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หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Screening of Halophilic Lipase-Producing Bacteria and Characterization of Enzyme for Fish Sauce Quality Improvement) ผู้เขียน:Werasit Kanlayakrit, อนันต์ บุญปาน สื่อสิ่งพิมพ์:pdf AbstractTwenty pure bacterial cultures isolated from Thai fish sauce were selected for lipase producing on Sehgal and Gibbons Complex (SGC)-Tween 80 agar containing 0-4 M NaCl. The results showed that isolate PB233 could produce the highest lipase activity. This isolate was identified based on morphological, physiological characteristics and compared 16S rRNA sequence to other bacteria. It was concluded that isolate PB233 belonged to Staphylococcus warneri. This strain could grow in 0-4 M NaCl but the best growth was observed at 0 M NaCl. Therefore, Staphylococcus warneri was classified as halotolerant bacteria. A halotolerant Staphylococcus warneri PB233 was cultured in mini jar fermenter using SGC medium containing 1% olive oil and 3 M NaCl. A typical pattern of lipase production showed that enzyme secretion was coupled to active cell multiplication and maximum activity was obtained at a stationary phase. The maximum production of lipase (90.12 U/ml) was observed at 48 hr. The lipase had optimum at pH 7.0 and at temperature of 40?C. It was stable between pH 7.0 and 9.0 and at temperatures between 30 and 40?C. This enzyme had marked halophilic enzyme properties and showed maximal activities in the presence of 2.5 M (15%) NaCl. |
หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Extracellular Halophilic Ribonuclease from a Halotolerant Pseudomonas sp. : Purification and Characterization) ผู้เขียน:Werasit Kanlayakrit, อนันต์ บุญปาน, Takahiro IKEDA, Somporn Tojai สื่อสิ่งพิมพ์:pdf AbstractA halotolerant bacterium, Pseudomonas sp. No. 3241, isolated from Thai fish sauce obtained in Suratthani province, produced an extracellular ribonuclease when cultivated aerobically without NaCl in Sehgal and Gibbons complex medium (SGC medium). Ribonuclease was purified by ethanol precipitation, Sephadex G-150 gel filtration and DEAE Toyopearl 650M anion-exchange chromatography. The purity and molecular weight were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The result showed that the molecular weight of ribonuclease from halotolerant Pseudomonas sp. No. 3241 was 61,000 daltons. Purified ribonuclease was optimum at pH 10.0 and at temperature of 40?C. Purified ribonuclease was stable between pH 6.0 and 10.0 and at temperatures between 30 and 40?C. This enzyme had marked halophilic enzyme properties that required an optimum NaCl concentration of 3.0 M (18%). |
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Researcherดร. สาวิตร ตระกูลน่าเลื่อมใส, ผู้ช่วยศาสตราจารย์ที่ทำงาน:สำนักงานเลขานุการ วิทยาลัยบูรณาการศาสตร์ สาขาที่สนใจ:สรีรวิทยาและชีววิทยาระดับโมเลกุลของแบคทีเรีย (Physiology and Molecular biology of Bacteria), อนุกรมวิธานระดับโมเลกุลของจุลินทรีย์ (•Molecular Systematics of Microorganisms), วิศวกรรมโปรตีน (Protein Engineering) Resume |
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