Optimization of Solid-State Fermentation with Lactobacillus brevis and Aspergillus oryzae for Trypsin Inhibitor Degradation in Soybean Meal

The aim of the present study was to optimize trypsin inhibitor degradation in soybean meal by solid-state fermentation （SSF） with Lactobacillus brevis and Aspergillus oryzae, and to determine the effect of SSF on phytic acid, crude protein, crude fat, and amino acid profile. Response surface methodology （RSM） with Box-Behnken design was used to optimize SSF. The optimal conditions derived from RSM for L. brevis fermentation were： pH=5. 1; inoculum size=10%; duration=72 h; substrate to water ratio=1.5. The minimum content of trypsin inhibitors was 6.4 mg g^-1 dry matter. The optimal conditions derived from RSM for A. oryzae fermentation were： substrate to water ratio= 0.8 1; inoculum size=4%; duration=120 h. The minimum content of trypsin inhibitors was 1.6 mg g^-1 dry matter. Both L. brevis and A. oryzae decreased trypsin inhibitors dramatically （57.1 and 89.2% respectively）. L. brevis fermentation did not affect phytic acid （0.4%） and crude fat （5.2%） considerably, whereas A. oryzae fermentation degraded phytic acid （34.8%） and crude fat （22.0%） contents to a certain extent. Crude protein content was increased after both fermentation （6.4 and 12.9% for L. brevis and A. oryzae respectively）. Urease activity was reduced greatly （83.3 and 58.3% for L. brevis and A. oryzae respectively）. In conclusion, SSF with A. oryzae and L. brevis reduced trypsin inhibitor content and modified major macronutrients in soybean meal.

Urinary trypsin inhibitor attenuates hepatic ischemia-reperfusion injury by reducing nuclear factor-kappa B activation

BACKGROUND: Urinary trypsin inhibitor (UTI) inhibits the inflammatory response and protects against ischemia-reperfusion (I/R) injury. The inflammatory response is mediated by nuclear factor-kappa B (NF-kappa B) and its related target genes and products such as vascular endothelial cell adhesion molecule and CXC chemokines. We aimed to assess the roles of those mediators in a UTI-treated mouse model of hepatic I/R injury. METHODS: Treatment group 1 (UTI given 5 minutes prior to liver ischemia), treatment group 2 (UTI given 5 minutes after the anhepatic phase) and a control group were investigated. Blood and liver samples were obtained and compared at 1, 3, 6 and 24 hours after reperfusion. RESULTS: Attenuation of pathological hepatocellular damage was greater in the treatment groups than in the control group (P < 0.05). Compared with the control group, the UTI treatment groups showed significantly lower serum alanine aminotransferase and aspartate aminotransferase levels, decreased myeloperoxidase activity, and reduced NF-kappa B activation. Also downregulated was the expression of tumor necrosis factor-alpha, cytokine-induced neutrophil chemoattractant, and macrophage inflammatory protein-2 at the mRNA level. P-selectin protein and intercellular adhesion molecule-1 protein expression were also downregulated. In addition, the treatment group I showed a better protective effect against I/R injury than the treatment group 2. CONCLUSIONS: UTI reduces NF-kappa B activation and downregulates the expression of its related mediators, followed by the inhibition of neutrophil aggregation and infiltration in hepatic I/R injury. The protective role of UTI is more effective in prevention than in treatment.

Purification, characterization and evaluation of insecticidal activity of trypsin inhibitor from Albizia lebbeck seeds

A Bowman-Birk inhibitor with activity against gut proteases of Helicoverpa armigera was extracted in 0.I M sodium phosphate buffer from defatted seed flour of Albizia lebbeck. It was purified to 29.62 folds with 51.43% recovery using ammonium sulfate precipitation, gel filtration chromatography on Sephadex G-100 column and ion ex- change chromatography on DEAE-Sephadex As0. The purified protein had a molecular weight of 12,303 daltons as determined by SDS-PAGE. It was found to be heat stable up to 60~C and had two pH optima of 7.5 and 9.0. The inhibitor exhibited non-competitive pattern of inhibition with a low Ki value of 0.2 ~tM. The inhibitoi- was found to be susceptible to varying concentrations of reducing agents like DTT and 2- mercaptoethanol, thereby indicating the role of disulphide bridges in maintaining its three dimensional structure and stability. The purified inhibitor caused mortality and suppressed larval growth ofPieris brassi- cae larvae. It was also found to be effective against gut trypsin extracted from Spodoptera littoralis. The sequence of the genes encoding for such inhibitors can be determined and the genes expressing protease inhibitors can be used in vegetable crops to confer resistance against insect pests and other plant pathogens.

