淀粉样乳杆菌ATCC 33621生产葡萄糖淀粉酶的培养条件。

J A James, B H Lee
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引用次数: 18

摘要

淀粉样乳杆菌ATCC 33621是一种活性解淀粉菌菌株,可产生细胞结合的葡萄糖淀粉酶(EC 3.2.1.3)。采用不含葡萄糖的de Man-Rogosa-Sharpe (MRS)培养基,在1.5 l的发酵罐中,在不同的糊精浓度(0.1-1.5% (w/v))、pH(4.5-6.5)和温度(25-55℃)下,研究了生长和葡萄糖淀粉酶产生的条件。通过法压细胞处理细胞制备细胞提取物,以释放细胞内蛋白质。然后测定葡萄糖淀粉酶活性。考察了pH(4.0 ~ 9.0)、温度(15 ~ 85℃)和底物(糊精和淀粉,0 ~ 2% w/v)浓度对粗酶活性的影响。在含有1%糊精(w/v)的MRS培养基中,在pH 5.5和37℃条件下,葡萄糖淀粉酶的产量在对数生长后期16-18 h达到最大值。粗酶的最适pH为6.0,最适温度为60℃,淀粉为底物,在浓度为1.5% (w/v)时获得最大活性。研究了离子和抑制剂对葡萄糖淀粉酶活性的影响。1 mmol l-1浓度的Ca2+和EDTA对酶活性影响不显著;而Pb2+和Co2+在浓度为1 mmol l-1时对活性有抑制作用。当葡萄糖淀粉酶活性在60℃下暴露约10分钟后下降时,发现粗酶具有耐热性。这种特性可以用于酿造低热量啤酒,其中仅使用温和的巴氏灭菌处理来灭活酶。消除残留酶的作用可以防止麦芽糊精在长期储存过程中进一步降解和变甜,从而有助于啤酒风味的稳定。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Cultural conditions for production of glucoamylase from Lactobacillus amylovorus ATCC 33621.

Lactobacillus amylovorus ATCC 33621 is an actively amylolytic bacterial strain which produces a cell-bound glucoamylase (EC 3.2.1.3). Conditions of growth and glucoamylase production were investigated using dextrose-free de Man-Rogosa-Sharpe (MRS) medium in a 1.5 l fermenter, with varying dextrin concentration (0.1-1.5% (w/v)), pH (4.5-6.5) and temperature (25-55 degrees C). Cell extracts were prepared by subjecting cells to treatment with a French Pressure cell in order to release intracellular proteins. Glucoamylase activity was then assayed. The effects of pH (4.0-9.0), temperature (15-85 degrees C) and substrate (dextrin and starch, 0-2% w/v) concentration on crude enzyme activity were investigated. Optimal growth was obtained in MRS medium containing 1% (w/v) dextrin, at pH 5.5 and 37 degrees C. Glucoamylase production was maximal at the late logarithmic phase of growth, during 16-18 h. Crude enzyme had a pH optimum of 6.0 and temperature optimum of 60 degrees C. With starch as the substrate, maximal activity was obtained at a concentration of 1.5% (w/v). The effects of ions and inhibitors on glucoamylase activity were also investigated. Enzyme activity was not significantly influenced by Ca2+ and EDTA at 1 mmol l-1 concentration; however Pb2+ and Co2+ were found to inhibit the activity at concentrations of 1 mmol l-1. The crude enzyme was found to be thermolabile when glucoamylase activity decreased after about 10 min exposure at 60 degrees C. This property can be exploited in the brewing of low calorie beers where only mild pasteurization treatments are used to inactivate enzymes. The elimination of residual enzyme effect would prevent further maltodextrin degradation and sweetening during long-term storage, thus helping to stabilize the flavour of beer.

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