Optimization and Production of Hyaluronidase by Streptococcus mitis MTCC 2695

Narayanan, Mahesh

doi:10.4172/2167-7956.1000101

Cited by 7 publications

(6 citation statements)

References 28 publications

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“…The selected isolate was cultured in 50 ml medium Erlenmeyer flasks and incubated at different temperatures, 25 °C, 30 °C ,37 °C and 45 °C. All flasks were shaking incubated at 150 rpm for 24 h. The cell free centrifugate was obtained at 4000 rpm centrifugation for 30 min using Beckman centrifuge (Model-Avanti™ -25 Beckman Co., U.S.A) and used for enzyme assay [ 48 ].…”

Section: Methodsmentioning

confidence: 99%

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Purification and characterization of the produced hyaluronidase by Brucella Intermedia MEFS for antioxidant and anticancer applications

Ebraheem,

El-Fakharany,

Husseiny

et al. 2024

Microb Cell Fact

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Hyaluronidase (hyase) is an endoglycosidase enzyme that degrades hyaluronic acid (HA) and is mostly known to be found in the extracellular matrix of connective tissues. In the current study, eleven bacteria isolates and one actinomycete were isolated from a roaster comb and screened for hyase production. Seven isolates were positive for hyase, and the most potent isolate was selected based on the diameter of the transparent zone. Based on the morphological, physiological, and 16 S rRNA characteristics, the most potent isolate was identified as Brucella intermedia MEFS with accession number OR794010. The environmental conditions supporting the maximum production of hyase were optimized to be incubation at 30 ºC for 48 h and pH 7, which caused a 1.17-fold increase in hyase production with an activity of 84 U/mL. Hyase was purified using a standard protocol, including precipitation with ammonium sulphate, DEAE as ion exchange chromatography, and size exclusion chromatography using Sephacryle S100, with a specific activity of 9.3-fold compared with the crude enzyme. The results revealed that the molecular weight of hyase was 65 KDa, and the optimum conditions for hyase activity were at pH 7.0 and 37 °C for 30 min. The purified hyase showed potent anticancer activities against colon, lung, skin, and breast cancer cell lines with low toxicity against normal somatic cells. The cell viability of hyase-treated cancer cells was found to be in a dose dependent manner. Hyase also controlled the growth factor-induced cell cycle progression of breast cancer cells and caused relative changes in angiogenesis-related genes as well as suppressed many pro-inflammatory proteins in MDA cells compared with 5-fluorouracil, indicating the significant role of hyase as an anticancer agent. In addition, hyase recorded the highest DPPH scavenging activity of 65.49% and total antioxidant activity of 71.84% at a concentration of 200 µg/mL.

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Section: Methodsmentioning

confidence: 99%

“…The suitable fermentation period supporting the maximum production of enzyme was investigated at different periods, 16,24, 48, 72 and 96 h at 150 rpm [ 48 ].…”

Section: Methodsmentioning

confidence: 99%

Purification and characterization of the produced hyaluronidase by Brucella Intermedia MEFS for antioxidant and anticancer applications

Ebraheem,

El-Fakharany,

Husseiny

et al. 2024

Microb Cell Fact

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“…Studies revealed that hly plays a significant role in producing proinflammatory cytokines (Campo et al, 2012). Furthermore, hly is a means of enhancing mobility across the body's tissues, and as an antigenic distinguish that prevents their being recognized by phagocytes of the immune system (Mahesh et al, 2012). as a result, hly is an important factor in the pathogenicity of GBS.…”

Section: Detection Of Hly Genementioning

confidence: 99%

Distribution Of Virulence Factors Genes And Their Association With Antibiotics Resistance In Streptococcus Agalactiae Isolated From Pregnant Women In Al Anbar City

Alani¹,

Meani²

2022

Journal of Pharmaceutical Negative Results

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Group B streptococci (GBS) are globally recognized to cause adverse pregnancy outcomes, such as stillbirths and miscarriages, andare one of the main causes of newborn sepsis and meningitis. The high resistance of GBS to antibiotics becomes difficult orimpossible to treat, becoming increasingly common, causing a global health crisis. It complicates their eradication, potentiallyleading to the development of chronic infections. A total of 181 specimens were obtained from pregnant women. Out of thesespecimens, 22 isolates were bacteriologically identified as S.agalactiae. They were collected from Al-Anbar Province hospitals.Twenty-two isolates were identified as GBS depending on cultural and microscopical properties, automated (VITEK-2 system), andmolecular identification based on atr gene, which is an essential gene expressed isolates in all S.agalactiae. Polymerase chain reaction(PCR) was used to detect the prevalence of virulence factors and antibiotic resistance genes; ermB gene was found in 22/22(100%),hly gene in twenty-one isolates (95.45%), scpB also found in twenty-one isolates (95.45%), tet gene (95.45%), mefA gene12/22(54.54%), Rib gene was found only in five isolates (22.72%), bca found in three isolates only (13.63%), bac not found in anyisolates(0%).

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“…Hyaluronidases are naturally found in mammals, insects, leaches and bacteria (Bertolami & Donoff, 1982). Several prokaryotic microorganisms produced hyaluronate lyases as Streptomyces (Laurent & Fraser, 1992), Staphylococcus (Ahmed, 2014) and Streptococcus (Mahesh et al, 2012) were different in substrate specificity. Different sources of hyaluronidases vary in their molecular weight, based on substrate specificity, pH optima and catalytic mechanism (Yingprasertchai et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Characterization and Immobilization of A Novel Hyaluronidase Produced By Streptomyces roseofulvus

Reda

El-Shanawany

2019

Egypt. J. Bot.

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M AXIMUM hyaluronidase production by Streptomyces roseofulvus S10 (LC314796) was attained when it was cultured in submerged fermentation process under favorable conditions, pH 5 at 40ºC for 6 days. Hyaluronidase was purified to its homogeneity by 9.2 fold with molecular weight of 97kDa under denaturing SDS-PAGE. Mg +2 exerted highly stimulatory effect on S. roseofulvus S10 hyaluronidase activity and was significantly reduced in presence of Mn +2 , Zn +2 , and EDTA. Optimum reaction was attained at pH 9 and the pH stability of enzyme ranged between 9-10 at 35°C. To protect the intrinsic activity and halftime of hyaluronidase, several carriers and immobilization of hyaluronidase were investigated. The immobilized enzyme had higher thermal stability than free one with T m values; 46.1°C and 24.7°C, respectively. Maximum affinity of free and immobilized hyaluronidase was for hyaluronic acid followed by bovine albumin. Free enzyme had a high catalytic affinity of hyaluronic acid compared with immobilized enzyme. Our results demonstrated that S. roseofulvus S10 hyaluronidase was highly stable to pH and high temperature. These properties of long-term stability facilitate its wide range of applications.

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Optimization and Production of Hyaluronidase by Streptococcus mitis MTCC 2695

Cited by 7 publications

References 28 publications

Purification and characterization of the produced hyaluronidase by Brucella Intermedia MEFS for antioxidant and anticancer applications

Purification and characterization of the produced hyaluronidase by Brucella Intermedia MEFS for antioxidant and anticancer applications

Distribution Of Virulence Factors Genes And Their Association With Antibiotics Resistance In Streptococcus Agalactiae Isolated From Pregnant Women In Al Anbar City

Characterization and Immobilization of A Novel Hyaluronidase Produced By Streptomyces roseofulvus

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