Purification and Trypsin Inhibitor Activity of a Sporamin B from Sweet Potato (Ipomoea batatas Lam. 55-2)

Sporamin is a soluble protein in sweet potato, and falls into two distinct homology groups, subfamilies A and B. In this research, a sporamin B was purified and its amino acid sequences, trypsin inhibitor activity （Ti activity） were analyzed. This sporamin B was isolated from sweet potato tubers [Ipomoea batatas （L.） Lam cv. 55-2] through extraction of the water-soluble fraction, dialysis, ultrafiltration and ion-exchange chromatography. Homology determined by polyacrylamide gel electrophoresis showed that mainly one bond appeared in gel after being reduced by SDS （sodium dodecyl sulfate）, or by SDS and 2-mercaptoethanol, or in native situation. By comparing the data of the polypeptide mass Matrix-assisted laser desorption/ionization time-of-flight （MALDI-TOF） mass spectrometry with those of the mass of the theoretical amino acid sequences from NCBI protein database, it was revealed that it was Q40091｜Q40091_IPOBA, sweet potato sporamin B - Ipomoea Batatas （sweet potato） （Batate）. The sequence coverage was 70.6%. N-terminal sequence was SETPV （Ser-Glu-Thr-Pro-Val）. There is a linear relationship between trypsin inhibitor activity （Ti activity） and amounts of this sporamin B （3-18 μg mL-1）. The equation of linear regression was y = 2.5809x ＋ 17.049 （r2 = 0.9966）. There was a curvilinear relationship between Ti activity and amounts of this sporamin B （21-150 μg mL-1）. The equation of curvilinear regression is y = 14.417ln（x） ＋ 23.26 （r2 = 0.9924）. The concentration of sporamin B with Ti activity after heating at 40°C may induce part denature of this sporamin B, and there was no statistic difference after heating at 40, 50, 60°C for 20 min. Heat treatment at more than 90°C leads to a dramatic decrease of trypsin inhibitor efficiency. The results suggested that Q40091｜Q40091_IPOBA was the major sporamin B in sweet potato tubers [Ipomoea Batatas （L.） Lam cv. 55-2], which had strong Ti activity, and was stable to both thermal and DTT （DL-dithiothreitol） relatively.

Relationship between inter-α-trypsin inhibitor heavy chain 4 and ovarian cancer

Objective:The inter-α-trypsin inhibitor heavy chain 4(ITIH4)protein is involved in the development of tumors.However,the relationship between ITIH4 and ovarian cancer(OC)has not been extensively examined.This study aimed to explore the effect of ITIH4 on OC and to identify its underlying mechanism.Methods:Expressions of ITIH4 in OC tissues and cells were determined using quantitative reverse transcription polymerase chain reaction(RT-qPCR)and western blots.The function of ITIH4 in the OC cell line HO8910 pm was tested via ITIH4 knockdown.The cell growth rate was measured using MTT and colony formation assays.Flow cytometry was performed to evaluate cell cycle progression.Cell migration and invasion abilities were observed using the transwell migration assay.Results:ITIH4 was downregulated in OC tissues and cells.ITIH4 knockdown promoted cell growth and cell cycle progression.Consistent with these results,inhibition of ITIH4 in OC cells significantly increased cell migration and invasion abilities.Cox regression analysis suggests that ITIH4 expression alone is not a good predictor of the prognosis of malignant ovarian tumors in patients.Conclusions:ITIH4 inhibits the progression of OC,suggesting that ITIH4 may be a useful biomarker for OC.This study may provide a potential novel target for the treatment of OC.

Silica-supported Macroporous Chitosan Bead for Affinity Purification of Trypsin Inhibitor

Macroporous cross-linking chitosan layer coated on silica gel （CTS-SiO2） was prepared by phase inversion and polyethylene glycol （PEG）molecular imprinting methods. Formation of macroporous surtace was investigated by scanning electron microscopy （SEM） and BET analysis.The prepared bead was activated by reacting with 1,2-ethylene digiycidyl ether for introducing epoxy groups, and trypsin could be efficiently immobilized on the bead as a biospecific ligand.The bead bearing trypsin was employed to purify trypsin inhibitor （TIs） from egg white as affinity adsorbent.

