Research Progress on Screening of High-yield Xylanase-producing Strains

doi:10.19586/j.2095-2341.2025.0070

Current Biotechnology ›› 2026, Vol. 16 ›› Issue (1): 10-17.DOI: 10.19586/j.2095-2341.2025.0070

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Research Progress on Screening of High-yield Xylanase-producing Strains

Jiazeng GAO¹^,²^,³^,⁴(), Yunshu XIAO¹^,²^,³^,⁴, Wenzheng YAN¹^,²^,³^,⁴, Yongli LI¹^,²^,³^,⁴, Zhanying LIU¹^,²^,³^,⁴, Jianhua HU¹^,²^,³^,⁴()

^1.Key Laboratory of Synthetic Biology，Inner Mongolia Autonomous Region，Hohhot 010051，China
^2.Inner Mongolia Autonomous Region Engineering Research Center for Bio-fermentation Green Manufacturing，Hohhot 010051，China
^3.Engineering Research Center of Inner Mongolia for Green Manufacturing in Bio-fermentation Industry，Hohhot 010051，China
^4.School of Chemical Engineering，Inner Mongolia University of Technology，Hohhot 010051，China

Received:2025-06-20 Accepted:2025-11-07 Online:2026-01-25 Published:2026-02-12
Contact: Jianhua HU

Abstract

Abstract:

Xylan， the main component of plant hemicellulose， is a complex pentosan polysaccharide characterized by abundant content， low cost and renewability. However， it suffers from problems such as poor degradability， low utilization rate， and easy causes of resource waste and environmental pollution. