α-Amylase from mung beans (Vigna radiata) – Correlation of biochemical properties and tertiary structure by homology modelling

Tripathi, Pallavi; Leggio, Leila Lo; Mansfeld, Johanna; Ulbrich‐Hofmann, Renate; Kayastha, Arvind M.

doi:10.1016/j.phytochem.2007.04.006

Cited by 42 publications

(44 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The optimal activity of DzAmy3 at pH 8.0 is in accordance with chloroplast α-amylase of AtAMY3 (pH 7.5-8.0). The plant α-amylases are highly active in acidic to neutral range (Ben Elarbi et al 2009;Kanwal et al 2004;Kumari et al 2010;Noman et al 2006;Tripathi et al 2007). We hypothesized that optimal activity at pH 8.0 is unique property for activity in the plastid stroma (Seung et al 2013).…”

Section: Organismmentioning

confidence: 94%

See 1 more Smart Citation

α-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

Posoongnoen

Ubonbal

Thammasirirak

et al. 2015

Plant Biotechnology

View full text Add to dashboard Cite

Amylase is hypothesized to involve in the initiation of intracellular starch granule digestion in the plastids of ripening durians. A putative α-amylase from Mon Thong durian (Durio zibethinus Murr. cv. Mon Thong; DzAmy3) was successfully isolated and its gene contain a 2,679 base pair open reading frame, which encodes 892 amino acids with a calculated molecular mass of 93.7 kDa and an isoelectric point of 5.77. The DzAmy3 contains starch binding domain with a putative plastid transit peptide and α-amylase like domain. Phylogenetic tree analysis proved it into the family three of plant α-amylases. The predicted structural model proposed a catalytic triad (Asp611, Glu636 and Asp719) for general acid/base hydrolysis. Recombinant DzAmy3 (rDzAmy3) was successfully expressed in Escherichia coli. rDzAmy3 hydrolyzed starch and ethylidene-pNP-G7 which confirms the authenticity of DzAmy3 gene and functional α-amylase. The rDzAmy3 had an optimum activity at pH 8.0 and 30°C. It was stable in the pH range of 7-8 at 37°C, temperature range of 5-20°C and in the presence of 1% (v/v) Tween 20 and Triton X-100. Substrate specificity analysis revealed that rDzAmy3 was active toward β-limit dextrin, starch, amylopectin, amylose and glycogen.

show abstract

Section: Organismmentioning

confidence: 94%

“…α-Amylases are found in animal organs, microorganisms, germinated cereal seeds and higher plants (Brena et al 1996). The amylase family currently accounts for approximately 30% of the world's enzyme production (van der Maarel et al 2002). This family has wide application in industries (Aiyer 2005;Souza and Magalhaes 2010).…”

mentioning

confidence: 99%

α-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

Posoongnoen

Ubonbal

Thammasirirak

et al. 2015

Plant Biotechnology

View full text Add to dashboard Cite

show abstract

“…and pea etc. (Greenwood et al, 1965;Beers and Duke, 1988;Tripathi et al, 2007). Kapoor (2005) has shown the presence of urease enzyme in D. biflorus.…”

Section: Effect Of Ph and Temperature On The Purified Enzymementioning

confidence: 99%

“…Production of α-amylase enzyme from germinating seedlings is a part and parcel of the life controlling processes of leguminous plants (Greenwood et al, 1965;Tripathi et al, 2007). Yield of amylase in germinating seedlings of this plant also comes out to be very high, as accounting to 27.7 IUml -1 , which simply proves that this plant source can be easily utilized in industry for extraction of this enzyme.…”

Section: Introductionmentioning

confidence: 99%

Partial purification and characterisation of some low molecular weight á - amylases from Dolichos biflorus

