Enzymic degradation of raffinose family oligosaccharides in soymilk by immobilized α-galactosidase from Gibberella fujikuroi

Thippeswamy, S.; Mulimani, V. H.

doi:10.1016/s0032-9592(02)00010-9

Cited by 50 publications

(58 citation statements)

References 16 publications

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“…resistance of substrate to diffuse into the immobilization matrix and resistance of the products to diffuse out). Seventy six percent hydrolysis of raffinose family sugars in soymilk by immobilized enzyme for 12 h is the highest reduction so far among the other reports on polyacrylamide immobilization of a-galactosidase (Thananunkul et al 1976;Thippeswamy & Mulimani 2002). Higher oligosaccharide hydrolysis by free enzyme may occur because of better access of substrate to the free enzyme.…”

Section: Batch Reactionmentioning

confidence: 93%

“…Higher oligosaccharide hydrolysis by free enzyme may occur because of better access of substrate to the free enzyme. Thananunkul et al (1976) have reported 50% hydrolysis whereas Thippeswamy & Mulimani (2002) have reported 71% hydrolysis after 12 h incubation of soymilk with immobilized enzyme.…”

Section: Batch Reactionmentioning

confidence: 99%

“…Thananunkul et al (1976) reported that fluidized bed containing a-galactosidase-gel complex hydrolyzed 60% of the raffinose and stachyose in soymilk but at a flow rate of 30 ml h )1 . Thippeswamy & Mulimani (2002) reported that oligosaccharide degradation of 84% at a flow rate of 25 ml h )1 . Prashanth & Mulimani (2005) reported that oligosaccharide degradation of 90% at a flow rate of 40 ml h )1 .…”

Section: Continuous Modementioning

confidence: 99%

“…There are some reports on the immobilization of a-galactosidase, e.g. in calcium alginate (Prashanth & Mulimani 2005), and in polyacrylamide gel (Thananunkul et al 1976;Thippeswamy & Mulimani 2002) and its use for reducing oligosaccharides in soymilk, but polyacrylamide supports are not useful in food processing because of toxicity.…”

Section: Introductionmentioning

confidence: 99%

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Hydrolysis of Galacto-oligosaccharides in Soymilk by κ-carrageenan-entrapped α-galactosidase from Aspergillus Oryzae

Girigowda

Mulimani

2006

World J Microbiol Biotechnol

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a-Galactosidase was immobilized in j-carrageenan. The optimum pH of the soluble enzyme and immobilized enzyme was 4.8. The optimum temperature of the soluble enzyme was 50°C and that of the immobilized enzyme was increased to 53°C. The immobilized enzyme was used in batch, repeated batch, and in the continuous mode to degrade the raffinose family sugars present in soymilk. Two hours incubation with free and immobilized a-galactosidase resulted in 88 and 75% reduction in raffinose family oligosaccharides in soymilk respectively. In the repeated batch, 61% reduction was obtained in the fourth cycle. A fluidized bed reactor was designed to treat soymilk continuously. The performance of immobilized a-galactosidase was also tested in a fluidized bed reactor at different flow rates and 92% reduction of raffinose family oligosaccharides in soymilk was obtained at 25 ml h )1 flow rate. The study revealed that immobilized a-galactosidase in continuous mode is efficient in reducing the oligosaccharides present in the soymilk.

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Section: Batch Reactionmentioning

confidence: 93%

Section: Batch Reactionmentioning

confidence: 99%

Section: Continuous Modementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Hydrolysis of Galacto-oligosaccharides in Soymilk by κ-carrageenan-entrapped α-galactosidase from Aspergillus Oryzae

Girigowda

Mulimani

2006

World J Microbiol Biotechnol

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“…There are several reports available in the literature of the use of -galactosidase from plant and fungal sources for the removal of raYnose family sugars from soybean Xour and soybean milk [9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Multiple α-galactosidases from Aspergillus foetidus ZU-G1: purification, characterization and application in soybean milk hydrolysis

Liu

2012

Eur Food Res Technol

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Galactosidase had applied in food and feed industries for hydrolyzing raYnose series oligosaccharides (RO) that are the factors primarily responsible for Xatulence upon ingestion of soybean-derived products. The objective of the current work was to purify the -galactosidase of Aspergillus foetidus ZU-G1 and compared the biochemical and hydrolytic properties of three major -galactosidase forms ( -gal I, -gal II and -gal III). The molecular mass of the puriWed enzyme as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was 106.3, 49.7 and 109.9 kDa, respectively. Its optimum reaction temperature was 60°C and stable below 50°C. The optimum pH of -gal I and -gal III was 5.0 and -gal II was 4.0. Under 28°C conditions for 24 h, -gal I was stable at pH 4.0, -gal II was stable at pH 6.0, and -gal III was pH 5.0. -Galactosidase was completely inhibited by Ag + . CuSO 4 ·5H 2 O and SDS were powerful inhibitors of -gal I and -gal III but had little eVect to -gal II. EDTA did not strongly aVect -gal I and -gal III, while strongly aVect -gal II. CaCl 2 ·2H 2 O, MgSO 4 ·7H 2 O and MnSO 4 ·7H 2 O were activation for -gal I, -gal II and -gal III. No signiWcant inhibition of enzymes activity was observed in the presence of raYnose, lactose as well as other sugars tested. Synthetic substrate p-nitrophenyl--D-galactopyranoside was not preferentially hydrolyzed than natural substrates, such as melibiose, stachyose and raYnose. Under 40 and 50°C incubation for 1-5 h, the stachyose of soybean milk was degraded by -gal I, -gal II and -gal III and strongly hydrolyzed by -gal II, and the raYnose of soybean milk was completely hydrolyzed by -gal II and weakly hydrolyzed by -gal I and -gal III. The distinct hydrolytic and biochemical properties of -gal I, -gal II and -gal III further signify the -galactosidase of A. foetidus ZU-G1 was propitious to soybean milk and related food industry.

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Other Applications of Fluidization

Smith¹

2007

Applications of Fluidization to Food Processing

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Enzymic degradation of raffinose family oligosaccharides in soymilk by immobilized α-galactosidase from Gibberella fujikuroi

Cited by 50 publications

References 16 publications

Hydrolysis of Galacto-oligosaccharides in Soymilk by κ-carrageenan-entrapped α-galactosidase from Aspergillus Oryzae

Hydrolysis of Galacto-oligosaccharides in Soymilk by κ-carrageenan-entrapped α-galactosidase from Aspergillus Oryzae

Multiple α-galactosidases from Aspergillus foetidus ZU-G1: purification, characterization and application in soybean milk hydrolysis

Other Applications of Fluidization

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