Thermostable Tannase from Aspergillus Niger and Its Application in the Enzymatic Extraction of Green Tea

Yuan, Shao; Zhang, Yonghui; Zhang, F.; Yang, Qing; Weng, Han‐Rong; Xiao, Qiong; Xiao, Anfeng

doi:10.3390/molecules25040952

Cited by 44 publications

(42 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…There were dynamic changes in Miang catechin, especially the biotransformation of EGCG to EGC and ECG to EC during the production process [ 16 ]. With regard to the substrate specificity results, all CATs could be used for biotransformation [ 31 ], antioxidant activity enhancement, and extraction of tea catechins [ 32 ], as well as the improvement of the sweet aftertaste of tea products [ 4 ]. Regarding the properties of CAT from Cy.…”

Section: Discussionmentioning

confidence: 99%

Acid Stable Yeast Cell-Associated Tannase with High Capability in Gallated Catechin Biotransformation

et al. 2021

View full text Add to dashboard Cite

Previously, nine tannin-tolerant and tannase-producing yeasts were isolated from Miang; all produced cell-associated tannase (CAT) during growth in tannin substrate. Among which, only CAT from Sporidiobolus ruineniae showed better stability than its purified form. Yet, it is of particular interest to directly characterize CATs from the latter yeasts. In this study, four CATs from yeasts, namely Cyberlindnera rhodanensis A22.3, Candida sp. A39.3, Debaryomyces hansenii A45.1, and Cy. rhodanensis A45.3 were characterized. The results indicate that all CATs were produced within the same production yield (11 mU/mL). Most CATs exhibited similar pH and temperature optima and stabilities, except for CAT from Cy. rhodanensis A22.3. This CAT was assigned as acid-stable tannase due to its unusual optimum pH of 2.0 with pH stability and half-life thermostability in the range of pH 2.0–4.0, and 70 °C, respectively. All CATs demonstrated high substrate specificity toward epigallocatechin gallate and epicatechin gallate, thus forming epigallocatechin and epicatechin, respectively. Moreover, they showed operational stability to repeated use for up to five cycles without loss of the initial activity. Therefore, CATs from these yeasts could be useful for the extraction and biotransformation of tea catechins and related applications.

show abstract

Section: Discussionmentioning

confidence: 99%

Acid Stable Yeast Cell-Associated Tannase with High Capability in Gallated Catechin Biotransformation

et al. 2021

View full text Add to dashboard Cite

show abstract

“…The β‐mannanases were more thermally stable in the crude extract than in the purified β‐mannanases produced by A. terreus , 18 which maintained 85% and 50% of the enzymatic activity after 1 h at 50 °C and 60 °C, respectively. The ability of P. citrinum mannanase to support high temperatures and acid pH conditions makes it interesting for biotechnological processes, mostly to reduce the risks of microbial contamination 43 …”

Section: Discussionmentioning

confidence: 99%

“…The ability of P. citrinum mannanase to support high temperatures and acid pH conditions makes it interesting for biotechnological processes, mostly to reduce the risks of microbial contamination. 43 Freeze-drying can be used to preserve the enzyme activity for a more extended period in SSF processes. 44 Stored under the form of lyophilized solids, the relative activity of the enzyme initially dropped (∼10%), thereafter exhibiting high storage stability (surpassing 100% of residual activity) for 30 days.…”

Section: Discussionmentioning

confidence: 99%

β‐Mannanase production by Penicillium citrinum through solid‐state fermentation using açaí residual biomass (Euterpe oleracea)

Lima

Silva

et al. 2021

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND Açaí core (Euterpe oleracea) is a residual biomass with high mannan content; thus it can become a good inducer for mannanase production by solid‐state fermentation (SSF). β‐Mannanase production from Penicillium citrinum was investigated using açaí seed as inducer and carbon source through SSF, as well as the properties of β‐mannanase in the crude extract. RESULTS In this study, a two‐stage screening was performed. The P. citrinum strain exhibited high specific enzymatic activity (29 ± 0.2 U mg−1 protein). Nitrogen addition was necessary to improve β‐mannanase activity (an increase of 389% with sodium nitrate). The effect of pH and temperature on β‐mannanase activity in the crude extract was evaluated, with the highest activity found at pH 4.6 and a temperature of 40–60 °C. The enzymes exhibited good thermal stability with 5 h of incubation at 40, 50 and 60 °C, retaining 90%, 55% and 60% of the initial activity, respectively. Furthermore, P. citrinum β‐mannanase exhibited high specificity against ivory nut mannan (234% relative activity), good activity in the presence of a range of metal ions and the ability to hydrolyze locust bean gum, producing mannose and mannooligosaccharides. CONCLUSION Based on such data, açaí seed can be used as an inducer of β‐mannanase. The P. citrinum crude enzymatic extract, rich in β‐mannanase, has potential industrial applications, especially in the food and feed industries.

show abstract

“…Ester-type catechins (EGCG and ECG) [ 12 ] in tea infusion could be hydrolyzed into non-ester-type catechins (EGC and EC), which improved the sweet aftertaste of tea infusion since EGC and EC are the main contributors for sweet aftertaste. Tannase treatment was also shown to increase polyphenol recovery rate [ 13 , 14 ] in tea extraction process due to the degradation due to its hydrolysis toward the diferulic acid dimer in the plant cell wall. The biological activities of tannase-treated tea extracts, such as antioxidant activity and inhibition effect on digestive enzymes, are also improved [ 15 ].…”

Section: Introductionmentioning

confidence: 99%

Chitosan Activated with Genipin: A Nontoxic Natural Carrier for Tannase Immobilization and Its Application in Enhancing Biological Activities of Tea Extract

et al. 2021

Self Cite

View full text Add to dashboard Cite

In this work, a non-toxic chitosan-based carrier was constructed via genipin activation and applied for the immobilization of tannase. The immobilization carriers and immobilized tannase were characterized using Fourier transform infrared spectroscopy and thermogravimetric analysis. Activation conditions (genipin concentration, activation temperature, activation pH and activation time) and immobilizations conditions (enzyme amount, immobilization time, immobilization temperature, immobilization pH, and shaking speed) were optimized. The activity and activity recovery rate of the immobilized tannase prepared using optimal activation and immobilization conditions reached 29.2 U/g and 53.6%, respectively. The immobilized tannase exhibited better environmental adaptability and stability. The immobilized tannase retained 20.1% of the initial activity after 12 cycles and retained 81.12% of residual activity after 30 days storage. The catechins composition analysis of tea extract indicated that the concentration of non-ester-type catechins, EGC and EC, were increased by 1758% and 807% after enzymatic treatment. Biological activity studies of tea extract revealed that tea extract treated with the immobilized tannase possessed higher antioxidant activity, higher inhibitory effect on α-amylase, and lower inhibitory effect on α-glucosidase. Our results demonstrate that chitosan activated with genipin could be an effective non-toxic carrier for tannase immobilization and enhancing biological activities of tea extract.

show abstract

Thermostable Tannase from Aspergillus Niger and Its Application in the Enzymatic Extraction of Green Tea

Cited by 44 publications

References 43 publications

Acid Stable Yeast Cell-Associated Tannase with High Capability in Gallated Catechin Biotransformation

Acid Stable Yeast Cell-Associated Tannase with High Capability in Gallated Catechin Biotransformation

β‐Mannanase production by Penicillium citrinum through solid‐state fermentation using açaí residual biomass (Euterpe oleracea)

Chitosan Activated with Genipin: A Nontoxic Natural Carrier for Tannase Immobilization and Its Application in Enhancing Biological Activities of Tea Extract

Contact Info

Product

Resources

About