Partial purification characterization of Lactobacillus sp. G5 lipase and their probiotic potential

Rashmi B. S., . and Gayathri D., . Partial purification characterization of Lactobacillus sp. G5 lipase and their probiotic potential. pp. 1737-1743. ISSN 22317546

Lipase from Lactobacillus sp G5 isolate was partially purified and characterized. Out of 22 isolates only seven (G1-G7) were phenotypically and biochemically characterized as Lactobacillus. However only G5 isolate showed highest enzyme activity of 31.27 U/ml and chosen for partial purification and characterization. After ammonium sulphate precipitation and dialysis specific activity of the enzyme was found to be 0.770 IU. During optimization the enzyme showed maximum activity at pH 8/40C. Stability was found at pH range 7-9 with temperature range 30C-60C. The enzyme showed maximum activity at a pNPA concentration of 0.150 mg/1.5 ml/1 ml enzyme solution. Vmax and Km values were 27.32 U/ml and 0.04 mg/min. Among several substrates tested (tween-20 olive oil castor oil palm oil glycerol tributyrate and ghee) maximum affinity was observed towards glycerol tributyrate. Further the G5 isolate showed good number of probiotic qualities viz. tolerated 1.5 bile salt for 4 h and at 2 the viability decreased while luxuriant growth was observed at pH 3 and survived at pH 1 and 2 for 4 h. In addition G5 exhibited resistance to lincomycin and was sensitive to chlorotetracyclin. The results obtained in the present study would indicate the stability of Lactobacillus G5 isolate in hydrolyzing lipids and probably a promising probiotic candidate.

Full text available from: Official URL: http://ifrj.upm.edu.my/21%20(05)%202014/5%20IFRJ%2...

Abstract

Lipase from Lactobacillus sp G5 isolate was partially purified and characterized. Out of 22 isolates only seven (G1-G7) were phenotypically and biochemically characterized as Lactobacillus. However only G5 isolate showed highest enzyme activity of 31.27 U/ml and chosen for partial purification and characterization. After ammonium sulphate precipitation and dialysis specific activity of the enzyme was found to be 0.770 IU. During optimization the enzyme showed maximum activity at pH 8/40C. Stability was found at pH range 7-9 with temperature range 30C-60C. The enzyme showed maximum activity at a pNPA concentration of 0.150 mg/1.5 ml/1 ml enzyme solution. Vmax and Km values were 27.32 U/ml and 0.04 mg/min. Among several substrates tested (tween-20 olive oil castor oil palm oil glycerol tributyrate and ghee) maximum affinity was observed towards glycerol tributyrate. Further the G5 isolate showed good number of probiotic qualities viz. tolerated 1.5 bile salt for 4 h and at 2 the viability decreased while luxuriant growth was observed at pH 3 and survived at pH 1 and 2 for 4 h. In addition G5 exhibited resistance to lincomycin and was sensitive to chlorotetracyclin. The results obtained in the present study would indicate the stability of Lactobacillus G5 isolate in hydrolyzing lipids and probably a promising probiotic candidate.

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Item Type:	Article
AGROVOC Term:	Lactobacillus
AGROVOC Term:	Lipases
AGROVOC Term:	Probiotics
AGROVOC Term:	Purification
AGROVOC Term:	Disease prevention
Depositing User:	Ms. Suzila Mohamad Kasim
Last Modified:	24 Apr 2025 06:27
URI:	http://webagris.upm.edu.my/id/eprint/21843

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