{'fraction_non_alphanumeric': 0.021739130434782608, 'fraction_numerical': 0.00644122383252818, 'mean_word_length': 5.473958333333333, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Purification of Lipase: A Review

The review spans a decade of research work ranging from 1989 to 1999, and reviews numerous articles dealing with lipase purification. Different purification techniques and their relation to the source of the enzyme are examined. It has been observed that some proteins tend to be unstable in solution, and pose several problems during separation. Various difficulties encountered during separation, and approaches to solve them are analyzed. Comparison is made with respect to three parameters, namely, specific activity, activity recovery, and purification factor. A one-on-one comparison of a specific purification technique (especially in chromatography) is difficult if not impossible, due to the different kinds of packing used. However, it is possible to classify separation by type such as gel filtration chromatography, affinity chromatography, ion exchange chromatography and so on. Since protein purification is normally done in a series of sequential chromatographic steps involving a combination of the above-mentioned techniques, the effect of the order or sequence of steps on the final purification level is examined. This is of crucial importance when planning protein purification protocols.