A Novel Trypsin Inhibitor-Like Cysteine-Rich Peptide from the Frog Lepidobatrachus laevis Containing ProteinaseInhibiting Activity

Various bio-active substances in amphibian skins play important roles in survival of the amphibians.Many protease inhibitor peptides have been identified from amphibian skins,which are supposed to negatively modulate the activity of proteases to avoid premature degradation or release of skin peptides,or to inhibit extracellular proteases produced by invading bacteria.However,there is no information on the proteinase inhibitors from the frog Lepidobatrachus laevis which is unique in South America.In this work,a cDNA encoding a novel trypsin inhibitor-like(TIL)cysteine-rich peptide was identified from the skin cDNA library of L.laevis.The 240-bp coding region encodes an 80-amino acid residue precursor protein containing 10 half-cysteines.By sequence comparison and signal peptide prediction,the precursor was predicted to release a 55-amino acid mature peptide with amino acid sequence,IRCPKDKIYKFCGSPCPPSCKDLTPNCIAVCKKGCFCRDGTVDNNHGKCVKKENC.The mature peptide was named LL-TIL.LL-TIL shares significant domain similarity with the peptides from the TIL supper family.Antimicrobial and trypsin-inhibitory abilities of recombinant LL-TIL were tested.Recombinant LL-TIL showed no antimicrobial activity,while it had trypsin-inhibiting activity with aKi of 16.5178 lM.These results suggested there was TIL peptide with proteinase-inhibiting activity in the skin of frog L.laevis.To the best of our knowledge,this is the first report of TIL peptide from frog skin.

CRYSTAL STRUCTURE OF THE COMPLEX OF MUNG BEAN TRYPSIN INHIBITOR LYSINE ACTIVE FRAGMENT WITH BOVINE TRYPSIN AT 1.8 A RESOLUTION

The structure of the complex of mung bean trypsin inhibitor lysine active fragment with bovine trypsin has been determined at a resolution of 1.8 A by A-ray crystallographic analysis and the complex model refined by restrained least-squares minimization with the data between 10 and 1.8 resolution.The current conventional R factor is 17.3%,and the model con- tains 1648 protein atoms,219 inhibitor atoms and 126 water molecules.The most prominent feature of the inhibitor fragment is that it does not contain any alpha-helices.Most of the chain fold in an irregular fashion.The seven residues of the binding segment of the inhibitor lysine active frag- ment are in specific contact with bovine trypsin.The binding interaction and geometry around the reactive site are similar to that observed in other studies of trypsin-inhibitor complexes.

Pancreatic secretory trypsin inhibitor:More than a trypsin inhibitor

Kazal-type serine protease inhibitor is one of the most important and widely distributed protease inhibitor families.Pancreatic secretory trypsin inhibitor(PSTI),also known as serine protease inhibitor Kazal typeⅠ(SPINK1),binds rapidly to trypsin,inhibits its activity and is likely to protect the pancreas from prematurely activated trypsinogen.Therefore,it is an important factor in the onset of pancreatitis.Recent studies found that PSTI/SPINK1 is also involved in self-regulation of acinar cell phagocytosis,proliferation and growth of a variety of cell lines.In addition,it takes part in the response to inflammatory factor or injury and is highly related to adult type Ⅱ citrullinemia.

Storage Proteins and Trypsin Inhibitors of an Underutilized Legume, <i>Mucuna</i>: Variability and Their Stability during Germination

The proteins and trypsin inhibitors were isolated from the seeds of different varieties/accessions of an underutilized legume, Mucuna. The crude protein content of all the germplasms of Mucuna is varied from 15% - 26%, showed little variation and contain higher crude protein when compared with other Mucuna species reported earlier and the pulse crops commonly consumed in India. The seeds of all the varieties of Mucuna exhibited trypsin inhibitor activity. The trypsin inhibitor activity varied from 11 - 14 TIA/mg of protein. Not much variation was observed in trypsin inhibitory activities in soaked seeds compared to dry seeds. Germination of Mucuna pruriens has been carried out and the change in the protein content and trypsin inhibitors were monitored. The protein content of the endosperm increased up to 72 hrs of germination and then decreased. The trypsin inhibitory activity decreased with increase in germination time. The trypsin inhibitor activity was decreased from 14.81 TIA/mg to 2.62 TIA/mg (82% reduction in the trypsin inhibitor activity) after 144 hrs germination.

A Kunitz trypsin inhibitor from chickpea (<i>Cicer arietinum</i>L.) that exerts an antimicrobial effect on Fusarium oxysporum f.sp. ciceris

Fusarium oxysporum f.sp. ciceris (Foc) is one of the most important fungal pathogens of chickpea and is regarded as a constant threat in tropical and subtropical countries. In order to correlate Fusarium wilt resistance/susceptibility in Cicer arietinum to the presence or absence of trypsin inhibitor (TI) in the crude extract, trypsin inhibitory assay (TIA) and in vitro activity of TI against Foc were studied. In the present study, a 20 kDa trypsin inhibitor was purified from Fusarium wilt resistant cultivar (viz. JG 2001-12) by ammonium sulfate precipitation, dialysis and chromatographies with Sephadex G-100 and Diethyl aminoethyl cellulose (DEAE-cellulose-52) ion-exchange column. Results of pathogenecity assay were found to be in correlation to the trypsin inhibitor assay where the Fusarium wilt resistant cultivar showed high trypsin inhibitory activity (99%) in the presence of trypsin enzyme using both natural and synthetic substrates. Preliminary studies using crude extracts of JG 2001-12 showed a decrease in radial growth of Foc. A 45%-82% reduction in conidium germination at 20 μg&middotmL-1?Cicer arietinum trypsin inhibitor (CaTI) concentration was observed, thereby, indicating the use of CaTI in suppression of pathogen and in its deployment through transgenic plants for the management of Fusarium wilt.

Credible and Facile Fluorometric Detection of Soybean Trypsin Inhibitor Activity with a Water-Soluble Poly(diphenylacetylene) Derivative

Herein,a novel method for fl uorometric detection of soybean trypsin inhibitor(SBTI)activity based on a water-soluble poly(diphenylacetylene)derivative was reported.Fluorescence quenching of the polymer via p-nitroaniline,produced from the trypsin-catalyzed decomposition of N-benzoyl-DL-arginine-4-nitroanilide hydrochloride(L-BAPA),was well described using the Stern-Volmer equation.SBTI activity was quantitatively assessed based on changes in the fl uorescence intensity of the polymer.This strategy has several advantages,such as high sensitivity and ease of operation.Moreover,its applicability to other biochemical analyses is promising.

Vegetative Storage Protein with Trypsin Inhibitor Activity Occurs in Sapindus mukorassi,a Sapindaceae Deciduous Tree

A vegetative storage protein （VSP） with trypsin inhibitor activity in a deciduous tree, Sapindus mukorassi, was characterized by means of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Western-blot, immuno-histochemical localization, light- and electro-microscopy, together with analysis of proteinase inhibitor activity of the purified VSP in vitro. There were two proteins with molecular masses of about 23 and 27 kDa in a relatively high content in the bark tissues of terminal branches of S. mukorassi in leafless periods. The proteins decreased markedly during young shoot development, indicating their role in seasonal nitrogen storage. Immuno-histochemical localization with the polyclonal antibodies raised against the 23 kDa protein demonstrated that the 23 kDa protein was the major component of protein inclusions in protein-storing cells. The protein inclusions were identified by protein-specific staining and should correspond to the electron-dense materials in different forms in the vacuoles of phloem parenchyma cells and phloem ray parenchyma cells under an electron microscope. So, the 23 kDa protein was a typical VSP in S. mukorassi. The 23 and 27 kDa proteins shared no immuno-relatedness, whereas the 23 kDa protein was immuno-related with the 22 kDa VSP in lychee and possessed trypsin inhibitor activity. The 23 kDa protein may confer dual functions： nitrogen storage and defense.

TOTAL SYNTHESIS OF Trichosanthes TRYPSIN INHIBITOR AND ITS ANALOGUE

Trichosanthes trypsin inhibitor (TTI) is a peptide consisting of 27 amino acid residues with three pairs of disulfide bonds. This paper reports the total synthesis and disulfide bond refolding of this inhibitor and its analogue. After purification, the amino acid sequence and stoichiometrical inhibitory activity against trypsin of the synthetic inhibitor were compatible with those of the natural inhibitor. The analogue of this inhibitor in which residue Met in position 6 was replaced by Ala was also synthesized. The antitrypsin activity of this synthetic analogue was also approximate to that of the natural inhibitor.

The amino acid sequence of a double-headed trypsin inhibitor from the seeds of Momordica charantia Linn.Cucurbitaceae

A double-headed trypsin inhibitor(MCI-1)was isolated and purified from the seeds of Momordica charantia Linn.Cucurbitaceae,by using the trypsin-sepharose-4B affinity chroma- tography and CM-Sephadex-C50 ion exchange chromatography.It is composed of 77 amino acid residues:Asp_8 Thr_1 Ser_4 Glu_8 Pro_2 Gly_6 Ala_4 Cys_(14) Val_2 Met_4 Ile_8 Leu_1 Phe_1 His_3 Lys_ Arg_7. The amino acid sequence of MCI-1 was determined by sequencing the cyanogen bromide,tryptic and staphylococcus aureus V8 proteolytic peptides,then aligned by overlapped sequences.The result shows that MCI-1 contains 7 pairs of disulfide bonds,its sequence showed the high homology with those of “Bowman-Birk”inhibitors.About 50% trypsin inhibitory activity still remained after MCI-1 was cleavaged with cyanogen bromide.

STUDIES ON NATURAL AND MODIFIED PEPTIDE Trichosanthes TRYPSIN INHIBITORS

A peptide trypsin inhibitor was isolated and purified from the roots of Trichosanthes kirilowii （a Chinese medical herb） by using immobilized anhydro-trypsin affinity chromatography and HPLC C18 column reverse chromatography. It contains two major components, both consisting of 27 amino acid residues with three pairs of disulfide bonds. The sequence determination indicated that the difference between them is only in the ninth position, being Gln and Lys, respectively. The peptide bond of the inhibitor reactive site Arg-Ile （3--4） is easy to cleave at low pH by trypsin, resulting in a modified inhibitor. It might be the smallest naturally occurring protein inhibitor so far known. The modification reaction of the Trichosanthes inhibitor with trypsin is similar to the catalytic enzyme-substrate reaction. The dissociation constant of the modified inhibitor with trypsin is around fourfold that of the natural inhibitor.

Mung Bean Trypsin Inhibitor——Synthesis of a Fragment and Its Analogues

The Lys active fragment of the mung bean trypsin inhibitor is composed of two peptidechains,one with 26 amino acid residues and the other with 9 residues linked by two interdisulfide bonds.The two peptide chains could be separated successfully from each other by reduction.with DTT followedby gel filtration.The reduced long peptide chain containing 6 Cys residues was subjected to air oxidation,and about 25% of the original antitrypsin activity of the Lys fragment was recovered.Following the previ-ously reported sequence,the solid-phase synthesis of this long peptide chain and its disulfide bond refold-ing are presented.Unexpectedly,the synthetic peptide showed much lower antitrypsin activity than thenatural one after reduction and air reoxidation.In order to explain this uncompatible result,we redeter-mined the sequence of the native long peptide chain of the Lys active fragment and obtained the result thatthe P′2 position is Ile instead of Lys as previously reported.To ascertain the correct sequence,we synthe-sized another 22-peptide following the newly determined 26-peptide sequence,and skimming two residuesrespectively from N-terminus and C-terminus.After reduction and reoxidation,the synthetic 22-peptidehad the same antitrypsin activity as that of the native 26-peptide.Meanwhile,an analogue of this 22-pep-tide in which the residue Lys at the reactive site was replaced by Ala was also synthesized.This syntheticanalogue did not show any activity either to trypsin or to elastase.

血清LncRNA FAF、ITIH4在慢性心力衰竭患者中的表达意义及对预后的预测价值

目的探讨血清长链非编码RNA(LncRNA)FAF、间α胰蛋白酶抑制因子重链4(ITIH4)在慢性心力衰竭(CHF)患者中的表达意义及对预后的预测价值。方法选择2020年1月—2022年1月安徽医科大学第二附属医院急诊内科收治的CHF患者187例为CHF组,再根据NYHA心功能分级分为Ⅱ级亚组65例,Ⅲ级亚组77例,Ⅳ级亚组45例。于同期招募健康志愿者103例为健康对照组。2组受试者均检测血清LncRNA FAF表达和ITIH4水平,CHF患者出院后随访12个月,统计随访期间主要不良心血管事件(MACE)发生率;多因素Logistic回归分析影响CHF患者发生MACE的因素;受试者工作特征(ROC)曲线分析LncRNA FAF、ITIH4预测CHF患者发生MACE的价值。结果CHF组血清LncRNA FAF表达、ITIH4水平低于健康对照组(t/P=24.469/<0.001、35.196/<0.001)。血清LncRNA FAF表达、ITIH4水平Ⅳ级亚组低于Ⅲ级亚组低于Ⅱ级亚组(F/P=91.653/<0.001、102.345/<0.001)。MACE亚组血清LncRNA FAF表达,ITIH4水平低于非MACE亚组(t/P=13.556/<0.001、6.293/<0.001)。NYHAⅣ级、高水平NT-proBNP是CHF患者发生MACE的危险因素[OR(95%CI)=4.627(2.245~9.538)、2.284(1.505~3.468)],高表达LncRNA FAF、高水平ITIH4是保护因素[OR(95%CI)=0.599(0.425~0.844)、0.666(0.478~0.928)]。LncRNA FAF、ITIH4及二者联合预测CHF患者发生MACE的曲线下面积为0.796、0.801、0.896,二者联合预测曲线下面积高于单独预测(Z=2.453、2.404,均P<0.001)。结论CHF患者血清LncRNA FAF表达和ITIH4水平均降低,且与不良预后有关,联合LncRNA FAF和ITIH4可预测CHF患者预后不良风险。

