaces, but they also accumulate to high concentrations in the seed oils of a few plant species, including jojoba (Simmondsia chinensis), a desert shrub that is the major commercial source of these compounds. Here, we report the identification and characterization of WSD1, a member of the bifunctional wax ester synthase/diacylglycerol acyltransferase gene family, which plays a key role in wax ester synthesis in Arabidopsis (Arabidopsis thaliana) stems, as first evidenced by severely reduced wax ester levels of in the stem wax of wsd1 mutants. In vitro assays using protein extracts from Escherichia coli expressing WSD1 showed that this enzyme has a high level of wax synthase activity and approximately 10-fold lower level of diacylglycerol acyltransferase activity. Expression of the WSD1 gene in Saccharomyces cerevisiae resulted in the accumulation of wax esters, but not triacylglycerol, indicating that WSD1 predominantly functions as a wax synthase. Analyses of WSD1 expression revealed that this gene is transcribed in flowers, top parts of stems, and leaves. Fully functional yellow fluorescent protein-tagged WSD1 protein was localized to the endoplasmic reticulum, demonstrating that biosynthesis of wax esters, the final products of the alcohol-forming pathway, occurs in this subcellular compartment.},
	keywords = {ABC, CLONING, CONDENSING ENZYME, ELONGATION, GENE-EXPRESSION, PLANT CUTICULAR WAXES, SURFACES, THALIANA, TRANSFORMATION, TRANSGENIC ARABIDOPSIS, TRANSPORTER},
	isbn = {0032-0889},
	url = {<Go to ISI>://000258947600010},
	author = {Li, F. and Wu, X. and Lam, P. and Bird, D. and Zheng, H. and Samuels, L. and Jetter, R. and Kunst, L.}
}
@article {3984,
	title = {On-line monitoring and control of methanol concentration in shake-flask cultures of Pichia pastoris},
	journal = {Biotechnology and Bioengineering},
	volume = {56},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: XZ728Times Cited: 48Cited Reference Count: 19},
	month = {Nov},
	pages = {279-286},
	type = {Article},
	abstract = {The methylotrophic yeast Pichia pastoris can be used to express recombinant genes at high levels under the control of the methanol-inducible alcohol oxidase 1 (AOX1) promoter. Accurate regulation of the methanol concentration in P. pastoris cultures is necessary to maintain induction, while preventing accumulation of methanol to cytotoxic levels. We developed an inexpensive methanol sensor that uses a gas-permeable silicone rubber tube immersed in the culture medium and an organic solvent vapor detector. The sensor was used to monitor methanol concentration continuously throughout a fed-batch shake-flask culture of a P. pastoris clone producing the N-lobe of human transferrin. The sensor calibration was stable for the duration of the culture and the output signal accurately reflected the methanol concentration determined off-line by HPLC. A closed-loop control system utilizing this sensor was developed and used to maintain a 0.3\% (v/v) methanol concentration in the culture. Use of this system resulted in a fivefold increase in volumetric protein productivity over levels obtained using the conventional fed-batch protocol. (C) 1997 John Wiley \& Sons, Inc.},
	keywords = {fermentation, GENE-EXPRESSION, methanol monitoring and control, methanol sensor, methylotrophic yeast, Pichia pastoris, PROTEINS, SEMICONDUCTOR GAS SENSORS, shake-flask cultures, TRANSFERRIN, YEAST},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1997XZ72800005},
	author = {Guarna, M. M. and Lesnicki, G. J. and Tam, B. M. and Robinson, J. and Radziminski, C. Z. and Hasenwinkle, D. and Boraston, A. and Jervis, E. and MacGillivray, R. T. A. and Turner, R. F. B. and Kilburn, D. G.}
}