Garg

Dobriyal

2011

JANS

View full text Add to dashboard Cite

Dolichos biflorus, a commonly used legume in Uttarakhand, produces alpha amylase enzyme for conversion of starch present in its cotyledons to glucose, so that this glucose can be further utilized for the life controlling processes, glycolysis and Kreb's cycle. Yield of this α -amylase isolated from the germinating legume comes out to be 27.7 IUml -1 . Maximal amylase production occurs at pH 6.1 at 45 O C. The enzyme was purified two fold, first with ultra-filtration and then with Ion-exchange chromatography. Ultra-filtration revealed size of amylase to be between 10 kDa and 30 kDa, against larger sizes of other bacterial amylases. The pH and temperature optima for purified enzyme were 6.1 and 45 O C respectively. The K m for starch came out to be 1.95 mgml -1 . This finding of generating one more new and low-price source of α -amylase is a great advancement in biotechnology.

show abstract

“…This enzyme has been used for the degradation and saccharification of starch in the fields of food, bakery, paper, sugar and starch industries (Monfort et a., 1996;Pandey et al, 2000;Van der Maarel et al, 2002;Gupta et al, 2003). -Amylases distributes over bacteria, fungi, plants, invertebrates, and higher animals and many of these enzymes belong to glycoside-hydrolase-family 13 (GHF13) (Jensen and Olsen 1992;Henry et al, 1993;Iefuji et al, 1996;Le Moine et al, 1997;Koyama et al, 2000;Saxena et al, 2007;Tripathi et al, 2007;Hmidet et al, 2008;Elarbi et al, 2009;Nikapitiya et al, 2009). This enzyme plays a crucial role in the degradation of storage -glucan providing maltooligosaccharides and glucose, the most important carbon and energy sources in many organisms.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic properties and primary structures of two α-amylase isozymes from the Pacific abalone Haliotis discus hannai

Kumagai

Satoh

Inoue

et al. 2013

Comparative Biochemistry and Physiology Part B: Biochemistry an

View full text Add to dashboard Cite

Two -amylase (EC 3.2.1.1) isozymes, HdAmy58 and HdAmy82, with approximate molecular masses of 58 kDa and 82 kDa, respectively, were isolated from the digestive fluid of the pacific abalone Haliotis discus hannai. Optimal temperatures and pHs for HdAmy58 and HdAmy82 were at 30 o C and 6.7, and 30 o C and 6.1, respectively. Both enzymes similarly degraded starch, glycogen, and maltooligosaccharides larger than maltotriose producing maltose and maltotriose as the major degradation products. However, the activity toward maltotetraose was appreciably higher in HdAmy82 than HdAmy58. cDNAs encoding HdAmy58 and HdAmy82 were cloned and the amino-acid sequences of 511 and 694 residues for HdAmy58 and HdAmy82, respectively, were deduced. The putative catalytic domains of HdAmy58 and HdAmy82 were located in the 17-511 th and 19-500 th amino-acid regions, respectively, and they showed approximately 50% amino-acid identity to each other. These sequences also showed 62 -99% amino-acid identity to the catalytic domains of known -amylases that belong to glycoside-hydrolase-family 13. The difference in the molecular masses between HdAmy58 and HdAmy82 was ascribed to the extension of approximately 190 residues in the C-terminus of HdAmy82. This extended region showed 41 -63% amino-acid identity with the ancillary domains of several -amylases previously reported.

show abstract

α-Amylase from mung beans (Vigna radiata) – Correlation of biochemical properties and tertiary structure by homology modelling

Cited by 42 publications

References 45 publications

α-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

α-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

Partial purification and characterisation of some low molecular weight á - amylases from Dolichos biflorus

Enzymatic properties and primary structures of two α-amylase isozymes from the Pacific abalone Haliotis discus hannai

Contact Info

Product

Resources

About

α-Amylase from mung beans (Vigna radiata) – Correlation of biochemical properties and tertiary structure by homology modelling

Cited by 42 publications

References 45 publications

&#x3b1;-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

&#x3b1;-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

Partial purification and characterisation of some low molecular weight á - amylases from Dolichos biflorus

Enzymatic properties and primary structures of two α-amylase isozymes from the Pacific abalone Haliotis discus hannai

Contact Info

Product

Resources

About

α-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

α-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression