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1.
温度、pH对缢蛏(Sinonovacula constricta)消化酶活力的影响 总被引：8，自引：0，他引：8
本文研究了温度、pH对缢蛏(Sinonovacula constricta(Lamarck))三种主要消化酶(蛋白酶、淀粉酶和纤维素酶)活力的影响。结果表明：当温度在5～75℃之间时，蛋白酶、纤维素酶和淀粉酶的最适温度分别为为55℃、45℃和65℃；在不同的pH范围内，蛋白酶的最适PH值为9．2，淀粉酶的最适PH值为6．3和7．7，纤维素酶的最适PH值为5．2。缢蛏的淀粉酶和蛋白酶活力较大，纤维素酶活力极微。 相似文献
2.
Dot enzyme-linked immunosorbent assay （dot-ELISA）, indirect ELISA and Westem blot were performed to detect the virulent protease secreted by Vibrio anguillarum which was isolated from the diseased left-eyed flounder, Paralichthys olivaceous. Sensitivity results showed that dot-ELISA is a more sensitive, rapid and simple technique for the protease detection. The minimal detectable amount of protease is about 7 pg in the dot-ELISA test, while 7.8 ng in the indirect ELISA and 6.25 ng in the Westem blot respectively. Protease could be detected 2 h after incubation of V. anguillarum in the 2216E liquid medium but enzyme activity was very low at that period. From 6 to 12 h, the amount and enzyme activity of protease increased markedly and reached maximum at stationary phase. Analysis of serum samples periodically collected from the infected flounders showed that after 2 h of infection by V. anguillarum, the pathogenic bacteria could be detected in the blood of the infected flounders but no protease was found. It was 5-6 h after infection that the protease was detected in blood and then the amount increased as infection advanced. Quantitative detection of protease either incubation in the medium or from the blood of infected flounders could be accomplished in virtue of positive controls of quantificational protease standards （＂marker＂） so that the alterations ofprotease secretion both in vitro and in vivo could be understood generally. In addition, the indirect ELISA and dot-ELISA were also performed to detect V. anguillarum cells. Results indicated that the sensitivity of indirect ELISA to bacteria cells is higher than that of the dot-ELISA, and that the minimal detectable amount is approximately 10^4 cell/mL in the indirect ELISA, while 10^5 cell/mL in the dot-ELISA. 相似文献
3.
107 strains producing protease were screened from 260 strains of Antarctic psychrophilic bacteria, among which proteolytic activity of five strains was more than 45 U ml^-1. The 16S rRNA gcne sequences homology and phylogcnetic analysis of five Antarctic psychrophillc bacteria showed that NJ276, NJS-9, NJ16-70,NJ345 belonged tO the described genus Pseudoalteromonas and NJ341 belonged to the genus Colwellia. The growth and the protease characteristic of four Antarctic psychrophilic bacteria had been studied, and the result showed that the 6ptimal temperature for growth and protease-produeing of four strains was about 10℃. Their growth and protease-produeing were still high during incubatlng 2-5 days. The maximum proteolytic activity occurred at pH 9 for four Antarctic psychrophilic bacteria. The optimal temperature of protease action of both strains NJ276 and NJ5-9 was about 50℃, however, the optimal temperature of protease aetlon of both strains NJ341 and NJ345 was about 40 ℃, and their proteolytic activity under 0℃ exhibited nearly 30% of the maximum activity, but their thermal stabilities were weaker. These results indicated that proteases from NJ341 and NJ345 were low-temperature proteases. 相似文献
4.
土壤丛枝菌根真菌分泌的球囊霉素相关土壤蛋白(GRSP)是土壤碳库变化的重要指标, 为明确其在会仙岩溶湿地不同土地利用方式下的分布特征及影响因素, 以会仙岩溶沼泽, 并由其转变而来的水稻田、旱地、果园和弃耕地4种不同土地利用方式为研究对象, 采集0–10 cm、10–20 cm和20–40 cm这3个层次的土样, 对不同土地利用方式下球囊霉素相关土壤蛋白分布特征及其与土壤因子的关系进行了研究。结果表明, 不同土层总球囊霉素相关土壤蛋白(T-GRSP)含量为1.08～3.35 mg/g, 占土壤有机碳的12.33%～19.73%, 球囊霉素相关土壤蛋白是湿地土壤中的一个重要碳库。球囊霉素相关土壤蛋白在不同土地利用方式和土层之间均表现出显著差异, 随土层深度的增加表现出降低趋势。沼泽土壤中总球囊霉素相关土壤蛋白、易提取球囊霉素相关土壤蛋白(EE-GRSP)含量和有机碳(SOC)的含量均高于其它4种土地利用方式(水稻田、旱地、园土和弃耕地)。GRSP分别与蛋白酶、SOC和全氮(TN)呈极显著正相关(P＜0.01), 分别与速效氮(AN)、速效磷(AP)、粘粒和粉粒呈显著正相关(P＜0.05)。EE-GRSP与SOC和TN呈极显著正相关(P＜0.01), 分别与蛋白酶和粘粒呈显著正相关(P＜0.05)。主成分分析表明, 粉粒、SOC、AN和TN是影响球囊霉素相关蛋白分布特征和反映会仙岩溶湿地土壤营养状况的主要因子。会仙岩溶湿地土壤中的球囊霉素相关土壤蛋白对土壤碳封存有重要贡献。 相似文献
5.
