Yokoyama S, Oobayashi A, Tanabe O, Icheshima E
Appl Microbiol. 1974 Nov;28(5):742-7. doi: 10.1128/am.28.5.742-747.1974.
Penicillium janthinellum IFO-8070 produced an acid carboxypeptidase of molecular weight 51,000 in a liquid medium at 25 C. Maximum enzyme concentration was obtained within 3 to 6 days in a medium containing 2% wheat bran, 1% defatted soybean, and 1% KH(2)PO(4); the initial pH was 2 to 4. When submerged aerobic conditions were used, a 51,000-molecular-weight acid carboxypeptidase was produced and no detectable amounts of 160,000-molecular-weight acid carboxypeptidase were produced. Acid carboxypeptidase with a molecular weight of 51,000 was purified 330-fold from koji culture to yield a crystalline protein which was demonstrated by disc electrophoresis to be homogeneous. The purification method included ammonium sulfate fractionation, Amberlite CG-50 chromatography, acetone fractionation, Amberlite CG-50 rechromatography, and concentration in a collodion bag. The specific activity of the enzyme was about three times more than that of the acid carboxypeptidase from Aspergillus saitoi.
产黄青霉IFO - 8070在25℃的液体培养基中产生了一种分子量为51,000的酸性羧肽酶。在含有2%麦麸、1%脱脂大豆和1% KH₂PO₄的培养基中，3至6天内可获得最大酶浓度；初始pH值为2至4。当采用深层需氧条件时，产生了分子量为51,000的酸性羧肽酶，未检测到分子量为160,000的酸性羧肽酶。从曲霉菌培养物中纯化出分子量为51,000的酸性羧肽酶330倍，得到一种结晶蛋白，圆盘电泳显示其为纯一的。纯化方法包括硫酸铵分级分离、Amberlite CG - 50层析、丙酮分级分离、Amberlite CG - 50再层析以及在火棉胶袋中浓缩。该酶的比活性约为斋藤曲霉酸性羧肽酶的三倍。