草鱼丝氨酸蛋白粗酶的提取、酶学特性及大豆胰蛋白酶抑制剂对其活性的影响

【目的】探究草鱼(Ctenopharyngodon idellus)肌原纤维结合型丝氨酸蛋白酶(MBSP)粗酶的提取方法、酶学特性,以及大豆胰蛋白酶抑制剂(STI)对草鱼鱼糜凝胶品质的影响,为改善传统草鱼鱼糜制品品质提供理论基础。【方法】从草鱼背肌中提取MBSP粗酶液,探究提取过程中漂洗次数(1~5次)、热处理温度(35、40、45、50、55℃)、酸洗脱pH值(pH 4.0、pH 5.5)对提取液酶活性的影响,获得最佳提取条件;设置梯度实验探究所得酶的最适温度、pH、稳定性等酶学特性,最后探究大豆胰蛋白酶抑制剂对粗酶酶活性的影响及其对草鱼鱼糜凝胶性能的调控。【结果及结论】经3次漂洗、45℃热处理、pH 4.0酸洗脱后得到的草鱼MBSP粗酶液酶活性最高(P<0.05);所得MBSP最适pH值在9.0附近,最适温度为45℃,具有较好的温度稳定性(P<0.05),其活性可被Na^(+)在一定程度上抑制且被K+、Ca^(2+)激活(P<0.05);STI添加可以显著改善草鱼鱼糜质构,其对草鱼肌原纤维结合型丝氨酸蛋白酶有可逆竞争性抑制作用,半抑制质量浓度为10.85μg/mL,抑制常数Ki=0.24μmol/L。

吸入性乙酰半胱氨酸联合乌司他丁治疗重症肺炎的临床疗效

【目的】探讨吸入性乙酰半胱氨酸联合乌司他丁治疗重症肺炎的疗效。【方法】选取2021年3月至2023年3月本院收治的110例重症肺炎患者,按1∶1随机分为对照组(采用吸入性乙酰半胱氨酸联合抗感染治疗)和观察组(在对照组基础上联合乌司他丁治疗),每组55例,均治疗2周。比较两组临床疗效、退热时间、肺部啰音和咳嗽消失时间、不良反应发生率,以及炎症因子[白细胞介素-6(IL-6)、肿瘤坏死因子-α(TNF-α)、C反应蛋白(CRP)]、血气分析指标[动脉血氧分压(PaO_(2))、动脉血氧饱和度(SaO_(2))和动脉血二氧化碳分压(PaCO_(2))]、急性生理学与慢性健康状况评分系统Ⅱ(APACHEⅡ)评分。【结果】观察组总有效率为90.91%,显著高于对照组的76.36%,差异具有统计学意义(P<0.05)。观察组退热时间、肺部啰音和咳嗽消失时间均显著短于对照组(P<0.05)。观察组治疗2周后IL-6、TNF-α、CRP水平及PaCO_(2)低于对照组(P<0.05),PaO_(2)、SaO_(2)明显高于对照组(P<0.05)。治疗2周后,观察组生理评分、慢性健康状态评分均明显低于对照组,差异有统计学意义(P<0.05)。两组不良反应总发生率比较,差异无统计学意义(P>0.05)。【结论】吸入性乙酰半胱氨酸联合乌司他丁治疗重症肺炎患者疗效显著,能有效改善患者呼吸功能、减轻炎症反应,且不增加不良反应发生率,值得临床推广应用。