Decomposition of Insoluble and Hard-to-Degrade Animal Proteins by Enzyme E77 and Its Potential Applications |
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Authors: | Hui Zhao Shinji Mitsuiki Mikako Takasugi Masashi Sakai Masatoshi Goto Hiroaki Kanouchi Tatsuzo Oka |
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Affiliation: | (1) Laboratory for Conservation and Utilization of Bio-resources, Yunnan University, Kunming, 650091, China;(2) Department of Applied Chemistry and Biochemistry, Kyushu Sangyo University, Fukuoka 813-8503, Japan;(3) Division of Bioresource and Bioenviromental Sciences, Kyushu University, Fukuoka 812-8581, Japan;(4) Department of Veterinary Physiology, Kagoshima University, Kagoshima 890-0065, Japan; |
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Abstract: | Insoluble and hard-to-degrade animal proteins are group of troublesome proteins, such as collagen, elastin, keratin, and prion proteins that are largely generated by the meat industry and ultimately converted to industrial wastes. We analyzed the ability of the abnormal prion protein-degrading enzyme E77 to degrade insoluble and hard-to-degrade animal proteins including keratin, collagen, and elastin. The results indicate that E77 has a much higher keratinolytic activity than proteinase K and subtilisin. Maximal E77 keratinolytic activity was observed at pH 12.0 and 65 °C. E77 was also adsorbed by keratin in a pH-independent manner. E77 showed lower collagenolytic and elastinolytic specificities than proteinase K and subtilisin. Moreover, E77 treatment did not damage collagens in ovine small intestines but did almost completely remove the muscles. We consider that E77 has the potential ability for application in the processing of animal feedstuffs and sausages. |
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