Production and Purification of a New Chillproofing Enzyme and Its Properties |
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Authors: | Reisuke Takahashi Kanji Oda Kazu Okada Kei Arima |
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Institution: | 1. The Research Laboratories of Kirin Brewery Co., Ltd., Takasaki, Gumma Pref., Japan;2. Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo, Tokyo,Japan |
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Abstract: | Chillproofing enzyme was obtained from broth cultures of Serratia marcescens B–103. This extracellular enzyme, tentatively, named the S-enzyme was highly purified from the culture supernatant by ammonium sulfate precipitation, ethanol fractionation, gel filtration on Sephadex G–200 and column chromatography on DEAE-Sephadex A–50.The purified preparation appeared homogeneous on a ultracentrifugation with a sedimentation coefficient of 3.14 S and a molecular weight of 38,000~45,000 determined by the method of Whitaker.The S-enzyme hydrolyzed various proteins at pH 4~6 and at low temperature hydrolyzed nitrogenous substances which may cause chill haze in beer. So the chillproofing activity of the S-enzyme may be due to its proteolytic activity.The S-enzyme was stable at 4°C at pH 5~10.5. It was completely inactivated by heating at 60°C for 10 min, and was inactivated by Hg2+ and Pb2+ and activated by Mn2+, Ca2+. Mg2+ and Zn2+ |
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Keywords: | Japanese miso human RSa cells mutation ultraviolet C (UVC) glucose regulated protein 78 (GRP78) |
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