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| Content Provider | Springer Nature Link |
|---|---|
| Author | Lang, Chong Yang, Rujian Yang, Ying Gao, Bei Zhao, Li Wei, Wei Wang, Hualei Matsukawa, Shingo Xie, Jingli Wei, Dongzhi |
| Copyright Year | 2016 |
| Abstract | An arabinanase gene was cloned by overlap-PCR from Penicillium sp. Y702 and expressed in Pichia pastoris. The recombinant enzyme was named AbnC702 with 20 U/mg of endo-arabinanase activity toward linear α-1,5-l-arabinan. The optimal pH and temperature of AbnC702 were 5.0 and 50 °C, respectively. The recombinant AbnC702 was highly stable at pH 5.0–7.0 and 50 °C. It could retain about 72.3 % of maximum specific activity at pH 5.0 after incubation for 2.5 h, which indicated AbnC702 was an acid-adapted enzyme. The K $_{m}$ and V $_{max}$ values were 24.8 ± 4.7 mg/ml and 88.5 ± 5.6 U/mg, respectively. A three-dimensional structure of AbnC702 was made by homology modeling, and the counting of acidic/basic amino residues within the region of 10 Å around the active site, as well the hydrogen bonds within the area of 5 Å around the active site, might theoretically interpret the acid adaptability of AbnC702. Analysis of hydrolysis products by thin layer chromatography (TLC) combined with high-performance liquid chromatography (HPLC) verified that the recombinant AbnC702 was an endo-1,5-α-l-arabinanase, which yielded arabinobiose and arabinotriose as major products. AbnC702 was applied in pectin extraction from apple pomace with synergistic action of α-L-arabinofuranosidase. |
| Starting Page | 900 |
| Ending Page | 916 |
| Page Count | 17 |
| File Format | |
| ISSN | 02732289 |
| Journal | Applied Biochemistry and Biotechnology |
| Volume Number | 180 |
| Issue Number | 5 |
| e-ISSN | 15590291 |
| Language | English |
| Publisher | Springer US |
| Publisher Date | 2016-06-01 |
| Publisher Place | New York |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Endo-1,5-α-l-arabinanase GH 43 Acid-adapted Pectin extraction Apple pomace Biotechnology Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology |
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