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Highlights • Code comparisons build confidence in simulators to model interdependent processes. • International hydrate reservoir simulators are compared over five complex problems. • Geomechanical processes significantly impact response of gas hydrate reservoirs. • Simulators yielded comparable results, however many differences are noted. • Equivalent constitutive models are required to achieve agreement across simulators. Geologic reservoirs containing gas hydrate occur beneath permafrost environments and within marine continental slope sediments, representing a potentially vast natural gas source. Numerical simulators provide scientists and engineers with tools for understanding how production efficiency depends on the numerous, interdependent (coupled) processes associated with potential production strategies for these gas hydrate reservoirs. Confidence in the modeling and forecasting abilities of these gas hydrate reservoir simulators (GHRSs) grows with successful comparisons against laboratory and field test results, but such results are rare, particularly in natural settings. The hydrate community recognized another approach to building confidence in the GHRS: comparing simulation results between independently developed and executed computer codes on structured problems specifically tailored to the interdependent processes relevant for gas hydrate-bearing systems. The United States Department of Energy, National Energy Technology Laboratory, (DOE/NETL), sponsored the first international gas hydrate code comparison study, IGHCCS1, in the early 2000s. IGHCCS1 focused on coupled thermal and hydrologic processes associated with producing gas hydrates from geologic reservoirs via depressurization and thermal stimulation. Subsequently, GHRSs have advanced to model more complex production technologies and incorporate geomechanical processes into the existing framework of coupled thermal and hydrologic modeling. This paper contributes to the validation of these recent GHRS developments by providing results from a second GHRS code comparison study, IGHCCS2, also sponsored by DOE/NETL. IGHCCS2 includes participants from an international collection of universities, research institutes, industry, national laboratories, and national geologic surveys. Study participants developed a series of five benchmark problems principally involving gas hydrate processes with geomechanical components. The five problems range from simple geometries with analytical solutions to a representation of the world's first offshore production test of methane hydrates, which was conducted with the depressurization method off the coast of Japan. To identify strengths and limitations in the various GHRSs, study participants submitted solutions for the benchmark problems and discussed differing results via teleconferences. The GHRSs evolved over the course of IGHCCS2 as researchers modified their simulators to reflect new insights, lessons learned, and suggested performance enhancements. The five benchmark problems, final sample solutions, and lessons learned that are presented here document the study outcomes and serve as a reference guide for developing and testing gas hydrate reservoir simulators.

Summary In the advanced stage of protein glycation, Amadori compounds are degraded to 2-oxoaldehydes such as 3-deoxyglucosone (3DG) and glucosone, which react as cross-linkers. In the present paper, NADPH-dependent aldo-keto reductases in porcine tissues were investigated using methylglyoxal (MG), 3DG, and acetaldehyde as substrates. Three reductases, enzyme (I), (II), and (III), were purified from porcine liver. Enzyme (I) named 2-oxoaldehyde reductase was major enzyme metabolizing 3DG, but it was inactive toward alcohols, indicating that enzyme (I) is different from alcohol dehydrogenase (aldehyde reductase). Enzyme (II), which was identified as aldose reductase, was also active toward 3DG. Although enzyme (III) was inactive toward 3DG, it was much active toward acetaldehyde and MG, and showed typical property of aldehyde reductase, EC 1.1.1.2. 2-Oxoaldehyde reductase was purified from chicken liver, and this enzyme inhibited effectively polymerization of glycated lysozyme in vitro.