ORCID Profile
0000-0003-0212-3277
Current Organisation
Chiang Mai University
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Publisher: Elsevier BV
Date: 05-2019
DOI: 10.1016/J.PEP.2019.01.005
Abstract: Lactobacillus pentosus BA-7 and L. pentosus QA1-5 are tannin-tolerant lactic acid bacteria that were isolated from Miang, a traditional fermented tea-leaf found in northern Thailand and a tannin-rich substrate. Tannase encoding genes were isolated, cloned and overexpressed in Escherichia coli BL21(DE3). The recombinant tannase was produced with production yields of 40 and 39 KU/L for LpTanBA-7 and LpTanQA1-5, respectively. Both revealed the same molecular weight of 50 kDa as estimated by SDS-PAGE and were optimally active under alkaline pH conditions LpTanQA1-5 revealed optimal temperatures in a range of 37-40 °C as is typically found in lactic acid bacteria, while LpTanBA-7 was active at higher temperatures with an optimum temperature range of 45-55 °C. LpTanBA-7 was found to be more stable within the same range of temperatures than LpTanQA1-5. Furthermore, it was active and stable toward various organic solvents and produced 50 mg/mL of gallic acid from 100 mg/mL tannic acid. Based on the results, LpTanBA-7 is considered a new alkali-moderately thermophilic tannase obtained from lactic acid bacterium that may be capable of a feasible production capacity of gallic acid and its esters. Furthermore, tannase that is active at high temperatures could also be used in tea products in order to develop a sweet aftertaste, as well as to improve levels of antioxidant activity.
Publisher: Elsevier BV
Date: 10-2017
DOI: 10.1016/J.IJBIOMAC.2017.05.168
Abstract: Lactobacillus plantarum S21 α-amylase possesses 475 amino acids at the C-terminal region identified as the starch-binding domain (SBD) and has been previously reported to play a role in raw starch degradation. To understand the specific roles of this SBD, cloning and expression of the complete (AmyL9) and C-terminally truncated (AmyL9Δ
Publisher: Elsevier BV
Date: 10-2015
Publisher: Elsevier BV
Date: 02-2018
DOI: 10.1016/J.IJBIOMAC.2017.09.060
Abstract: Gene encoding cyclomaltodextrinase (Cdx) from amylolytic lactic acid bacterium Enterococcus faecium K-1 was cloned and nucleotide sequence was analyzed. The open-reading frame consisted of 1767bp encoding 588 deduced amino acids. Consequently, four typically conserved regions of the glycoside hydrolase family 13 were revealed however, nine exceeding amino acids (DSYQMTDVP) were found at the 282-290 position in comparison to previously reported cyclomaltodextrinases. This difference is believed to have an influence on the substrate specificity of this enzyme. The recombinant CDases expressed in Escherichia coli BL21 (CDX_E) and Lactobacillus plantarum WCFS1 (CDX_L) with high expression levels of 8041 and 5511U/L were purified by Ni-NTA affinity chromatography. The active form CDX is a dimeric protein with two identical subunits of 62kDa, approximately. Both CDX_E and CDX_L revealed nearly similar properties, but the thermostability of CDX_L was slightly higher. Mn
Publisher: Springer Science and Business Media LLC
Date: 15-09-2015
Publisher: Springer Science and Business Media LLC
Date: 25-04-2020
DOI: 10.1186/S12934-020-01353-W
Abstract: Gallic acid has received a significant amount of interest for its biological properties. Thus, there have been recent attempts to apply this substance in various industries and in particular the feed industry. As opposed to yeasts, fungi and bacteria and their tannases have been well documented for their potential bioconversion and specifically for the biotransformation of tannic acid to gallic acid. In this research, Sporidiobolus ruineniae A45.2 is introduced as a newly pigment-producing and tannase-producing yeast that has gained great interest for its use as an additive in animal feed. However, there is a lack of information on the efficacy of gallic acid production from tannic acid and the relevant tannase properties. The objective of this research study is to optimize the medium composition and conditions for the co-production of gallic acid from tannic acid and tannase with a focus on developing an integrated production strategy for its application as a feed additive. Tannase produced by S. ruineniae A45.2 has been classified as a cell-associated tannase (CAT). Co-production of gallic acid obtained from tannic acid and CAT by S. ruineniae A45.2 was optimized using response surface methodology and then validated with the synthesis of 11.2 g/L gallic acid from 12.3 g/L tannic acid and the production of 31.1 mU/mL CAT after 48 h of cultivation in a 1-L stirred tank fermenter. Tannase was isolated from the cell wall, purified and characterized in comparison with its native form (CAT). The purified enzyme (PT) revealed the same range of pH and temperature optima (pH 7) as CAT but was distinctively less stable. Specifically, CAT was stable at up to 70 °C for 60 min, and active under its optimal conditions (40 °C) at up to 8 runs. Co-production of gallic acid and CAT is considered an integrated and green production strategy. S. ruineniae biomass could be promoted as an alternative source of carotenoids and tannase. Thus, the biomass, in combination with gallic acid that was formed in the fermentation medium, could be directly used as a feed additive. On the other hand, gallic acid could be isolated and purified for food and pharmaceutical applications. This paper is the first of its kind to report that the CAT obtained from yeast can be resistant to high temperatures of up to 70 °C.
No related grants have been discovered for Apinun Kanpiengjai.