Salt-independent thermophilic 伪-amylase from Bacillus megaterium VUMB109: An efficacy testing for preparation of maltooligosaccharides

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• 作者：Malabendu Jana^a ; Chiranjit Maity^b ; ^{riwkchiranjit@yahoo.co.in} ; Saptadip Samanta^b ; Bikas Ranjan Pati^b ; Syed Sirajul Islam^c ; Pradeep K. Das Mohapatra^b ; Keshab Chandra Mondal^b ; ^{mondalkc@gmail.com}
• 关键词：伪-Amylase ; Oligosaccharides ; Maltotriose ; Maltopentose ; Bacillus megaterium
• 刊名：Industrial Crops and Products
• 出版年：2013
• 期刊代码：56_09266690
• 类别：abs
• 出版时间：January, 2013
• 卷：41
• 期：Complete
• 页码：386-391
• 文件大小：614 K

摘要

An amylase (est. M_w 150 kDa) was purified 27.39-folds from the culture broth of Bacillus megaterium VUMB109. The purified enzyme was not inhibited by p-chloromercuro benzoate and iodoacetamide (10 mM), it rapidly decolorized the blue color of starch-iodine complex and produced 伪-anomeric products from starch hydrolysis, thus, it is an endo-attacking 伪-amylase. The enzymatic activity was not affected by any metal ion and EDTA, therefore, it is not in the class of metalloenzyme. The purified 伪-amylase showed higher affinity (K_m = 1.5 渭M; V_max/K_m = 0.38 and K_cat/K_m = 2.5 脳 10⁶) to starch than other tested substrates like amylose, amylopectin and glycogen. Maltooligomer mixture with high proportion of maltopentaose (G5) and maltotriose (G3) was produced during hydrolysis of starch, amylopectin and amylose. It exhibited high degree of hydrolysis on raw potato starch than wheat, rice and corn starches. Thus the studied 伪-amylase could be exploited as a useful catalyst in the bioprocessing of maltooligomer mixture as food supplement for baby and aged people.