Purification and characterization of an extracellular α-amylase produced by Lactobacillus manihotivorans LMG 18010T, an amylolytic lactic acid bacterium

被引:99
作者
Aguilar, G
Morlon-Guyot, J
Trejo-Aguilar, B
Guyot, JP
机构
[1] IRD, ORSTOM, Lab Biotechnol Microbienne Trop, Montpellier 1, France
[2] Univ Nacl Autonoma Mexico, Fac Quim, Dept Alimentos & Biotecnol, Mexico City 04510, DF, Mexico
关键词
alpha-amylase; lactic acid bacteria; Lactobacillus manihotivorans; starch; cassava sour starch;
D O I
10.1016/S0141-0229(00)00230-1
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
This work presents the purification and characterization of an extracellular alpha-amylase (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) produced by a new lactic acid bacterium: Lactobacillus manihotivorans able to produce L(+) lactic acid from starch. The molecular weight was found to be 135 kDa. The temperature and pH optimum were 55 degrees C and 5.5, respectively, and pI was 3.8. The alpha-amylase had good stability at pH range from 5 to 6 and the enzyme was sensitive to temperature, losing activity within 1 h of incubation at 55 degrees C. Higher thermal stability was observed when the enzyme was incubated in presence of soluble starch, K-m value and activation energy were 3.44 mg/ml and 32.55 kJ/mol, respectively. Amylose was found to be a better substrate than soluble starch and amylopectin. Al3+, Fe3+, and Hg2+ (10 mM) almost completely inhibited the alpha-amylase. (C) 2000 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:406 / 413
页数:8
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