This critical review article examines the composition and source of inulin and oligofructose, the physiological effects of their consumption, and how these materials relate to the concept of dietary fiber. Inulin and oligofructose are fructans extracted on a commercial basis from the chicory root. Inulin has been defined as a polydisperse carbohydrate material consisting mainly, if not exclusively, of beta (2-1) fructosyl-fructose links ranging from 2 to 60 units long. Native chicory inulin has an average degree of polymerization (DP) of 10 to 20, whereas oligofructose contains chains of DP 2 to 10, with an average DP of 4. While a universally accepted definition for dietary fiber does not exist, it is generally agreed that this term includes saccharides (+ lignin) that are not hydrolyzed or absorbed in the upper part of the gastrointestinal tract. These materials reach the colon, where they may be totally fermented, partially fermented, or remain unfermented. In addition, fibers contribute to fecal bulking. Inulin and oligofructose are not digested in the upper part of the gastrointestinal tract or are they absorbed and metabolized in the glycolytic pathway, or directly stored as glycogen like 'sugars' or starches. None of the molecules of fructose and glucose that form inulin and oligofructose appear in the portal blood. These materials are quantitatively fermented by the microflora of the colon; further, it has been demonstrated that this fermentation leads to the selective stimulation of the growth of the bifidobacteria population. After reviewing their chemistry, origin, and physiological effects, it is the opinion of the authors that inulin and oligofructose are dietary fiber. They share the basic common characteristics of dietary fibers, that is, saccharides of plant origin, resistance to digestion and absorption in the small intestine, and fermentation in the colon to produce short-chain fatty acids that are absorbed and metabolized in various parts of the body. Moreover, this fermentation induces a bulking effect.

Two heat-stable and trypsin-labile inhibitors of phosphorylase phosphatase, designated inhibitor-1 and inhibitor-2, were partially purified from extracts of rabbit skeletal muscle by heating and column chromatography using DEAE-cellulose and Bio-gel P-60. Inhibitor-1 exists in an active phosphorylated form and an inactive dephosphorylated form. The interconversion of phosphorylated inhibitor-1 and dephosphorylated inhibitor-1 is mediated by protein kinase dependent on adenosine 3' : 5'-monophosphate (cyclic AMP) and a Mn2+-stimulated phosphoprotein phosphatase. Inhibitory activity of inhibitor-2 is not influenced by treatment with either the kinase or the Mn2+-stimulated phosphatase. The molecular weights of inhibitor-1 and inhibitor-2 estimated by sodium dodecylsulfate-polyacrylamide gel electrophoresis are 26 000 and 33 000 respectively. Both inhibitor-I and inhibitor-2 inhibit phosphorylase phosphatase by a mechanism which appears to be non-competitive with respect to the substrate phosphorylase a. Inhibitor fractions at early stages of purification also inhibit cyclic-AMP-dependent histone phosphorylation, but this kinase inhibitory activity resides with a protein moiety which is separable from inhibitor-1 and inhibitor-2.Regulation of glycogenolysis by cyclic AMP occurs at mulriple enzyme sites. Cyclic-AMP-dependent protein kinase controls the activities of phosphorylase kinase and glycogen synthase [l-41. Direct phosphorylation of these two enzymes by protein kinase has been demonstrated [5 -71, and the involvement of these phosphorylations in vivo in the control of glycogenolysis is established [8,9]. We recently provided evidence that phosphorylase phosphatase is also regulated by cyclic-AMP-dependent protein kinase [lo]; direct phosphorylation of the enzyme, however, could not be demonstrated. This was explained by an alternative mechanism involving the phosphorylation of a heat-stable protein, which in the phosphorylated state is a potent inhibitor of phosphorylase phosphatase [lo].Recently, a number of heat-stable protein inhibitors of phosphoprotein phosphatase have been described in Ehrlich ascites cells [ll], and rabbit liver [12,13]. We also observed a second heat-stable inhibitor protein that was associated with rabbit muscle phosphatase [14] and was separated away from the ___-

The use of high fructose corn syrup (HFCS) has increased over the past several decades in the United States while overweight and obesity rates have risen dramatically. Some scientists hypothesize that HFCS consumption has uniquely contributed to the increasing mean body mass index (BMI) of the U.S. population. The Center for Food, Nutrition, and Agriculture Policy convened an expert panel to discuss the published scientific literature examining the relationship between consumption of HFCS or "soft drinks" (proxy for HFCS) and weight gain. The authors conducted original analysis to address certain gaps in the literature. Evidence from ecological studies linking HFCS consumption with rising BMI rates is unreliable. Evidence from epidemiologic studies and randomized controlled trials is inconclusive. Studies analyzing the differences between HFCS and sucrose consumption and their contributions to weight gain do not exist. HFCS and sucrose have similar monosaccharide compositions and sweetness values. The fructose:glucose (F:G) ratio in the U.S. food supply has not appreciably changed since the introduction of HFCS in the 1960s. It is unclear why HFCS would affect satiety or absorption and metabolism of fructose any differently than would sucrose. Based on the currently available evidence, the expert panel concluded that HFCS does not appear to contribute to overweight and obesity any differently than do other energy sources. Research recommendations were made to improve our understanding of the association of HFCS and weight gain.

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