An alkaline protease from Acetes chinensis was purified and characterized in this study. The steps of purification include ammonium sulfate precipitation, ion-exchange
chromatography with Q-sepharose Fast Flow, gel filtration chromatography with S300 and the second ion-exchange chromatography
with Q-sepharose Fast Flow. The protease was isolated and purified, which was present and active on protein substrates (azocasein
and casein). The specific protease activity was 17.15 folds and the recovery was 4.67. The molecular weight of the protease
was estimated at 23.2 kD by SDS-PAGE. With azocasein as the susbstrate, the optimal temperature was 55°C and the optimal pH
value was 5.5. Ion Ca2+ could enhance the proteolytic activity of the protease, while Cu2+, EDTA and PMSF could inhibit its activity. 相似文献
6.
7.
Dewi Seswita Zilda 《中国海洋大学学报(英文版)》2012,11(2):213-218
A total of 69 strains of thermophilic bacteria were isolated from water, soil and sediment samples from three Indonesia’s hot spring areas (Pantai cermin, Kalianda and Banyu wedang) by using Minimal Synthetic Medium (MSM). The extreme thermophile Brevibacillus sp. PLI-1 was found to produce extracellular thermophilic alkaline protease with optimal activity at 70℃ and pH 8.0-9.0. The molecular weight of the protease was estimated to be around 56 kD by SDS-PAGE. The maximum activity of the protease was 26.54 U mL-1. The protease activity did not decrease after 30 min and still retained more than 70% of relative activity after 60 min at 70℃ and pH 8.0. The ion Mg2+ was found to promote protease activity at both low and high concentrations, whereas Cu2+ and Zn2+ could almost completely inhibit the activity. Divalent cation chelator EDTA inhibited the enzyme activity by 55.06% ± 0.27%, while the inhibition caused by PMSF, Leupeptin, Pepstain A and Benzamidine were 66.78% ± 3.25%, 52.37% ± 0.25%, 62.47% ± 2.96% and 50.99% ± 0.24%, respectively. Based on these observations, the enzyme activity was conspicuously sensitive to the serine and cysteine protease inhibitors. All these results indicated that the protease isolated from the strain PLI-1 was a thermophilic protease and had a high-temperature stability and a pH stability. 相似文献
8.
利用选择性筛选培养基从所构建的深海沉积物宏基因组文库中筛选得到一株产蛋白酶的克隆（CAPR0002）,对其进行了酶学性质分析．结果表明该酶的最适作用温度为65cc,最适作用pH值为9．0．该蛋白酶具有较好的热稳定性,在40cC以下的温度中可长期保持稳定,在50℃中处理6h后仍能保持60％的活力,在60℃下保温30rain后仍能保持约60％的活力．Ca^2＋、Mg^2＋、sr^2＋、co^2＋对该蛋白酶有明显的促进作用,而且ca^2＋的存在可明显提高该蛋白酶的热稳定性,ca^2＋、sr^2＋、c0^2＋这3种离子均在3．0mmol／dm^3。浓度时具有最高的促进作用,当浓度高于3．0mmol／dm’时,这3种离子对酶活力的促进作用减弱．Hg^2＋、Fe^2＋、cu¨对酶有明显的抑制作用．CAPR02蛋白酶在pH值为7。5～9．5时活力较高,pH值为7。5时可保持约80％的活力,pH值为9．5时保持60％的活力,而在pH值高于9．5的条件下酶活力下降较快,pH值为10．0时活力降为约15％,表明CAPR02属于碱性蛋白酶．丝氨酸蛋白酶抑制剂PMSF、E一64和AEBSF对CAPR02蛋白酶均无抑制作用,显示该酶不属于丝氨酸蛋白酶,而EDTA对酶有明显的抑制作用,表明该酶属于金属蛋白酶． 相似文献
9.
A psychrophilic bacterium strain 547 producing cold-adaptive alkaline protease was isolated from the deep sea sediment of Prydz Bay, Antarctica. The organism was identified as a Planomicrobium species by 16S rRNA analysis. The optimal and highest growth temperatures for strain 547 were 15℃ and 30℃, respectively. The extracellular protease was purified by ammonium sulfate precipitation and DEAE cellulose-52 chromatography. The optimal temperature and pH for the activity of the purified enzyme were 35 ℃ and pH 9.0, respectively. The enzyme retained approximately 40% of its activity after 2 h of incubation at 50℃. The enzymatic activity was inhibited by 1 mmol/L phenylmethyl sulfonylfluoride (PMSF) and hydrochloride 4-(2-aminoethyl)-benzenesulfonyl fluoride (AEBSF), indicating that it was a serine protease. The presence of Ca2+ and Mn2+ increased the activity of the enzyme. The protease gene with a size of 1 269 bp was cloned from Planomicrobium sp. 547 using primers designed based on the conserved sequences of proteases in GenBank. The Planomicrobium sp. 547 protease contained a domain belonging to the peptidase S8 family, which has a length of 309 amino acid (AA) residues. The alignment and phylogenetic analysis of the AA sequence indicated that the protease belonged to the subtilisin family. 相似文献
10.
研究了动物蛋白酶 1 0 58水解鱼是鱼蛋白时 ,酶量、温度、作用时间对鱼是鱼蛋白质水解率和苦味的影响。结果表明 :酶浓度的提高 ,水解时间的延长 ,均使鱼是鱼蛋白水解率明显提高。最适水解温度为 50℃ ,当温度高于 50℃时 ,水解率逐渐下降 ,蛋白酶开始失活。苦味值随水解率提高而增加。用正交试验的方法 ,经综合分析和试验得出 ,该蛋白酶水解鱼是鱼的最佳条件是酶量与底物之比为 1 .5∶ 1 0 0 0 ;温度为 50℃ ;水解时间为 4h。 相似文献