Optimization Production of an Endo-β-1,4-Xylanase from Streptomyces thermocarboxydus Using Wheat Bran as Sole Carbon Source

IF 4.6 Q2 GREEN & SUSTAINABLE SCIENCE & TECHNOLOGY
Recycling Pub Date : 2024-06-09 DOI:10.3390/recycling9030050
Thi Ngoc Tran, C. Doan, Thi Kieu Loan Dinh, Thi Hai Ninh Duong, Thi Thuc Uyen Phan, Thi Thuy Loan Le, Trung Dung Tran, Pham Hung Quang Hoang, A. Nguyen, San-Lang Wang
{"title":"Optimization Production of an Endo-β-1,4-Xylanase from Streptomyces thermocarboxydus Using Wheat Bran as Sole Carbon Source","authors":"Thi Ngoc Tran, C. Doan, Thi Kieu Loan Dinh, Thi Hai Ninh Duong, Thi Thuc Uyen Phan, Thi Thuy Loan Le, Trung Dung Tran, Pham Hung Quang Hoang, A. Nguyen, San-Lang Wang","doi":"10.3390/recycling9030050","DOIUrl":null,"url":null,"abstract":"Xylanases, key enzymes for hydrolyzing xylan, have diverse industrial applications. The bioprocessing of agricultural byproducts to produce xylanase through fermentation approaches is gaining importance due to its significant potential to reduce enzyme production costs. In this work, the productivity of Streptomyces thermocarboxydus TKU045 xylanase was enhanced through liquid fermentation employing wheat bran as the sole carbon source. The maximum xylanase activity (25.314 ± 1.635 U/mL) was obtained using the following optima factors: 2% (w/v) wheat bran, 1.4% (w/v) KNO3, an initial pH of 9.8, an incubation temperature of 37.3 °C, and an incubation time of 2.2 days. Xylanase (Xyn_TKU045) of 43 kDa molecular weight was isolated from the culture supernatant and was biochemically characterized. Analysis through liquid chromatography with tandem mass spectrometry revealed a maximum amino acid identity of 19% with an endo-1,4-β-xylanase produced by Streptomyces lividans. Xyn_TKU045 exhibited optimal activity at pH 6, with remarkable stability within the pH range of 6.0 to 8.0. The enzyme demonstrated maximum efficiency at 60 °C and considerable stability at ≤70 °C. Mg2+, Mn2+, Ba2+, Ca2+, 2-mercaptoethanol, Tween 20, Tween 40, and Triton X-100 positively influenced Xyn_TKU045, while Zn2+, Fe2+, Fe3+, Cu2+, and sodium dodecyl sulfate exhibited adverse impact. The kinetic properties of Xyn_TKU045 were a Km of 0.628 mg/mL, a kcat of 75.075 s−1 and a kcat/Km of 119.617 mL mg−1s−1. Finally, Xyn_TKU045 could effectively catalyze birchwood xylan into xylotriose and xylobiose as the major products.","PeriodicalId":36729,"journal":{"name":"Recycling","volume":null,"pages":null},"PeriodicalIF":4.6000,"publicationDate":"2024-06-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Recycling","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3390/recycling9030050","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"GREEN & SUSTAINABLE SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Xylanases, key enzymes for hydrolyzing xylan, have diverse industrial applications. The bioprocessing of agricultural byproducts to produce xylanase through fermentation approaches is gaining importance due to its significant potential to reduce enzyme production costs. In this work, the productivity of Streptomyces thermocarboxydus TKU045 xylanase was enhanced through liquid fermentation employing wheat bran as the sole carbon source. The maximum xylanase activity (25.314 ± 1.635 U/mL) was obtained using the following optima factors: 2% (w/v) wheat bran, 1.4% (w/v) KNO3, an initial pH of 9.8, an incubation temperature of 37.3 °C, and an incubation time of 2.2 days. Xylanase (Xyn_TKU045) of 43 kDa molecular weight was isolated from the culture supernatant and was biochemically characterized. Analysis through liquid chromatography with tandem mass spectrometry revealed a maximum amino acid identity of 19% with an endo-1,4-β-xylanase produced by Streptomyces lividans. Xyn_TKU045 exhibited optimal activity at pH 6, with remarkable stability within the pH range of 6.0 to 8.0. The enzyme demonstrated maximum efficiency at 60 °C and considerable stability at ≤70 °C. Mg2+, Mn2+, Ba2+, Ca2+, 2-mercaptoethanol, Tween 20, Tween 40, and Triton X-100 positively influenced Xyn_TKU045, while Zn2+, Fe2+, Fe3+, Cu2+, and sodium dodecyl sulfate exhibited adverse impact. The kinetic properties of Xyn_TKU045 were a Km of 0.628 mg/mL, a kcat of 75.075 s−1 and a kcat/Km of 119.617 mL mg−1s−1. Finally, Xyn_TKU045 could effectively catalyze birchwood xylan into xylotriose and xylobiose as the major products.
以麦麸为唯一碳源优化热羧酸链霉菌内β-1,4-木聚糖酶的生产
木聚糖酶是水解木聚糖的关键酶,具有多种工业应用。由于具有降低酶生产成本的巨大潜力,通过发酵方法对农副产品进行生物加工以生产木聚糖酶正变得越来越重要。在这项工作中,以麦麸为唯一碳源,通过液体发酵提高了热羧酸链霉菌(Streptomyces thermocarboxydus TKU045)木聚糖酶的生产率。在使用以下最佳因子时,木聚糖酶活性最高(25.314 ± 1.635 U/mL):2%(w/v)麦麸、1.4%(w/v)KNO3、初始 pH 值为 9.8、培养温度为 37.3 °C、培养时间为 2.2 天。从培养上清液中分离出分子量为 43 kDa 的木聚糖酶(Xyn_TKU045),并对其进行了生化鉴定。液相色谱-串联质谱分析表明,Xyn_TKU045 与生化链霉菌(Streptomyces lividans)产生的内切-1,4-β-木聚糖酶(endo-1,4-β-xylanase)氨基酸的最大相同度为 19%。Xyn_TKU045 在 pH 值为 6 时表现出最佳活性,在 pH 值为 6.0 至 8.0 的范围内具有显著的稳定性。该酶在 60 ℃ 时效率最高,在 ≤70 ℃ 时相当稳定。Mg2+、Mn2+、Ba2+、Ca2+、2-巯基乙醇、吐温 20、吐温 40 和 Triton X-100 对 Xyn_TKU045 有正面影响,而 Zn2+、Fe2+、Fe3+、Cu2+ 和十二烷基硫酸钠则有负面影响。Xyn_TKU045 的动力学特性为 Km 为 0.628 mg/mL,kcat 为 75.075 s-1,kcat/Km 为 119.617 mL mg-1s-1。最后,Xyn_TKU045 能有效地将桦木木聚糖催化成主要产物木三糖和木二糖。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Recycling
Recycling Environmental Science-Management, Monitoring, Policy and Law
CiteScore
6.80
自引率
7.00%
发文量
84
审稿时长
11 weeks
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信