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Lipase activity of Lactobacillus brevis

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Summary

The intracellular lipase from a strain of Lactobacillus brevis was partially purified and properties of the enzyme studied. Of the simple triglycerides, tripropionin was hydrolysed most easily by the enzyme as compared to others such as tributyrin, tricaproin and tricaprylin. Of the natural triglycerides such as butter oil and coconut oil, the former was degraded more readily than the latter. Among unsaturated triglycerides, the enzyme preferentially hydrolysed triolein as compared to olive oil. Highest enzymatic activity was observed at 30° C after 3.5 h incubation at pH 6.5. Salts of manganese, magnesium, sodium and calcium stimulated lipase activity while silver, mercury and Zinc were inhibitory. The enzyme was completely inactivated at 62.8° C after 30 min and at 71.7° C after 16 sec.

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Authors and Affiliations

  1. National Dairy Research Institute, Karnal, India

    Harish Chander, N. B. Chebbi & B. Ranganathan

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  1. Harish Chander
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  2. N. B. Chebbi
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  3. B. Ranganathan
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Chander, H., Chebbi, N.B. & Ranganathan, B. Lipase activity of Lactobacillus brevis . Archiv. Mikrobiol. 92, 171–174 (1973). https://doi.org/10.1007/BF00425014

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  • DOI: https://doi.org/10.1007/BF00425014

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