急性炎性疾病患者乳酸林格氏液液体动力学

目的:探索炎性疾病患者的乳酸林格氏液（Ringer's lactate,RL）液体动力学特征以及炎性生物标记物是否可以作为协变量影响RL分布和排泄。方法:本研究为前瞻性队列研究。选择40例美国麻醉医师分级（ASA）I-II级，腹腔镜下择期胆囊切除术（胆囊炎组，n=20）或者腹腔镜下急诊阑尾切除术（阑尾炎组，n=20）。所有患者麻醉诱导前开始输注RL，按15 mL/kg，35 min内输毕。采用酶联免疫（enzyme-linked immunosorbent assay,ELISA）方法测定血浆炎症（TNF-α,IL-10和CRP）或者内皮损伤生物标记物（syndecan-1,SDC-1）；利用血红蛋白（Hb）稀释-时间曲线和尿量，使用Phoenix软件，采用非线性混合效应模型分析计算RL液体动力学参数和协变量的影响。结果:与胆囊炎组相比，阑尾炎组RL从组织间隙到血浆的转运速率常数（k21）显著降低（14×10-3min-1 versus 35×10-3min-1;P=0.012）。阑尾炎组C反应蛋白（CRP）升高［中位数38.1(1.8-143.6) μg/mL versus 1.3(0.1-159.0) μg/mL;P<0.001］；与清醒状态相比，麻醉期间（输液开始后30～45 min），液体从中央室中到外周室的转运速率常数（k12）显著增加（57×10-3min-1 versus 32×10-3min-1；P<0.01）。清除速率常数（k10）降低90%（0.6×10-3min-1 versus 5.3×10-3min-1;P<0.001）。无论在清醒状态还是麻醉状态下低血压均能降低液体清除；炎症或者内膜损伤的生物标记物不能作为显著影响RL液体动力学参数的协变量。结论:阑尾炎或者胆囊炎患者术前输入液体后“炎症反应的生物标记物”不是RL的液体动力学的协变量，但是两组患者中，全身麻醉期间输入液体的清除率下降。     

Synergistic antimicrobial effect of lactocin AL705 and nisin combined with organic acid salts against Listeria innocua 7 in broth and a hard cheese

The effectiveness of antimicrobial mixtures against Listeria innocua 7, used as a L. monocytogenes surrogate, was investigated in broth and a food system. Synergistic effects were found for nisin (Nis), potassium sorbate (PS), calcium propionate (CP) and sodium lactate (SL), Nis + PS being the most effective binary mixture that exhibited listericidal activity in broth. To assess the effect of adding lactocin AL705 (AL705) to Nis + organic acid salt combinations, tridimensional isobolograms were generated. Sub-MIC combinations of the antimicrobials exerted bactericidal activity against L. innocua 7 after AL705 addition to the binary mixtures. However, when applied on Sardo cheese contaminated with L. innocua 7 (initial inoculum 4.45 ± 0.06 CFU g⁻¹), only Nis + PS + AL705 produced count reductions respect to the control, reaching 3.04 ± 0.35 CFU g⁻¹ counts after 15 days at 15 °C. Ternary combinations containing AL705 showed potential to reduce antimicrobial usages for L. innocua 7 inhibition.     

Kinetic behaviour of muscle LDH immobilized in nylon tubing

Immobilization was carried out of the lactate dehydrogenase (LDH) from rabbit muscle (EC 1.1.1.27), cross-linked through the bifunctional reactive glutar-aldehyde on to nylon tubing (1 m long, 53cm² internal surface area). Immobilized LDH inactivation kinetics are of first order (t_1/2 = 3·6 years, k = 5·4,e^?4 day^?1 to 5°C). The smaller effect of pH on activity than in the case of LDH in solution can be explained on the basis of limitation to proton diffusion towards the support. A limiting effect to free external diffusion of the substrate towards and products from the support was also observed, an effect which seems to determine the effective kinetic behaviour of immobilized LDH. The apparent optimum temperature is centred around 40°C, observing a clear inactivation (thermal denaturation) above this temperature. In the temperature range studied (10–40°C), the co-existence was seen of a kinetic control accompanied by another control, involving diffusional transport of substrates and products, on the global activity of the immobilized enzyme. This makes the Arrhenius profiles curvilinear. Both graphic and statistical non-linear regression analysis of the kinetic data—rate, v, versus substrate concentration [S]—carried out under conditions in which the diffusional limitations can be considered negligible (high recirculation flow rate), permitted investigation of the intrinsic kinetic behaviour of immobilized LDH. In this sense, it can be deduced that the rate equation to which these data seem to be fitted is of the polynomial quotient type in [S] of minimum degree 2:2. Although the diffusional limitations have a marked effect on the type of global kinetics shown by immobilized LDH, temperature was not found to affect its v[S] behaviour. The experimental evidence obtained thus indicates that the rate equation in the 10-40°C temperature range continues to be a rational equation of at least degree 2:2 in [S].     

