@article {1198,
	title = {Determination of polydextrose as dietary fiber in foods.},
	journal = {J AOAC Int},
	volume = {83},
	year = {2000},
	month = {2000 Jul-Aug},
	pages = {1006-12},
	abstract = {<p>Polydextrose (Litesse) provides physiological effects consistent with dietary fiber. However, AOAC methods for measuring total dietary fiber (TDF) in foods include an ethanol precipitation step in which polydextrose and similar carbohydrates are discarded and therefore not quantitated. This study describes a method developed to quantitate polydextrose in foods. The new method includes water extraction, centrifugal ultrafiltration, multienzyme hydrolysis, and anion exchange chromatography with electrochemical detection. Six foods were prepared with 4 levels of polydextrose to test the ruggedness of the method. Internal validation demonstrated the ruggedness of the method with recoveries ranging from 83 to 104\% with an average of 95\% (n = 24) and relative standard deviation of recoveries ranging from 0.7 to 13\% with an average of 3.3\% (n = 24). The value is added to that obtained for dietary fiber content of foods using the AOAC methods, to determine the TDF content of the food.</p>},
	keywords = {Animals, Anions, Bacterial Proteins, Beverages, Cacao, Candy, Chromatography, Ion Exchange, Dietary Fiber, Ethanol, Food Analysis, Glucan 1,4-alpha-Glucosidase, Glucans, Glycoside Hydrolases, Humans, Hydrolysis, Isoamylase, Tea, Ultrafiltration},
	issn = {1060-3271},
	author = {Craig, S A and Holden, J F and Khaled, M Y and Craig, S A and Holden, J F and Khaled, M Y}
}
@article {1197,
	title = {Overview of hyperthermophiles and their heat-shock proteins.},
	journal = {Adv Protein Chem},
	volume = {48},
	year = {1996},
	month = {1996},
	pages = {1-34},
	keywords = {Archaea, Bacterial Proteins, Heat-Shock Proteins, Hot Temperature, Phylogeny},
	issn = {0065-3233},
	author = {Baross, J A and Holden, J F}
}
@article {1196,
	title = {Enhanced thermotolerance and temperature-induced changes in protein composition in the hyperthermophilic archaeon ES4.},
	journal = {J Bacteriol},
	volume = {175},
	year = {1993},
	month = {1993 May},
	pages = {2839-43},
	abstract = {<p>The hyperthermophilic archaeon ES4, a heterotrophic sulfur reducer isolated from a deep-sea hydrothermal vent, is capable of protecting itself from thermal stress at temperatures above its optimum for growth. The thermotolerance of ES4 was determined by exposing log-phase cells to various lethal high temperatures. When ES4 was shifted from 95 to 102 degrees C, it displayed recovery from an exponential rate of death, followed by transient thermotolerance. When ES4 was shifted directly from 95 to either 105 or 108 degrees C, only exponential death occurred. However, a shift from 95 to 105 degrees C with an intermediate incubation at 102 degrees C also gave ES4 transient thermotolerance to 105 degrees C. The protein composition of ES4 was examined at temperatures ranging from 75 to 102 degrees C by one-dimensional electrophoresis. Two proteins with molecular masses of approximately 90 and 150 kDa significantly decreased in abundance with increasing growth temperature, while a 98-kDa protein, present at very low levels at normal growth temperatures (76 to 99 degrees C), was more abundant at higher temperatures. The enhanced tolerance to hyperthermal conditions after a mild hyperthermal exposure and the increased abundance of the 98-kDa protein at above-optimal temperatures imply that ES4 is capable of a heat shock-like response previously unseen in hyperthermophilic archaea.</p>},
	keywords = {Archaea, Bacterial Proteins, Blotting, Western, Electrophoresis, Polyacrylamide Gel, Hot Temperature},
	issn = {0021-9193},
	author = {Holden, J F and Baross, J A}
}
