Penicillium citrinum CFAM 521 Isolated From the Amazon Region: A Novel Source of a Fibrinolytic Enzyme.

IF 2.8 Q3 MICROBIOLOGY International Journal of Microbiology Pub Date : 2024-10-29 eCollection Date: 2024-01-01 DOI:10.1155/2024/5306083
Thayana Cruz de Souza, Marcos Gustavo Araujo Schwarz, Daniela Marinho da Silva, Carolina Rabelo Maia, Cláudia Patrícia Mendes de Araújo, Antônio Alcirley da Silva Balieiro, Luiz Antonio de Oliveira, Wim Maurits Sylvain Degrave, Ormezinda Celeste Cristo Fernandes, Leila Mendonça-Lima
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Abstract

Fibrinolytic agents are essential in treating thrombosis, playing a critical role in improving survival rates in cardiovascular diseases. Microbial fibrinolytic proteases have emerged as promising alternatives due to their affordability, specificity, lower toxicity, and reduced side effects. Consequently, the search for microorganisms capable of producing these enzymes has gained significant economic importance in the pharmaceutical industry. This study reports and characterizes a novel fibrinolytic enzyme produced by Penicillium citrinum CFAM 521, a strain isolated from the Amazon region. The enzyme was purified using a polyethylene glycol (PEG)-phosphate salt aqueous two-phase system (ATPS). The effects of PEG molecular weight, PEG concentration, and phosphate concentration on the protease partition coefficient (K) were evaluated through a 22 full factorial design. The enzyme exhibited both fibrinolytic and fibrinogenolytic activities. After partitioning in a two-phase system with 10% (w/w) PEG and 15% (w/w) sodium phosphate, the fibrinolytic proteases were predominantly retained in the salt-rich bottom phase (K = 0.33). The enzyme has a molecular weight of 34 kDa, with optimal pH and temperature at 9°C and 37°C, respectively. Inhibitory analysis confirmed that it is a serine protease, and its activity was enhanced by the addition of Mn2+. Notably, the enzyme exhibited no hemolytic activity. Therefore, P. citrinum CFAM 521 represents a novel source of fibrinolytic enzymes, highlighting its potential as an alternative for the development of thrombolytic agents.

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从亚马逊地区分离的柠檬青霉 CFAM 521:纤溶酶的新来源。
纤溶药物是治疗血栓形成的基本药物,在提高心血管疾病的存活率方面发挥着至关重要的作用。微生物纤溶蛋白酶因其价格低廉、特异性强、毒性低和副作用小等优点,已成为有前途的替代品。因此,寻找能够生产这些酶的微生物在制药业具有重要的经济意义。本研究报告了从亚马逊地区分离出的柠檬青霉 CFAM 521 产生的一种新型纤维蛋白溶解酶,并描述了其特性。该酶采用聚乙二醇(PEG)-磷酸盐水双相体系(ATPS)进行纯化。通过 22 个全因子设计,评估了 PEG 分子量、PEG 浓度和磷酸盐浓度对蛋白酶分配系数(K)的影响。该酶具有纤维蛋白溶解和纤维蛋白原溶解两种活性。在含有 10%(重量比)PEG 和 15%(重量比)磷酸钠的两相体系中分配后,纤溶蛋白酶主要保留在富含盐分的底相(K = 0.33)。该酶的分子量为 34 kDa,最佳 pH 值和温度分别为 9°C 和 37°C。抑制分析证实它是一种丝氨酸蛋白酶,加入 Mn2+ 可增强其活性。值得注意的是,该酶没有溶血活性。因此,P. citrinum CFAM 521 代表了一种新的纤维蛋白溶解酶来源,凸显了其作为开发血栓溶解剂替代品的潜力。
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来源期刊
CiteScore
7.90
自引率
0.00%
发文量
57
审稿时长
13 weeks
期刊介绍: International Journal of Microbiology is a peer-reviewed, Open Access journal that publishes original research articles, review articles, and clinical studies on microorganisms and their interaction with hosts and the environment. The journal covers all microbes, including bacteria, fungi, viruses, archaea, and protozoa. Basic science will be considered, as well as medical and applied research.
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