Digit Pipelined Arithmetic for 3-D Massively Parallel Optoelectronic Circuits

A concept for a future integer arithmetic unit suitable for a realization with 3-D optoelectronic very large scale integrated (VLSI) circuits is presented. Due to the use of optical interconnections running vertically to the circuit's surface no pin limitation is given. This allows massively parallelism and a higher throughput performance than in all-electronic solutions. To exploit the potential of optical interconnections in VLSI systems efficiently well-adapted low-level algorithms and architectures have to be developed. This is demonstrated for a pipelined arithmetic unit using a redundant number representation. A transistor layout for the optoelectronic circuits is given as well as a specification for the necessary optical interconnection scheme linking the circuits with free-space optics. It is shown that the throughput can be increased by a factor of 10 to 50 compared to current all-electronic processors by considering state-of-the-art optical and optoelectronic technology. Furthermore we present results we gained by investigations on a first realized optoelectronic VLSI test chip.     

Biochemical Characterization of Pyranose Oxidase from Streptomyces canus—Towards a Better Understanding of Pyranose Oxidase Homologues in Bacteria

Pyranose oxidase (POx, glucose 2-oxidase; EC 1.1.3.10, pyranose:oxygen 2-oxidoreductase) is an FAD-dependent oxidoreductase and a member of the auxiliary activity (AA) enzymes (subfamily AA3_4) in the CAZy database. Despite the general interest in fungal POxs, only a few bacterial POxs have been studied so far. Here, we report the biochemical characterization of a POx from Streptomyces canus (ScPOx), the sequence of which is positioned in a separate, hitherto unexplored clade of the POx phylogenetic tree. Kinetic analyses revealed that ScPOx uses monosaccharide sugars (such as d-glucose, d-xylose, d-galactose) as its electron-donor substrates, albeit with low catalytic efficiencies. Interestingly, various C- and O-glycosides (such as puerarin) were oxidized by ScPOx as well. Some of these glycosides are characteristic substrates for the recently described FAD-dependent C-glycoside 3-oxidase from Microbacterium trichothecenolyticum. Here, we show that FAD-dependent C-glycoside 3-oxidases and pyranose oxidases are enzymes belonging to the same sequence space.     

Impact of enzymatic mash maceration and storage on anthocyanin and color retention of pasteurized strawberry purées

Strawberry purées were prepared using a commercial polygalacturonase (PG) and a highly purified pectinesterase (PE) preparation, respectively. To elucidate the effect of pectin on color stability following enzymatic pulp maceration, pectin composition was studied by isolating and fractionating the alcohol-insoluble residue from the strawberry purées. The purées were stored at +20 and +4 °C in the dark over a period of 24 weeks monitoring the amounts of monomeric and polymeric anthocyanins as well as antioxidant activities (FRAP, TEAC). Individual anthocyanins were analyzed by HPLC–DAD–MS ⁿ , and color measurements were obtained in the CIE L*a*b* system. Pectin composition was significantly modified following enzymatic maceration of the purées. While PG treatment generally resulted in pectin losses, oxalate-soluble pectins were increased in PE-treated purées. After 24 weeks of storage, the best anthocyanin retention was observed in PE-treated purées. Such products also revealed greatest anthocyanin half-life values and lowest proportion of polymeric pigments. Compared to an untreated control, enzymatic purée maceration using the PG was also beneficial for pigment retention, but less effective than PE. In contrast, color and antioxidant activity were independent of both enzymatic treatments. An initial heating step (90 °C, 10 s) for immediate inactivation of native enzymes such as polyphenoloxidases slightly improved pigment stability, while lowered temperature during mash maceration was less effective. However, by far best color and pigment retention were achieved when the purées were stored at 4 °C in the dark.     

Diamine oxidase supplementation improves symptoms in patients with histamine intolerance

Food Science and Biotechnology - Histamine intolerance (HIT) is thought to be caused by a disproportionate amount of histamine in the body. The enzyme diamine oxidase (DAO) is considered for the...