PubMed · 5331620
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E D Wills. 1965. Lipases.. https://doi.org/10.1016/b978-1-4831-9939-9.50012-7
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Lipase I from Rhizopus niveus consists of two polypeptide chains bound non-covalently. Lipase I has been crystallized in a form suitable for X-ray diffraction analysis using the hanging drop method of vapour diffusion at 20 degrees C. The crystals grew at pH 6.0 to 7.0 using 14 to 16% polyethylene glycol 8000 as the precipitant. The crystals are tetragonal with space group P4(1) (or P4(3)) and cell dimensions of a = b = 83.7 A, c = 137.9 A. There are two protein molecules in the asymmetric unit. The diffraction pattern extends to at least 2.5 A resolution.
A method for detection of lipase in intestinal bacteria is suggested with fatty acid esters used as enzyme substrates. This modification not only allows the enzyme detection but is more rapid that the known procedures. Preliminary cultivation of bacteria in the accumulation media rich in organic substances helps shorten the time of investigation and simplifies reading the reaction.