Three Different Types of α-Amylases from<i>Aspergillus awamori</i>KT-11: Their Purifications, Properties, and Specificities

Anindyawati, Trisanti; Melliawati, Ruth; K, Ito; Iizuka, Masaru; Minamiura, Noshi

doi:10.1271/bbb.62.1351

Cited by 18 publications

(8 citation statements)

References 21 publications

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“…Depending on whether the optical rotation has shifted downward or upward it can be deduced that if the hydrolyzed products have alpha or beta anomeric configuration respectively. This study verifies the family of the enzyme to which it fits in (Anindyawati et al, 1998).…”

Section: Degree Of Starch Hydrolysissupporting

confidence: 69%

Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application

Sachdev

Ojha

Mishra

2016

Int J Appl Sci Biotechnol

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Amylase is one of the leading enzymes used in industry from decades. The preliminary function of this enzyme is the hydrolysis of the starch molecule into glucose units and oligosaccharides. Amylases have spectacular application in broad spectrum of industries such as food, detergent, pharmaceutical and fermentation industries. Among different type of amylases α-amylase is in utmost demand because of its striking features. This particular enzyme is a good substitute over the chemicals catalyst used in industries. α-amylases can be acquired from different sources such as microorganism, animals and plants. Microorganisms are the major source of production of amylase because of the ease of availability, manipulation and operation. The starch converting enzymes is basically generated using submerged fermentation. Some of the prominent characteristics of amylase are its mode of action, substrate specificity and operating condition (temperature and pH). Amylases from different bacterial sources contribute differently to the particular trait of the enzyme. Bacillus amylases have been studied and applied so far because of their robustness in nature and easy accessible pure form of it. Thus this makes it more specific and fit for distinct application in the industry. The purpose of this manuscript was the comparative analysis of the physical and chemical features of α amylases from Bacillus species. It also focuses on the unique characteristics of this enzyme and their industrial applications.

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Section: Degree Of Starch Hydrolysissupporting

confidence: 69%

Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application

Sachdev

Ojha

Mishra

2016

Int J Appl Sci Biotechnol

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“…The strain is referred to as A. awamori KT-11 in this study. The mold was cultivated for enzyme production, and the preparation of enzymes was carried out according to the method described previously (Anindyawati et al, 1998a).…”

Section: Microorganismmentioning

confidence: 99%

“…Preparation of Amyl III and GA I Amyl III was prepared according to the method described previously (Anindyawati et al, 1998a) with a slight modification. Approximate 10 g of a seed culture were inoculated onto a medium consisted of 500 g of wheat bran (Miyake Flour Milling Co., Ltd. Osaka, Japan) and 500 ml of tap water in a pan (32 × 21.5 × 8.5 cm in size, 3 cm in thickness).…”

Section: Measurement Of Enzyme Activities and Protein Concentrationmentioning

confidence: 99%

“…A strain named A. awamori KT-11 is a black mold that produces three kinds of amylolytic enzymes, and they have been identified as α-amylase (Anindyawati et al, 1998a), glucoamylase and α-glucosidase (Anindyawati et al, 1998b), in an extract from koji culture using wheat bran in the medium. We purified Amyl III (α-amylase), and GA I (glucoamylase) from a culture of this strain.…”

Section: Introductionmentioning

confidence: 99%

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Degradation of Raw Starch Granules by α-Amylase Purified from Culture of Aspergillus awamori KT-11

Matsubara¹,

Ammar²,

Anindyawati³

et al. 2004

BMB Reports

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Raw-starch-digesting α-amylase (Amyl III) was purified to an electrophoretically pure state from the extract of a koji culture of Aspergillus awamori KT-11 using wheat bran in the medium. The purified Amyl III digested not only soluble starch but also raw corn starch. The major products from the raw starch using Amyl III were maltotriose and maltose, although a small amount of glucose was produced. Amyl III acted on all raw starch granules that it has been tested on. However, it was considered that the action mode of the Amyl III on starch granules was different from that of glucoamylase judging from the observation of granules under a scanning electron microscope before and after enzyme reaction, and also from the reaction products. Glucoamylase (GA I) was also isolated and it was purified to an electrophoretically pure state from the extract. It was found that the electron micrographic features of the granules after treatment with the enzymes were quite different. A synergistic effect of Amyl III and GA I was observed for the digestion of raw starch granules.

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“…We previously reported that Aspergillus awamori KT-11, a black mold which was isolated from Indonesia air, produced three kinds of amylolytic enzymes (Anindyawati et al, 1998b). They were identified as α-amylases (named Amyl I, Amyl II and Amyl III), glucoamylase (GA I) and α-glucosidases (Anindyawati et al, 1998a).…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning and Determination of the Nucleotide Sequence of Raw Starch Digesting α-Amylase from Aspergillus awamori KT-11

Matsubara¹,

Ammar²,

Anindyawati³

et al. 2004

BMB Reports

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Complementary DNAs encoding α-amylases (Amyl I, Amyl III) and glucoamylase (GA I) were cloned from Aspergillus awamori KT-11 and their nucleotide sequences were determined. The sequence of Amyl III that was a raw starch digesting α-amylase was found to consist of a 1,902 bp open reading frame encoding 634 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. On the other hand, the sequence of Amyl I, which cannot act on raw starch, consisted of a 1,500 bp ORF encoding 499 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. The sequence of GA I consisted of a 1,920 bp ORF that encoded 639 amino acids. The signal peptide was composed of 24 amino acids. The amino acid sequence of Amyl III from the N-terminus to the amino acid number 499 showed 63.3% homology with Amyl I. However, the amino acid sequence from the amino acid number 501 to C-terminus, including the rawstarch-affinity site and the TS region rich in threonine and serine, showed 66.9% homology with GA I.

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Three Different Types of α-Amylases fromAspergillus awamoriKT-11: Their Purifications, Properties, and Specificities

Cited by 18 publications

References 21 publications

Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application

Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application

Degradation of Raw Starch Granules by α-Amylase Purified from Culture of Aspergillus awamori KT-11

Molecular Cloning and Determination of the Nucleotide Sequence of Raw Starch Digesting α-Amylase from Aspergillus awamori KT-11

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