Ghofran M Al-Harbi, Essam Kotb, Abeer A Almiman, Mahmoud M Berekaa, Salwa Alhamad, Nada F Alahmady, Meneerah A Aljafary, Nadiyah M Alqazlan, Reem I Alyami, Joud M Alqarni, Ebtesam Abdullah Al-Suhaimi
{"title":"阿拉伯-波斯湾地区l -天冬酰胺酶产菌的分离与鉴定:厦门芽孢杆菌ASP-J1-4产菌及其潜在应用初报","authors":"Ghofran M Al-Harbi, Essam Kotb, Abeer A Almiman, Mahmoud M Berekaa, Salwa Alhamad, Nada F Alahmady, Meneerah A Aljafary, Nadiyah M Alqazlan, Reem I Alyami, Joud M Alqarni, Ebtesam Abdullah Al-Suhaimi","doi":"10.3390/md23050194","DOIUrl":null,"url":null,"abstract":"<p><p>L-asparaginase (L-ASNase) functions as a chemotherapeutic enzyme with antitumor properties. It facilitates the degradation of L-asparagine (L-ASN), a vital amino acid required for the proliferation of tumor cells. In this study, we have isolated 177 L-ASNase-producing strains from the aquatic environment of the Arabian-Persian Gulf. The most potent isolate, ASP-J1-4, was an endophyte recovered from the seablite <i>Suaeda maritima</i> and was molecularly identified as <i>B. xiamenensis</i> (accession number PQ593941). The enzyme purified through DEAE-Sepharose displayed a molecular weight of 37 kDa based on the SDS-PAGE profile and lacked detectable L-glutaminase (L-GTNase) activity. Optimal enzyme activity was at 40 °C and pH 9.0, with stability at pH 7-9. The maximum stimulation effect was found in the presence of Fe<sup>3+</sup>, Mn<sup>2+</sup>, and Na<sup>+</sup> ions, respectively. The enzyme demonstrated a <i>V</i><sub>max</sub> of 35.71 U/mL and a <i>K</i><sub>m</sub> of 0.15 mM. Interestingly, ASP-J1-4 L-ASNase showed a dose-dependent inhibition against human colon carcinoma (HCT-116) and cervical Henrietta Lacks (HeLa) cell lines, with IC<sub>50</sub> values of 15.42 µg/mL and 12.13 µg/mL, respectively. These findings collectively suggest a biocompatible, efficient, and robust enzyme for potential applications in tumor therapy after validation of in vivo studies and clinical trials. This study introduces the first deep screening program for L-ASNase-producing bacteria harboring in the Arabian-Persian Gulf region. In addition, it launches <i>B. xiamenensis</i> and other species as new sources of L-ASNase.</p>","PeriodicalId":18222,"journal":{"name":"Marine Drugs","volume":"23 5","pages":""},"PeriodicalIF":4.9000,"publicationDate":"2025-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12113540/pdf/","citationCount":"0","resultStr":"{\"title\":\"Isolation and Characterization of L-Asparaginase-Producing Bacteria from the Arabian-Persian Gulf Region: First Report on <i>Bacillus xiamenensis</i> ASP-J1-4 as a Producer and Its Potential Application.\",\"authors\":\"Ghofran M Al-Harbi, Essam Kotb, Abeer A Almiman, Mahmoud M Berekaa, Salwa Alhamad, Nada F Alahmady, Meneerah A Aljafary, Nadiyah M Alqazlan, Reem I Alyami, Joud M Alqarni, Ebtesam Abdullah Al-Suhaimi\",\"doi\":\"10.3390/md23050194\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>L-asparaginase (L-ASNase) functions as a chemotherapeutic enzyme with antitumor properties. It facilitates the degradation of L-asparagine (L-ASN), a vital amino acid required for the proliferation of tumor cells. In this study, we have isolated 177 L-ASNase-producing strains from the aquatic environment of the Arabian-Persian Gulf. The most potent isolate, ASP-J1-4, was an endophyte recovered from the seablite <i>Suaeda maritima</i> and was molecularly identified as <i>B. xiamenensis</i> (accession number PQ593941). The enzyme purified through DEAE-Sepharose displayed a molecular weight of 37 kDa based on the SDS-PAGE profile and lacked detectable L-glutaminase (L-GTNase) activity. Optimal enzyme activity was at 40 °C and pH 9.0, with stability at pH 7-9. The maximum stimulation effect was found in the presence of Fe<sup>3+</sup>, Mn<sup>2+</sup>, and Na<sup>+</sup> ions, respectively. The enzyme demonstrated a <i>V</i><sub>max</sub> of 35.71 U/mL and a <i>K</i><sub>m</sub> of 0.15 mM. Interestingly, ASP-J1-4 L-ASNase showed a dose-dependent inhibition against human colon carcinoma (HCT-116) and cervical Henrietta Lacks (HeLa) cell lines, with IC<sub>50</sub> values of 15.42 µg/mL and 12.13 µg/mL, respectively. These findings collectively suggest a biocompatible, efficient, and robust enzyme for potential applications in tumor therapy after validation of in vivo studies and clinical trials. This study introduces the first deep screening program for L-ASNase-producing bacteria harboring in the Arabian-Persian Gulf region. 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Isolation and Characterization of L-Asparaginase-Producing Bacteria from the Arabian-Persian Gulf Region: First Report on Bacillus xiamenensis ASP-J1-4 as a Producer and Its Potential Application.
L-asparaginase (L-ASNase) functions as a chemotherapeutic enzyme with antitumor properties. It facilitates the degradation of L-asparagine (L-ASN), a vital amino acid required for the proliferation of tumor cells. In this study, we have isolated 177 L-ASNase-producing strains from the aquatic environment of the Arabian-Persian Gulf. The most potent isolate, ASP-J1-4, was an endophyte recovered from the seablite Suaeda maritima and was molecularly identified as B. xiamenensis (accession number PQ593941). The enzyme purified through DEAE-Sepharose displayed a molecular weight of 37 kDa based on the SDS-PAGE profile and lacked detectable L-glutaminase (L-GTNase) activity. Optimal enzyme activity was at 40 °C and pH 9.0, with stability at pH 7-9. The maximum stimulation effect was found in the presence of Fe3+, Mn2+, and Na+ ions, respectively. The enzyme demonstrated a Vmax of 35.71 U/mL and a Km of 0.15 mM. Interestingly, ASP-J1-4 L-ASNase showed a dose-dependent inhibition against human colon carcinoma (HCT-116) and cervical Henrietta Lacks (HeLa) cell lines, with IC50 values of 15.42 µg/mL and 12.13 µg/mL, respectively. These findings collectively suggest a biocompatible, efficient, and robust enzyme for potential applications in tumor therapy after validation of in vivo studies and clinical trials. This study introduces the first deep screening program for L-ASNase-producing bacteria harboring in the Arabian-Persian Gulf region. In addition, it launches B. xiamenensis and other species as new sources of L-ASNase.
期刊介绍:
Marine Drugs (ISSN 1660-3397) publishes reviews, regular research papers and short notes on the research, development and production of drugs from the sea. Our aim is to encourage scientists to publish their experimental and theoretical research in as much detail as possible, particularly synthetic procedures and characterization information for bioactive compounds. There is no restriction on the length of the experimental section.