The Effect of Lactates on the Quality of Microwave-Cooked Chicken Patties during Storage

ABSTRACT:  The aim of this study was to determine the effect of adding 3.3% sodium lactate (SL), 0.25% calcium lactate (CL), and 1.65% SL along with 0.125% CL (SL+CL) on the physicochemical properties, cooking characteristics, and microbiological quality of microwave-cooked chicken patties compared to control (no added lactates). The addition of lactates did not affect the proximate composition of cooked chicken patties. The pH of CL- or SL+CL-containing patties was significantly ( P < 0.05) reduced compared to control or SL patties. The SL-containing patties had lower ( P < 0.05) a _w values compared to control or CL patties. The CL- or SL+CL-containing patties had lower denatured myoglobin and higher ( P < 0.05) cooking yield, surface redness (CIE a *), and chroma values. However, addition of CL alone resulted in higher total expressible fluid, indicating lower water-holding capacity. The CL-containing patties exhibited lower Warner–Bratzler shear force values and higher ( P < 0.05) penetrometer reading compared to the SL-containing patties, indicating soft texture. Thiobarbituric acid (TBA) values were significantly ( P < 0.05) reduced in all lactate-containing patties compared to control up to the 7th day of refrigerated storage under aerobic conditions. No difference ( P > 0.05) was observed in aerobic plate counts between control and lactate-added patties during 28-d storage.     

Single amino acid substitutions can further increase the stability of a thermophilic L-lactate dehydrogenase

Lactate dehydrogenases are of considerable interest as stereospecificcatalysts in the chemical preparation of enantiomerically pure-hydroxyacid synthons. For such applications in synthetic organicchemistry it would be desirable to have enzymes which tolerateelevated temperatures for prolonged reaction times, to increaseproductivity and to extend then applicability to poor substrates.Here, two examples are reported of significant thermostabilizations,induced by sitedirected mutagenesis, of an already thermostableprotein, the L-lactate dehydrogenase (EC 1.1.1.27 [EC] , 35 kDa permonomer subunit) from Bacillus stearothermophilus. Thermal inactivationof this enzyme is accompanied by irreversible unfolding of thenative protein structure. The replacement of Argl71 by Tyr stabilizesthe enzyme against thermal inactivation and unfolding. Thisstabilizing effect appears to be based on improved interactionsbetween the subunits in the core of the active dimeric or tetramericforms of the enzyme. The thermal stability of L-lactate dehydrogenasevariants with an active site Arg residue, either in the 171(wild-type) or in the 102 position, is further increased bysulfate ions. The two stabilizing effects are additive, as foundfor the Argl71Tyr/ Gln1O2Arg double mutant, for which the stabilityof the protein in 100 mM sulfate solution reaches that of L-lactatedehydrogenases from extreme thermophiles. All mutant proteinsretain significant catalytic activity, both in the presenceand absence of stnhilfoing salts, and are viable catalysts inpreparative scale reactions.     

一种高效无污染合成丙酮酸乙酯的新方法

研究了由次氯酸钠和溴化钠催化氧化乳酸乙酯合成丙酮酸乙酯新工艺。并通过正交试验设计方法 ,得出最佳实验操作条件 :温度为 30℃以下 ,反应时间为 8h ,溴化钠与乳酸乙酯的摩尔比为 1∶2 ,盐酸与溴化钠的摩尔比为1∶1. 4,不采用光照 ,并由此得到丙酮酸乙酯最好收率为 82 . 86 %(文献值为 80 . 2 %) ,乳酸乙酯的转化率为10 0 %。     

氯化铁催化乳酸的酯化作用

报道了氯化铁水合物催化乳酸和醇的酯化作用制备了１５种乳酯。     

NO2氧化合成丙酮酸乙酯

研究了以NO2为氧化剂,催化氧化乳酸乙酯合成丙酮酸乙酯的新方法,讨论了氧化剂用量、反应时间、反应温度、催化剂用量等因素对反应的影响。在最佳实验条件下,产品收率大于75%,纯度达98%。本法最大的优点是为NO2废气的回收利用提供了新的途径。     

中空纤维超滤膜去除乳酸钙中蛋白质的研究

发酵法联合生产乳酸-乳酸钙工艺中,分离出的乳酸钙产品含有蛋白质、还原糖、重金属等杂质,影响产品的品质。本实验研究了中空纤维膜对乳酸钙中蛋白质的去除,并分析了压差、温度、浓度及pH值等因素的影响。得到了较好的工艺操作条件为Δp=0.05MPa,Δ=30g/L,30°C,pH=4。进一步提出用多步超滤能提高蛋白质的去除率15%～27%。     

维生素C催化合成乳酸异戊酯

首次利用维生素C催化乳酸和异戊醇合成了乳酸异戊酯。在0．1mol乳酸，0．2mol异戊醇和0．2g维生素C作用下，回流分水60min，酯收率达60．0％。结果表明：维生素C能够代替硫酸作为乳酸酯化的催化剂。