{'fraction_non_alphanumeric': 0.02619589977220957, 'fraction_numerical': 0.009111617312072893, 'mean_word_length': 6.088709677419355, '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}}
Cloning and expression of a Clostridium thermocellum xylanase gene in Escherichia coli

A Clostridium thermocellum xylanase gene, designated xynX, was cloned in Escherichia coli and was catagorized a novel gene as a result of the comparison of restriction patterns of the C. thermocellum xylanase genes so far reported. The xynX gene encodes a xylanase having the molecular weight of 105 kilodaltons. A number of smaller truncated proteins with activities towards 4‐methylumbelliferyl‐β‐d‐cellobioside and xylan were also produced. The enzyme hydrolyzed xylan to xylo‐oligosaccharide, indicating typical activity of endo‐β‐1,4‐xylanase. This endoxylanase hydrolyzed carboxymethylcellulose without notable reduction of the viscosity as an exo‐β‐1,4‐glucanase, even though the enzyme exhibited very low levels of activity against other soluble and insoluble cellulosic substrates.