Purification and characterization of a thermostable α-galactosidase from<i>Thielavia terrestris</i>NRRL 8126 in solid state fermentation

Saad, R. R.; Fawzi, Eman M.

doi:10.1556/abiol.63.2012.1.11

Cited by 11 publications

(2 citation statements)

References 26 publications

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“…TN17 [11], fungi such as Aspergillus terreus [12], and the mushroom Ganoderma lucidum [13]. Some thermophilic enzymes have been discovered, such as a thermophilic α-galactosidase from Neosarotrya fischeri P1 [14], and thermostable α-galactosidases from Lenzites elegans [15], Thielavia terrestris NRRL8126 [16], and Talaromyces emersonii [17]. The thermostability makes them suitable candidates for use in feed industries.…”

Section: Introductionmentioning

confidence: 99%

A Fungal α-Galactosidase from Tricholoma matsutake with Broad Substrate Specificity and Good Hydrolytic Activity on Raffinose Family Oligosaccharides

et al. 2015

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An acidic α-galactosidase designated as TMG was purified from the fruiting bodies The purification protocol entailed ion exchange chromatography on Q-Sepharose and of Tricholoma matsutake with 136-fold purification and a specific activity of 909 units/mg. Mono-Q and fast protein liquid chromatography on Superdex 75. TMG is a monomeric protein exhibiting a molecular mass of 47 kDa in SDS-PAGE and gel filtration. The purified enzyme was identified by LC-MS/MS and three inner amino acid sequences were obtained. The optimum pH and temperature for TMG with pNPGal as substrate were pH 4.5 and 55 °C, respectively. The α-galactosidase activity was strongly inhibited by K

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Section: Introductionmentioning

confidence: 99%

A Fungal α-Galactosidase from Tricholoma matsutake with Broad Substrate Specificity and Good Hydrolytic Activity on Raffinose Family Oligosaccharides

et al. 2015

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“…Microbial α-galactosidases are particularly widely applied in the food industries owing to their biochemical properties and catalytic efficiencies (Chauhan, Kumar, Siddiqi, & Sharma, 2015;Huang et al, 2018;Katrolia et al, 2012;Lee et al, 2018;Wang et al, 2014). α-Galactosidases from various microorganisms have been shown to degrade RFOs from soy milk (Ferreira et al, 2011;Huang et al, 2018;Jang et al, 2019;Katrolia et al, 2012;Saad & Fawzi, 2012). Although α-galactosidases have been characterized from various microbial sources, enzymes isolated from GRAS or food-grade microorganisms are considered as safe for applications in the food industries.…”

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confidence: 99%

Enhanced elimination of non‐digestible oligosaccharides from soy milk by immobilized α‐galactosidase: A comparative analysis

Katrolia

Liu

et al. 2019

J Food Biochem

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This study compared two immobilization matrices like calcium‐alginate and chitosan for immobilization of α‐galactosidase and evaluated their potential for the removal of non‐digestible raffinose family oligosaccharides from soy milk which cause abdominal discomfort. The pH optima of the free and immobilized enzymes were found to be similar at pH 4.0. The chitosan‐immobilized α‐galactosidase displayed higher optimal temperature (60°C) compared to alginate‐immobilized enzyme (45°C) and free enzyme (50°C). The chitosan‐immobilized and alginate‐immobilized α‐galactosidases displayed 93.7% and 97.6% hydrolysis of raffinose family oligosaccharides, respectively, while the free enzyme hydrolyzed only 30.3% oligosaccharides present in soy milk in 4 hr. Remarkably, both the immobilized enzymes showed complete removal of raffinose family oligosaccharides in 8 hr. Moreover, reusability studies indicate that even after five cycles of reuse, the chitosan and alginate‐immobilized enzymes displayed 99% and 60% hydrolysis, respectively. Practical applications In this study, we have used two inexpensive and non‐toxic matrices for immobilizing α‐galactosidase. We report that entrapment of α‐galactosidase with chitosan significantly improved the optimal temperature of α‐galactosidase, which is advantageous in food industry. The hydrolysis of raffinose family oligosaccharides in soy milk was also greatly enhanced after immobilization with chitosan and alginate. Thus, the results described in this study have relevance for development of safe, cost‐effective and efficient method for removal of non‐digestible soy oligosaccharides in food industry.

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Purification an α-galactosidase from Coriolus versicolor with acid-resistant and good degradation ability on raffinose family oligosaccharides

Liu

Wang

et al. 2013

World J Microbiol Biotechnol

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An acid-tolerant α-galactosidase (CVGI) was isolated from the fruiting bodies of Coriolus versicolor with a 229-fold of purification and a specific activity of 398.6 units mg⁻¹. It was purified to electrophoretic homogeneity by ion exchange chromatography and gel filtration chromatography. The purified enzyme gave a single band corresponding to a molecular mass of 40 kDa in SDS-PAGE and gel filtration. The α-galactosidase was identified by MALDI-TOF-MS and its inner peptides were sequenced by ESI-MS/MS. The optimum temperature and pH of the enzyme were determined as 60 °C and 3.0, respectively. The enzyme was very stable at a temperature range of 4-50 °C and at a pH range of 2-5. Among the metal ions tested, Cu²⁺, Cd²⁺ and Hg²⁺ ions have been shown to partially inhibit the activity of α-galactosidase, while the activity of CVGI was completely inactivated by Ag⁺ ions. N-bromosuccinamide inhibited enzyme activity by 100 %, indicating the importance of tryptophan residue(s) at or near the active site. CVGI had wide substrate specificity (p-nitrophenyl galactoside, melidiose, raffinose and stachyose). After treatment with CVGI, raffinose family oligosaccharide was hydrolyzed effectively to yield galactose and sucrose. The results showed that the general properties of the enzyme offer potential for use of this α-galactosidase in several production processes.

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Purification and characterization of a thermostable α-galactosidase fromThielavia terrestrisNRRL 8126 in solid state fermentation

Cited by 11 publications

References 26 publications

A Fungal α-Galactosidase from Tricholoma matsutake with Broad Substrate Specificity and Good Hydrolytic Activity on Raffinose Family Oligosaccharides

A Fungal α-Galactosidase from Tricholoma matsutake with Broad Substrate Specificity and Good Hydrolytic Activity on Raffinose Family Oligosaccharides

Enhanced elimination of non‐digestible oligosaccharides from soy milk by immobilized α‐galactosidase: A comparative analysis

Purification an α-galactosidase from Coriolus versicolor with acid-resistant and good degradation ability on raffinose family oligosaccharides

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