Production, purification and characterization of an α-amylase produced by Saccharomycopsis fibuligera

Gogoi, Barnali; Bezbaruah, R. L.; Pillai, K. R.; Baruah, J. N.

doi:10.1111/j.1365-2672.1987.tb05162.x

Cited by 7 publications

(11 citation statements)

References 31 publications

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“…The isolation and purification were conducted based on published methods 16,17 . The activity test of -amylase was performed with Fuwa method 18 and Mandels 19 method.…”

Section: Methods 221 Isolation Purification and Activity Test Of mentioning

confidence: 99%

Increasing Stability of a-amylase Obtained from Bacillus subtilis ITBCCB148 by Immobilization with Chitosan

Yandri¹,

Suhartati²,

Satria³

et al. 2020

Mediterr.J.Chem.,

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In this research, the immobilization of α-amylase from Bacillus subtilis ITBCCB148 by crosslinking method on chitosan matrix has been performed. This research aims to know the effect of immobilization on the thermal stability of α-amylase. The results showed that the native α-amylase has an optimum temperature of 65oC, KM = 1.6 mg mL-1 substrate, and Vmax = 39.7 µmol mL-1 min-1. The immobilized α-amylase has optimum temperature of 75oC, KM = 3.5 mg mL-1 substrate, and Vmax = 7.05 µmol mL-1 min-1. The residual activity of the native and immobilized enzyme on thermal stability test at 65oC for 80 minutes was 58% and 86.15%, respectively. The immobilized enzyme can be reused up to six repeated cycles.The thermodynamic data of native enzyme was t½ = 113.6 min, ki = 6.1x10-3 min-1, and ΔGi = 107.3 kJ mol-1, while the immobilized enzyme was t½ = 433.1 min, ki= 1.6x10-3 min-1, and ΔGi 111.1 kJ mol-1. Based on the decrease of ki, and the increase of ΔGi and half-life(t½) values, the immobilization of α-amylase with chitosan can increase the thermal stability of this enzyme.

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“…The isolation and purification were conducted based on published methods 16,17 . The activity test of -amylase was performed with Fuwa method 18 and Mandels 19 method.…”

Section: Methods 221 Isolation Purification and Activity Test Of mentioning

confidence: 99%

Increasing Stability of a-amylase Obtained from Bacillus subtilis ITBCCB148 by Immobilization with Chitosan

Yandri¹,

Suhartati²,

Satria³

et al. 2020

Mediterr.J.Chem.,

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“…FACCIOTTI et al [8] observed that the amylase activity of Aspergillus awamori decreased when the substrate content was increased up to 2%. Besides the carbon source, it has been suggested that the nitrogen source can also control amylase activity [9]. WAŚKO et al [10] reported a successful medium optimization using Plackett-Burman design.…”

Section: Introductionmentioning

confidence: 99%

A marked enhancement in production of amylase by Bacillus amyloliquefaciens in flask fermentation using statistical methods

Zhao

Zheng

Wang

et al. 2011

J. Cent. South Univ. Technol.

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A total of 126 bacterial strains were isolated from soil samples. Among them, 11 isolates were found positive for amylase production. Strain YL produced the largest zone of clearance on plate assay. The isolate YL was identified as Bacillus sp. based on morphological and physiochemical characterization. According to 16S rRNA gene sequencing data, the closest phylogenetic neighbor of strain YL was Bacillus amyloliquefaciens (99.54%). After that, an optimization of culture conditions was carried out for the improvement of α-amylase production. Response surface methodology (RSM) was applied to evaluate the effect of medium components including wheat bran, cottonseed extract, yeast extract, starch, NaCl and CaCl 2 . Three variables (wheat bran, cottonseed extract, and starch), which were identified to significantly affect amylase production by Plackett-Burman design were further optimized using response surface methodology of Box-Behnken design (BBD). The optimal concentrations estimated for each variable related to the maximum of amylase activity (86 kU/mL) were 10.80 g/L wheat bran, 9.90 g/L cottonseed extract, 0.5 g/L starch, 2.0 g/L yeast extract, 5.00 g/L NaCl and 2.00 g/L CaCl 2 . The fermentation using optimized culture medium allowed a significant increase in amylase production (by 3-fold). The improvement in the α-amylase production after optimization process can be considered adequate for large-scale applications.

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“…[1][2][3] There are four common types of assays that are used to determine the activity of a-amylase: (1) assays that measure the increase in reducing power by measuring the reducing sugars produced by the dinitrosalicylic acid (DNS) assay 2,4-9 or the Nelson-Somogyi 1,10,11 method; (2) assays that measure the stainability of residual starch by forming complexes with iodine, this method was developed by Fuwa; [9][10][11][12][13][14][15][16] (3) a colorimetric method in which starch is covalently labeled with various dyes and hydrolyzed by a-amylase to give soluble fragments that are measured colorimetrically aer the removal of the unhydrolyzed substrate; 17,18 and (4) assays based on the decrease in viscosity of starch solutions during enzymatic reaction. It acts on linear a(1,4) glycosidic linkages.…”

Section: Introductionmentioning

confidence: 99%

“…28,29 In addition, nano-optical sensors have been applied in the eld of high-sensitive analysis of protein and deoxyribonucleic acid (DNA). [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19] One lm is used for all measurements which prevents a source of error in the measurement process and gives low standard deviation values. It is used in light emitting diodes, 34 photodetectors, 35 sensors, 36 address decoders, 37 and electricallydriven lasers.…”

Section: Introductionmentioning

confidence: 99%

A new nano-optical sensor thin film cadmium sulfide doped in sol–gel matrix for assessment of α-amylase activity in human saliva

Attia

Zoulghena

Abdel‐Mottaleb

2014

Analyst

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A novel, simple, sensitive and precise spectrofluorimetric method is developed for measuring the activity of the α-amylase enzyme in human saliva. The remarkable quenching of the luminescence intensity at 634 nm of nano CdS doped in a sol-gel matrix by various concentrations of maltose (produced from the reaction of the enzyme with the starch substrate) was successfully used as an optical sensor for the assessment of α-amylase activity. The calibration plot was achieved over the concentration range 4.8 × 10(-10) to 1.2 × 10(-5) mol L(-1) maltose with a correlation coefficient of 0.999 and a detection limit of 5.7 × 10(-11) mol L(-1). The method was used satisfactorily for assessment of the α-amylase activity in a number of human saliva samples collected from various healthy volunteers.

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Production, purification and characterization of an α-amylase produced by Saccharomycopsis fibuligera

Cited by 7 publications

References 31 publications

Increasing Stability of a-amylase Obtained from Bacillus subtilis ITBCCB148 by Immobilization with Chitosan

Increasing Stability of a-amylase Obtained from Bacillus subtilis ITBCCB148 by Immobilization with Chitosan

A marked enhancement in production of amylase by Bacillus amyloliquefaciens in flask fermentation using statistical methods

A new nano-optical sensor thin film cadmium sulfide doped in sol–gel matrix for assessment of α-amylase activity in human saliva

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