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1. 发明授权

US5366883A .alpha.-amylase gene 失效
标题翻译： α-淀粉酶基因
公开(公告)号：US5366883A
公开(公告)日：1994-11-22
申请号：US894212
申请日：1992-06-09
申请人： Kiyozo Asada , Takashi Uemori , Hiroyuki Mukai , Ikunoshin Kato , Kenneth Laderman , Christian B. Anfinsen
发明人： Kiyozo Asada , Takashi Uemori , Hiroyuki Mukai , Ikunoshin Kato , Kenneth Laderman , Christian B. Anfinsen
IPC分类号： C07K14/195 , C12N1/21 , C12N9/26 , C12N9/28 , C12N15/09 , C12N15/56 , C12R1/125 , C12R1/19 , C12N15/63 , C12N15/75
CPC分类号： C12N9/2417 , C07K14/195
摘要： The present invention relates, in general, to a cloned .alpha.-amylase gene, and, in particular, to a cloned hyperthermophilic .alpha.-amylase gene and to methods of producing .alpha.-amylase using same.
摘要翻译：本发明一般涉及克隆的α-淀粉酶基因，特别是涉及克隆的超嗜热α-淀粉酶基因以及使用其生产α-淀粉酶的方法。

2. 发明授权

US5578479A Alpha-amylase from hyperthermophilic archaebacterium 失效
标题翻译：超嗜热古细菌的α-淀粉酶
公开(公告)号：US5578479A
公开(公告)日：1996-11-26
申请号：US893928
申请日：1992-06-09
申请人： Kenneth Laderman , Christian B. Anfinsen
发明人： Kenneth Laderman , Christian B. Anfinsen
IPC分类号： C07K7/08 , C07K14/00 , C07K14/195 , C07K14/41 , C12N1/20 , C12N9/28 , C12N15/09 , C12R1/01 , C12P19/14
CPC分类号： C12N9/2417 , Y10S435/822
摘要： The present invention relates, in general, to .alpha.-amylase, and, in particular to .alpha.-amylase from a hyperthermophilic archaebacterium, wherein said .alpha.-amylase is in pure form. The invention also relates to a method of purifying a hyperthermophilic .alpha.-amylase.
摘要翻译：本发明一般涉及α-淀粉酶，特别是涉及来自超嗜热古细菌的α-淀粉酶，其中所述α-淀粉酶是纯形式。本发明还涉及纯化超嗜热α-淀粉酶的方法。

3. 发明授权

US5391489A Proteolytic enzymes from hyperthermophilic bacteria and processes for their production 失效
标题翻译：来自超嗜热细菌的蛋白水解酶及其生产过程
公开(公告)号：US5391489A
公开(公告)日：1995-02-21
申请号：US83536
申请日：1993-06-30
申请人： Robert M. Kelly , Anne K. S. Robinson , Ilse I. Blumentals , Stephen H. Brown , Christian B. Anfinsen
发明人： Robert M. Kelly , Anne K. S. Robinson , Ilse I. Blumentals , Stephen H. Brown , Christian B. Anfinsen
IPC分类号： C12N9/52 , C12P21/04 , C12N9/50
CPC分类号： C12N9/52
摘要： Cell-free extracts from Pyrococcus furiosus were found to possess unusually high levels of proteolytic activity as measured by hydrolysis of azocasein; loss in activity was only 30% after incubation for 24 hours at 98.degree. C. and the half-life of proteolytic activity at that temperature was about 60 hours. Furthermore, cell-free extracts incubated at 98.degree. C. in 1% sodium dodecyl sulfate (SDS) for 24 hours yielded an SDS-resistant protease having a temperature optimum of at least 100.degree. C. The enzyme retained at least 40% of its activity when tested at 98.degree. C. by azocasein hydrolysis in the presence of 4M urea, 2M guanidinium chloride, 10 mM dithiothreitol or 150 mM .beta.-mercaptoethanol. The protease was found to have a pH optimum of 6.8 at 98.degree. C. and retained more than 45% of its activity at pH 9.3 and 82% of its activity at pH 4.5 in assays performed at those values. The protease was classified as a metalloprotease through inhibitor studies, and peptide hydrolysis showed trypsin-like cleavage with additional activities.
摘要翻译：发现激烈热球菌的无细胞提取物通过偶氮酪蛋白水解测定具有异常高水平的蛋白水解活性; 在98℃孵育24小时后，活性损失仅为30％，在该温度下蛋白水解活性的半衰期为约60小时。此外，在98℃，1％十二烷基硫酸钠（SDS）中孵育24小时的无细胞提取物产生温度最佳为至少100℃的SDS-抗性蛋白酶。酶保留其至少40％当在4M尿素，2M氯化胍胍，10mM二硫苏糖醇或150mMβ-巯基乙醇存在下，通过偶氮酪蛋白水解在98℃下测试活性。发现蛋白酶在98℃下的pH最佳值为6.8，并且在这些值下进行的分析中，在pH9.3下保留其活性高于45％，其pH值为4.5的活性为82％。蛋白酶通过抑制剂研究被分类为金属蛋白酶，肽水解显示胰蛋白酶样切割具有额外的活性。

