A review discussing the history of potato as a food, functional effects of natural pigment anthocyanin, development of anthocyanin-rich red potato varieties in Japan (inca red and inca purple), and the effect of the potato anthocyanin on prevention of stomach carcinogenesis in mice is provided.

Seibutsu Kogaku Kaishi

Purification and properties of a low-temperature-active enzyme degrading both cellulose and xylan from Acremonium alcalophilum JCM 7366

Author: Hayashi, Kazuya ; Ohara, Naohiro ; Kozaki, Michio ; Komagata, Kazuo ; Uchimura, Tai ; Nimura, Youchi ; Miiyaji, Tatsuro ; Suzuki, Hideo

A low-temperature-active CMCase from Acremonium alcalophilum JCM 7366 was purified by ammonium sulfate fractionation, QAE-Toyopearl 650c column chromatog., TSK gel ether-5PW high performance liquid column chromatog., and TSK gel G3000SWxl high performance liquid column chromatog.The mol. weight of the purified enzyme was estimated to be 46,000 and 48,000 by SDS-PAGE and TSK gel G3000SWxl gel filtration, resp.The isoelec. point was 4.4.The purified enzyme hydrolyzed CMC, and xylan.The main products after 24-h digestion of CMC or xylan were cellobiose or xylobiose, resp.The maximal CMCase and xylanase activities of the purified low-temperature-active enzyme were obtained at 40° and pH 7.0.The CMCase and xylanase activities of this enzyme at 0° were about 25.0% and 48.8%, resp., of its activities at 40°.Both these enzyme activities were stable at pH 5.5 to 10.0, and at 50° for 10 min.

Seibutsu Kogaku Kaishi

Low temperature-active cellulase produced by Acremonium alcaliphilum JCM 7366

Author: Hayashi, Kazuya ; Kozaki, Michio ; Komagata, Kazuo ; Uchimura, Tai ; Suzuki, Hideo ; Ohara, Naohiro ; Nimura, Youichi

A fungus which produced alk. cellulase was isolated from soil in Kanagawa prefecture, Japan, using cellulose as a substrate, under alk. conditions.The fungus was given the name A. alcaliphilum JCM 7366.The characteristics of the crude fungal cellulase were studied.The fungus produced carboxymethylcellulase (CMCase) and xylanase, whose activities were found even at 0° and under both alk. and acidic conditions.The maximal activities of the low-temperature-active CMCase and xylanase were obtained at 40° and pH 7.0, the maximal pH at 0° being the same as at 40°.At 0°, the activities of these enzymes were retained to the extent of >20% in the case of CMCase, and >40% in the case of xylanase, with respect to their activities at 40°.Low temperature-active CMCase and xylanase were induced in the presence of glucose as C source, but not in the presence of cellobiose and sophorose as C sources.

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