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脂肪酶产生菌Geofrichum sp. AS 2.1135产酶条件及酶一般性质的研究 总被引:5,自引:1,他引:4
在92株能同化油的地霉属菌株中,Geotrichum sp. AS2.1135菌株产脂肪酶活力为50—60u/ml,对其产酶条件的研究表明,不饱和长链脂肪酸和油类有利于酶的形成。在4%豆饼粉作为有机氮源的培养基中,加入0.2%尿素,酶活力显著增加,酶活达150u/ml。用聚乙二醇橄榄油乳化系统测定酶的作用最适pH为8.0,最适温度为4O一42℃。在pH4一9时5℃下存放24小时,或在pH 5和8时45℃保持15分钟,酶活力不变。 相似文献
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克鲁维酵母Y-85合成菊粉酶最适条件的研究 总被引:3,自引:0,他引:3
采用响应面方法(ResponseSurfaceMethod,RSM)对克鲁维酵母(Kluyveromycessp.)Y-85产菊粉酶培养基成份进行了优选,和正交试验相比,该法选出的最适培养基的酶发酵水平提高28%。用15L自控发酵罐进行产酶条件控制试验,并在1000L罐上进行5批次酶发酵中试,平均菊粉酶活性达68.9u/ml。 相似文献
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绿色糖单孢菌产木聚糖酶规律及其耐碱耐热性的初步研究 总被引:13,自引:2,他引:11
采用绿色糖单孢菌为实验材料,在不同诱导产酶培养基上经过192h的振荡培养,探索其产酶时程规律.结果表明,不同的诱导底物诱导产生的木聚糖酶活性差异不显著,但诱导产纤维素酶活性差异显著.其中松木粉加棉纱培养基诱导产纤维素酶活性为0.08IU/ml,与空白对照(5.40IU/ml)相比显著下降(P≤0.05).为了适应纸浆漂白实际应用中纤维素酶越少越好的要求,选择该培养基为最佳诱导产酶培养基.绿色糖单孢菌在上述培养基中培养156h后达到木聚糖酶产酶高峰。粗酶液酶活可达到9.03IU/ml.通过对该酶进行高温及碱性处理。实验结果表明绿色糖单孢菌分泌的木聚糖酶在pH7.0下反应表现最高活性,同时在90℃下保温3h后酶活为原来的63.55%,具有较好的耐碱耐热性. 相似文献
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产胆红素氧化酶菌种筛选 总被引:4,自引:0,他引:4
选出一株产胆红素氧化酶的菌种露湿漆斑菌—Myrotheciumr oriclum,简称MTR89—403。此菌产酶最适培养基:40—80%的马铃薯浸出液100ml、葡萄糖1g,pH6.0。培养条件:500ml三角瓶装100ml培养基,在27℃、200rpm旋转摇床培养84h,得到的最高酶活为1300u/L,比活为12.3u/mg蛋白。 相似文献
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木聚糖酶高产菌株Bacillus pumilus H—101的筛选及产酶条件的研究 总被引:6,自引:2,他引:6
从34株细菌中筛选到一株木聚糖酶高产菌株BacilluspumilusH-101。适宜的产酶培养基含2.0%小麦秸半纤维素、0.2%(NH4)2SO4、0.1%NH4NO3、0.1%K2HPO4、0.01%MgSO4·7H2O、0.02%NaC1、0.02%CaCl2·2H2O和1.0%的酵母膏。在上述培养基中,32℃振荡培养48h,总半纤维素酶活力达235.6u/ml,木聚精酶活力达1164.2u/ml酶反应的最适温度为50℃,最适酸碱度为pH6.5;Na 、Mg2 等离子可提高木聚精酶的水解活性,而Zn2 、Cu2 等离子则对木聚糖酶活性有明显的抑制作用。 相似文献
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温特曲霉AspergilluswentiiF-871是高效转化延胡索酸为L-苹果酸的变株,通过对其合成延胡索酸酶的因素进行研究,筛选了培养基主要营养元素有L-精氨酸、酪氨酸、丝氨酸、天冬氨酸、苏氨酸、赖氨酸及相应含量丰富的酵母粉、黄豆饼粉和玉米浆。该变株生长阶段条件为:pH6.0,温度2830℃,培养时间为24h,酶合成阶段最适条件:接种量15%,初始pH6.8,培养温度2830℃,装量8090ml/500ml,酶合成周期40h。在优化的培养条件下,F-871变株延胡索酸酶合成水平可达156.33u/g,100ml发酵液中的酶可将延胡索酸转化为L-苹果酸32.06g,比国内一步发酵法产酸88.5%提高约4倍,转化率由85%提高到106.87%,发酵周期由90h缩短至57h。 相似文献
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温特曲霉AspergilluswentiiF-871是高效转化延胡索酸为L-苹果酸的变株,通过对其合成延胡索酸酶的因素进行研究,筛选了培养基主要营养元素有L-精氨酸、酪氨酸、丝氨酸、天冬氨酸、苏氨酸、赖氨酸及相应含量丰富的酵母粉、黄豆饼粉和玉米浆。该变株生长阶段条件为:pH6.0,温度2830℃,培养时间为24h,酶合成阶段最适条件:接种量15%,初始pH6.8,培养温度2830℃,装量8090ml/500ml,酶合成周期40h。在优化的培养条件下,F-871变株延胡索酸酶合成水平可达156.33u/g,100ml发酵液中的酶可将延胡索酸转化为L-苹果酸32.06g,比国内一步发酵法产酸88.5%提高约4倍,转化率由85%提高到106.87%,发酵周期由90h缩短至57h。 相似文献
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The proteolytic enzymes are the most important group of commercially produced enzymes. The production of alkaline protease was optimized using a newly isolated Bacillus sp. RKY3. The fermentation variables were selected in accordance with the Plackett-Burman design and were further optimized via response surface methodological approach. Four significant variables (corn starch, yeast extract, corn steep liquor, and inoculum size) were selected for the optimization studies. The statistical model was constructed via central composite design (CCD) using three screened variables (corn starch, corn steep liquor, and inoculum size). An overall 2.3-fold increase in protease production was achieved in the optimized medium as compared with the unoptimized basal medium. Enzyme activity increased significantly with optimized medium (939 u ml(-1)) when compared with unoptimized medium (417 u ml(-1)). 相似文献
