秘鲁Maras Salterns产肠杆菌M55株新l -天冬酰胺酶

IF 1.6 4区生物学 Q4 BIOTECHNOLOGY & APPLIED MICROBIOLOGY

Chemical and Biochemical Engineering Quarterly Pub Date : 2022-07-26 DOI:10.15255/cabeq.2022.2064

Abad Hurtado, J. Flores-Santos, C. N. Flores-Fernández, S. Saavedra, João H. P. M. Santos, A. Pessoa-Júnior, M. Lienqueo, M. Bayro, A. Zavaleta

{"title":"秘鲁Maras Salterns产肠杆菌M55株新l -天冬酰胺酶","authors":"Abad Hurtado, J. Flores-Santos, C. N. Flores-Fernández, S. Saavedra, João H. P. M. Santos, A. Pessoa-Júnior, M. Lienqueo, M. Bayro, A. Zavaleta","doi":"10.15255/cabeq.2022.2064","DOIUrl":null,"url":null,"abstract":"L-Asparaginase (ASNase) is used in medicine for neoplasms treatment and in food industry for mitigation of acrylamide in high-temperature processed food. In medicine, commercial ASNases have exhibited side effects and l -glutaminase (GLNase) activity affecting the clinical treatment. The aim of this work was to study a novel ASNase from Enterobacter sp. M55 isolated from Maras Salters in Peru, which was purified and biochemically characterised. This ASNase exhibited a K m of 5.71 mM and a V max of 0.16 µmol mL –1 min –1 , as well as an optimum temperature and pH of 37 °C and 6, respectively. Moreover, a good activity (80 %) was observed at physiological pH. Likewise, the enzyme increased its activity by around 50% in presence of urea, glutathione, and glucose. Whilst in presence of serum compounds, it kept more that 60 % of activity. In addition, this ASNase showed low GLNase activity.","PeriodicalId":9765,"journal":{"name":"Chemical and Biochemical Engineering Quarterly","volume":" ","pages":""},"PeriodicalIF":1.6000,"publicationDate":"2022-07-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"A Novel L-Asparaginase from Enterobacter sp. Strain M55 from Maras Salterns in Peru\",\"authors\":\"Abad Hurtado, J. Flores-Santos, C. N. Flores-Fernández, S. Saavedra, João H. P. M. Santos, A. Pessoa-Júnior, M. Lienqueo, M. Bayro, A. Zavaleta\",\"doi\":\"10.15255/cabeq.2022.2064\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"L-Asparaginase (ASNase) is used in medicine for neoplasms treatment and in food industry for mitigation of acrylamide in high-temperature processed food. In medicine, commercial ASNases have exhibited side effects and l -glutaminase (GLNase) activity affecting the clinical treatment. The aim of this work was to study a novel ASNase from Enterobacter sp. M55 isolated from Maras Salters in Peru, which was purified and biochemically characterised. This ASNase exhibited a K m of 5.71 mM and a V max of 0.16 µmol mL –1 min –1 , as well as an optimum temperature and pH of 37 °C and 6, respectively. Moreover, a good activity (80 %) was observed at physiological pH. Likewise, the enzyme increased its activity by around 50% in presence of urea, glutathione, and glucose. Whilst in presence of serum compounds, it kept more that 60 % of activity. In addition, this ASNase showed low GLNase activity.\",\"PeriodicalId\":9765,\"journal\":{\"name\":\"Chemical and Biochemical Engineering Quarterly\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":1.6000,\"publicationDate\":\"2022-07-26\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Chemical and Biochemical Engineering Quarterly\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.15255/cabeq.2022.2064\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOTECHNOLOGY & APPLIED MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Chemical and Biochemical Engineering Quarterly","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.15255/cabeq.2022.2064","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}

引用次数: 1

摘要

L-天冬氨酸酶（ASNase）在医学上用于肿瘤治疗，在食品工业中用于缓解高温加工食品中的丙烯酰胺。在医学上，商业ASNase表现出副作用和影响临床治疗的l-谷氨酰胺酶（GLNase）活性。本工作的目的是研究从秘鲁Maras Salters分离的肠杆菌M55中分离的一种新的ASNase，该ASNase经过纯化和生化鉴定。该ASNase的K m为5.71 mM，V max为0.16µmol mL–1 min–1，最佳温度和pH分别为37°C和6。此外，在生理pH下观察到良好的活性（80%）。同样，在尿素、谷胱甘肽和葡萄糖存在的情况下，该酶的活性增加了约50%。当存在血清化合物时，它保持了60%以上的活性。此外，这种ASNase显示出低的GLNase活性。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文本刊更多论文

A Novel L-Asparaginase from Enterobacter sp. Strain M55 from Maras Salterns in Peru

L-Asparaginase (ASNase) is used in medicine for neoplasms treatment and in food industry for mitigation of acrylamide in high-temperature processed food. In medicine, commercial ASNases have exhibited side effects and l -glutaminase (GLNase) activity affecting the clinical treatment. The aim of this work was to study a novel ASNase from Enterobacter sp. M55 isolated from Maras Salters in Peru, which was purified and biochemically characterised. This ASNase exhibited a K m of 5.71 mM and a V max of 0.16 µmol mL –1 min –1 , as well as an optimum temperature and pH of 37 °C and 6, respectively. Moreover, a good activity (80 %) was observed at physiological pH. Likewise, the enzyme increased its activity by around 50% in presence of urea, glutathione, and glucose. Whilst in presence of serum compounds, it kept more that 60 % of activity. In addition, this ASNase showed low GLNase activity.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Chemical and Biochemical Engineering Quarterly 工程技术-工程：化工

CiteScore

2.70

自引率

6.70%

发文量

审稿时长

>12 weeks

期刊介绍： The journal provides an international forum for presentation of original papers, reviews and discussions on the latest developments in chemical and biochemical engineering. The scope of the journal is wide and no limitation except relevance to chemical and biochemical engineering is required. The criteria for the acceptance of papers are originality, quality of work and clarity of style. All papers are subject to reviewing by at least two international experts (blind peer review). The language of the journal is English. Final versions of the manuscripts are subject to metric (SI units and IUPAC recommendations) and English language reviewing. Editor and Editorial board make the final decision about acceptance of a manuscript. Page charges are excluded.