4. 发明授权

US5242817A Proteolytic enzymes from hyperthermophilic bacteria and processes for their production 失效
标题翻译：来自超嗜热细菌的蛋白水解酶及其生产过程
公开(公告)号：US5242817A
公开(公告)日：1993-09-07
申请号：US406327
申请日：1989-09-12
申请人： Robert M. Kelly , Anne K. S. Robinson , Ilse I. Blumentals , Stephen H. Brown , Christian B. Anfinsen
发明人： Robert M. Kelly , Anne K. S. Robinson , Ilse I. Blumentals , Stephen H. Brown , Christian B. Anfinsen
IPC分类号： C12N9/52
CPC分类号： C12N9/52
摘要： Cell-free extracts from Pyrococcus furiosus were found to possess unusually high levels of proteolytic activity as measured by hydrolysis of azocasein; loss in activity was only 30% after incubation for 24 hours at 98.degree. C. and the half-life of proteolytic activity at that temperature was about 60 hours. Furthermore, cell-free extracts incubated at 98.degree. C. in 1% sodium dodecyl sulfate (SDS) for 24 hours yielded an SDS-resistant protease having a temperature optimum of at least 100.degree. C. The enzyme retained at least 40% of its activity when tested at 98.degree. C. by azocasein hydrolysis in the presence of 4M urea, 2M guanidinium chloride, 10 mM dithiothreitol or 150 mM .beta.-mercaptoethanol. The protease was found to have a pH optimum of 6.8 at 98.degree. C. and retained more than 45% of its activity at pH 9.3 and 82% of its activity at pH 4.5 in assays performed at those values. The protease was classified as a metalloprotease through inhibitor studies, and peptide hydrolysis showed trypsin-like cleavage with additional activities.
摘要翻译：发现激烈热球菌的无细胞提取物通过偶氮酪蛋白水解测定具有异常高水平的蛋白水解活性; 在98℃孵育24小时后，活性损失仅为30％，在该温度下蛋白水解活性的半衰期为约60小时。此外，在98℃，1％十二烷基硫酸钠（SDS）中孵育24小时的无细胞提取物产生温度最佳为至少100℃的SDS-抗性蛋白酶。酶保留其至少40％当在4M尿素，2M氯化胍胍，10mM二硫苏糖醇或150mMβ-巯基乙醇存在下，通过偶氮酪蛋白水解在98℃下测试活性。发现蛋白酶在98℃下的pH最佳值为6.8，并且在这些值下进行的分析中，在pH9.3下保留其活性高于45％，其pH值为4.5的活性为82％。蛋白酶通过抑制剂研究被分类为金属蛋白酶，肽水解显示胰蛋白酶样切割具有额外的活性。

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