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A 2715 ft 2 (252 m 2 ), two story, residential home of the style typical of the Gaithersburg, Maryland area was constructed in 2012 to demonstrate technologies for net-zero energy (NZE) homes (or ZEH). The NIST Net-Zero Energy Residential Test Facility (NZERTF) functions as a laboratory to support the development and adoption of cost-effective NZE designs, technologies, construction methods, and building codes. The primary design goal was to meet the comfort and functional needs of the simulated occupants. The first annual test period began on July 1, 2013 and ended June 30, 2014. During the first year of operation, the home's annual energy consumption was 13039 kWh (4.8 kWh ft -2 , 51.7 kWh m -2 ), and the 10.2 kW solar photovoltaic system generated an excess of 484 kWh. During this period the heating and air conditioning of the home was performed by a novel air-source heat pump that utilized a reheat heat exchanger to allow hot compressor discharge gas to reheat the supply air during a dedicated dehumidification mode. During dedicated dehumidification, room temperature air was supplied to the living space until the relative humidity setpoint of 50% was satisfied. The heat pump consumed a total of 6225 kWh (2.3 kWh ft -2, 24.7 kWh m -2 ) of electrical energy for cooling, heating, and dehumidification. Annual cooling efficiency was 10.1 Btu W -1 h -1 (2.95 W W -1 ), relative to the rated SEER of the heat pump of 15.8 Btu W -1 h -1 (4.63 W W -1 ). Annual heating efficiency was 7.10 Btu W -1 h -1 (2.09 W W -1 ), compared with the unit's rated HSPF of 9.05 Btu W -1 h -1 (2.65 W W -1 ). These field measured efficiency numbers include dedicated dehumidification operation and standby energy use for the year. Annual sensible heat ratio was approximately 70%. Standby energy consumption was 5.2 % and 3.5 % of the total electrical energy used for cooling and heating, respectively.

Fish skeletal muscle prokallikrein was purified from black sea bass, Centropritis striata, and used for the production of polyclonal antiserum. Tissue proteins from primitive fish and teleosts, an alligator, and an insectivore were resolved by sodium dodecylsulfate-polyacrylamide gel electrophoresis, Western blotted, and probed with fish muscle prokallikrein antiserum. A recurring theme was the presence of approximately 36 and 72 kDa kallikrein-like proteins in skeletal muscle, heart, gill, kidney, and spleen of higher teleosts and in selected tissues of sturgeon, shark, alligator, and mole. The presence of immunoreactive kallikreins in osmoregulatory organs such as the gills of teleosts and the rectal gland of sharks signifies a potential role for these proteins in osmoregulation. Black sea bass, rock bass, and sturgeon contained many immunoreactive kallikreins in their swimbladders, which implicates a role for kallikreins in the regulation of blood flow and vascular permeability to facilitate gas exchange within the bladder. Kallikreins were consistently identified in skeletal muscle and heart of all the species evaluated and may regulate local blood flow, muscle contraction or relaxation, or participate in various transport processes. The antiserum to fish prokallikrein recognized immunoreactive kallikreins from pancreatic tissues from fish and lower vertebrates, but not from the pyloric caecum of sea bass. The wide distribution of tissue kallikrein in lower vertebrates suggests that it may participate in a variety of physiological functions.

Fish prokallikrein was isolated and characterized from skeletal muscle of the black sea bass, Centropristis striata. The prokallikrein was purified to apparent homogeneity by anion exchange perfusion chromatography and reversed phase high performance liquid chromatography. Initial identification was by its weak immunoreactivity with human tissue kallikrein antiserum. Two-dimensional gel electrophoresis and immunoblotting identified the protein as 36 kDa with a pI of 4.95-5.15. The prokallikrein was trypsin-activated to produce an approximately 36 kDa active enzyme as identified on an SDS-polyacrylamide gel overlayed with a membrane impregnated with the fluorogenic tripeptidyl substrate D-Val-Leu-Arg-7-amino-4-trifluoromethyl-coumarin. A potential dimer at 72 kDa was also enzymatically active. Bass kallikrein cleaved low molecular weight dog kininogen to release kinin peptide as determined by radioimmunoassay. The enzyme's amidolytic activity, with a pH optimum at 9.0, was inhibited by aprotinin, benzamidine, and phenylmethanesulphonyl fluoride, but not by elastatinal, soybean trypsin inhibitor, or limabean trypsin inhibitor. Polyclonal antiserum raised against the purified bass muscle prokallikrein recognized 36 kDa and 72 kDa proteins in bass heart, skeletal muscle, spleen, swimbladder, gill, and kidney by Western blot analyses. The wide distribution of immunoreactive proteins in the tissues suggests a potential physiological role for fish kallikreins in muscle contraction and/or relaxation, the regulation of local blood flow, and in osmoregulation. The detection of fish prokallikrein and its activation leads the way for an evaluation of the impact of kallikreins in fish health and disease processes and for studying the evolution of kallikreins and related serine proteinases.

Comminuted raw salmon containing various concentrations and combinations of sodium lactate, sodium chloride, and sodium nitrite was inoculated with 10 Listeria monocytogenes cells per g (150 cells/15-g sample), vacuum-packaged in oxygen-impermeable film and stored at 5 or 10°C. Samples were examined for growth of L. monocytogenes and total aerobic microorganisms at specific intervals for up to 50 d. Sodium lactate exhibited a concentration-dependent antilisterial effect that was enhanced by nitrite and/or increased concentrations of NaCl. At 5°C, total inhibition of L monocytogenes was achieved for up to 50 d by 2% sodium lactate in combination with 3% water-phase NaCl. At 10°C, total inhibition was achieved for up to 35 d by 3% sodium lactate in combination with 3% water-phase NaCl, or by 2% sodium lactate in combination with 125 ppm sodium nitrite and 3% water-phase NaCl. Sodium lactate and the other additives also inhibited growth of the aerobic microflora but to a lesser degree than L. monocytogenes .

The behavior of Listeria monocytogenes (10 Scott A cells per g) in cold-process (smoked) salmon containing 3, 5, or 6% water-phase NaCl was evaluated during 30 to 40 d storage at 5 or 10°C in either oxygen-permeable film or vacuum-sealed impermeable film. At 10°C, L. monocytogenes grew to 10 6 to 10 8 CFU/g by the second week, with no differences attributed to NaCl concentration except for an initial lag in the 6% NaCl samples. Vacuum packaging suppressed growth of L. monocytogenes by 10- to 100-fold in samples with 3 or 5% NaCl. Inhibition related to NaCl concentration was most apparent at 5°C and L. monocytogenes populations were held below 10 2 CFU/g by 6% NaCl. Growth of a 327 CFU/g inoculum was about 10-fold greater than a 10 CFU/g inoculum at 10°C and 100-fold greater at 5°C. Growth of two strains isolated from naturally contaminated, commercially prepared, cold-smoked fish did not differ from Scott A. The use of sugar in the product did not influence growth of L. monocytogenes . Maximum populations of aerobic microorganisms reached at 5 and 10°C were similar, although the rate of growth was somewhat delayed at 5°C, and some inhibition was shown by 5 and 6% NaCl and by vacuum packaging.