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大肠杆菌耦合乙酸分离的过滤培养 总被引:9,自引:0,他引:9
A fed-batch fermentation integrated with filtration process was proceeded in a synthetic medium with the use of a hollow-fibre membrane filter. The activity of αA interferon reached 1.4 ×109u/L,which was increased 320% over that of a control process. The integrated process was then proceeded in the synthetic medium supplemented with yeast extract during the earlier stage. The addition of yeast extract not only reduced the accumulation of acetate, but also promoted the production of αA interferon. The maximum activity achieved 1.9 ×109 u/L during the fermentation, which was increased 480% over that of a normal process. 相似文献
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V. Gullo I. Gunnarsson V. Hegde A. Horan D. Loebenberg J. Marquez M. Patel M. Puar J. Schwartz 《Journal of industrial microbiology & biotechnology》1991,8(1):65-68
Summary Sch 40873, a novel antifungal compound isolated from the fermentation broth of anActinomadura spp. was discovered in an assay designed to detect compounds with preferential activity against the invasive mycelial form ofCandida albicans. The geometric mean MIC of Sch 40873 against sevenCandida spp. in Sabouraud dextrose broth (yeast phase) was 58 g/ml and in Eagles minimum essential medium (mycelial phase) was <0.03 g/ml. Sch 40873 demonstrated slight in vivo topical activity in a hamster vaginal model. 相似文献
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Summary The production of -amylase by Bacillus licheniformis M27 in submerged fermentation was completely inhibited due to catabolic repression in medium containing 1% glucose. In contrast, the enzyme production in a solid state fermentation system was 19,550 units/ml extract even when the medium contained 15% glucose. The peak in enzyme titre was, however, shifted from 48 to 72 h. The ability of the solid state fermentation system to significantly overcome catabolic repression was not known earlier and is probably conferred by various physico-chemical factors and culture conditions specific to the system.
Offprint requests to: B. K. Lonsane 相似文献
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为获得广谱抗菌功能野生菌株并提高其发酵产物中抗菌物质的含量。采用管碟法和菌丝生长速率法筛选功能菌株,ITS序列分析鉴定功能菌株,通过响应面法和正交设计优化发酵生产抗菌物质的工艺。筛选到一株强效、广谱抗菌功能菌株,鉴定为Cerrena sp.,其发酵产物对金黄色葡萄球菌、大肠杆菌、白色念珠菌、枯草芽孢杆菌和水稻纹枯病菌有显著拮抗作用。该菌株的摇甁发酵配方及培养条件为:马铃薯13.99 g/L,蔗糖 41.58 g/L,VB1 0.027 g/L,麸皮7 g/L,KH2PO4 2 g/L,MgSO4·7H2O 2 g/L;摇床温度28 ℃、发酵周期10 d、种龄4 d、接种量8%、初始pH为5.0、装液量110 ml/250 ml。该菌株有明显抑菌活性,发酵工艺优化后抗菌活性提高了30.37%,为该菌株今后的应用、抗菌剂的分离提纯和产业化提供了实验依据。 相似文献
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Carvalho AF Gonçalves AZ da Silva R Gomes E 《Journal of microbiology (Seoul, Korea)》2006,44(3):276-283
The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal activity of 30 U/ml after 336 h of fermentation. In solid-state fermentation, the activity of the enzyme was 22 U/ml at 144 h in medium containing wheat bran and 5.8 U/ml at 48 h when cassava pulp was used as the culture medium. The enzyme was specific for maltose, very slowly hydrolyzed starch, dextrins (2-7G) and the synthetic substrate (alpha-PNPG), and did not hydrolyze sucrose. These properties suggest that the enzyme is a type II alpha-glucosidase. The optimum temperature of the enzyme was 70 degrees . In addition, the enzyme was highly thermostable (100% stability for 10 h at 60 degrees and a half-life of 15 min at 80 degrees), and stable within a wide pH range. 相似文献