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角蛋白酶及其研究进展 总被引:2,自引:0,他引:2
角蛋白在一般情况下很难被降解,工业上用高温、高压的办法降解角蛋白。然而,角蛋白酶能在温和的条件下降解角蛋白。本文对角蛋白的理化性质、发酵条件和分子生物学进行了综述。 相似文献
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可降解羽毛微生物能以羽毛粉为唯一营养源生长,而羽毛粉是一种大颗粒的不溶性底物,不能直接进入细胞内作为营养源同时作为一级信使来诱导酶基因表达.本文通过化学还原法水解羽毛得到可溶性羽毛角蛋白溶液,利用电泳和质谱验证其分子量约10 kD,为角蛋白单体.分别以该可溶性羽毛角蛋白及角蛋白单体酶解片段为诱导源,在无诱导源、羽毛粉为对照的情况下,测定72 h内嗜麦芽窄食单胞菌(S.maltophilia)DHHJ产生的角蛋白酶的酶活.在无诱导源时,角蛋白酶基因表现本底表达(0.5 U/mL);培养基中添加羽毛粉及角蛋白单体时,角蛋白酶表达量高,分别可达15 U/mL和20 U/mL.并且角蛋白单体酶解片段诱导酶表达较低(2.3 U/mL).该结果初步表明,水溶性角蛋白单体作为信号源与细菌细胞接触或进入细胞内,控制角蛋白酶基因表达.该结果为细菌降解角蛋白分子机制研究奠定基础. 相似文献
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为了提高凝结芽孢杆菌(Bacillus coagulans)X3角蛋白酶的水解效率,对其粗酶液的酶学性质及降解羽毛角蛋白的效果进行了研究。结果表明,粗酶液的最适反应温度为60℃,最适pH为7.0~8.0,在70~80℃时具有较好的热稳定性。金属离子中Ca2+、Mn2+对角蛋白酶活性起促进作用,Cu2+、Ni2+强烈抑制角蛋白酶活性,而Na+、Mg2+、Fe3+对酶活性无显著影响。化学试剂苯甲基磺酰氟(PMSF)、乙二胺四乙酸(EDTA)对酶活性有较强的抑制作用,β-巯基乙醇和二硫基苏糖醇(DTT)可显著提高酶活性,十二烷基磺酸钠(SDS)和二甲基亚砜(DMSO)对酶活性没有显著影响。优化条件下降解羽毛,产物中游离氨基酸的总量高达4.322 6 mg/mL,主要种类为缬氨酸、苯丙氨酸、酪氨酸、谷氨酸。研究结果为菌株X3酶解角蛋白废弃物提供了技术支撑。 相似文献
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皮肤癣菌外分泌角蛋白酶的研究进展 总被引:3,自引:1,他引:2
近年来角蛋白酶成为皮肤癣菌致病机制的研究热点,角蛋白酶在真菌的自身营养、组织入侵及控制宿主的防御机制上都发挥着重要的作用,同时也是研究真菌疫苗的一个候选抗原。 相似文献
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Worapot Suntornsuk Junthip Tongjun Poranee Onnim Hiroshi Oyama Kanok Ratanakanokchai Thanit Kusamran Kohei Oda 《World journal of microbiology & biotechnology》2005,21(6-7):1111-1117
Summary Isolation and identification of a thermotolerant feather-degrading bacterial strain from Thai soil as well as purification
and properties of its keratinase were investigated. The thermotolerant bacterium was identified as Bacillus licheniformis. The keratinase was purified to homogeneity by three-step chromatography. The purified enzyme exhibited a high specific activity
(218 U mg−1) with 86-fold purification and 25% yield. The enzyme was monomeric and had a molecular mass of 35 kDa. The optimum pH and
temperature for the enzyme were 8.5 and 60 °C, respectively. The enzyme activity was significantly inhibited by PMSF and partly
inhibited by EDTA and iodoacetamide, but was stimulated by metal ions. It hydrolysed soluble proteins with a relative activity
of 4–100% and insoluble proteins, including keratins, with a relative activity of 3–35%. Therefore, the enzyme could improve
the nutritional value of meat- and poultry-processing wastes containing keratins, collagen and gelatin. 相似文献
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Adriana Gushterova Evgenia Vasileva-Tonkova Elitza Dimova Peter Nedkov Thomas Haertlé 《World journal of microbiology & biotechnology》2005,21(6-7):831-834
Summary The ability of actinomycete strains newly isolated from Antarctic soils to produce keratinolytic enzymes during growth on
sheep wool waste was investigated. The strains which displayed highest keratinase activity and identified as Streptomyces flavis 2BG (mesophilic) and Microbispora aerata IMBAS-11A (thermophilic) were selected for a more detailed analysis. The addition of starch to the growth medium affected
keratinase secretion by both strains. After 5 days of cultivation, a 6-fold increase in keratinase activity of strain 11A
was observed in the presence of 11 g starch/l and a 9-fold increase in keratinase activity of the strain 2BG in the presence
of 5 g starch/l. The results obtained showed that both newly isolated strains are very promising for effective processing
of native keratinous wastes. To our knowledge, this is the first report of Antarctic actinomycete strains that were able to
grow on keratin-containing wastes by producing keratinolytic enzymes. 相似文献
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The ability of five keratinophilic fungi, i.e., Chrysosporium indicum, Geotrichum candidum, Gymnoascoideus petalosporus, Scopulariopsis brevicaulis, and Talaromyces trachyspermus, to digest human hair keratin in stationary culture has been studied. Degradation of human scalp hair was studied by determination of cysteine, cystine, inorganic sulfate, thiosulfate, total protein, keratinase and change in alkalinity of culture filtrate. Gymnoascoideus petalosporus showed maximum degradation as compared to remaining isolates when grown on human scalp hair as the sole source of nutrients in vitro. 相似文献
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Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin 总被引:4,自引:0,他引:4
Kim JS Kluskens LD de Vos WM Huber R van der Oost J 《Journal of molecular biology》2004,335(3):787-797
Structure-forming fibrous proteins like keratins, gelatins and collagens are degraded only by a few proteases as their tight packing limits access to the potential cleavage sites. To understand the keratin degradation in detail, we describe the first crystal structure of a keratin-degrading enzyme (keratinase), fervidolysin, from Fervidobacterium pennivorans as an immature form with propeptide (PD)-bound. The 1.7A resolution crystal structure shows that the protease is composed of four domains: a catalytic domain (CD), two beta-sandwich domains (SDs), and the PD domain. A structural alignment shows a distant relationship between the PD-CD substructure of fervidolysin and pro-subtilisin E. Tight binding of PD to the remaining part of the protease is mediated by hydrogen bonds along the domain surfaces and around the active cleft, and by the clamps to SD1 and SD2. The crystal structure of this multi-domain protein fervidolysin provides insights into proenzyme activation and the role of non-catalytic domains, suggesting a functional relationship to the fibronectin (FN)-like domains of the human promatrix metalloprotease-2 (proMMP-2) that degrades the fibrous polymeric substrate gelatin. 相似文献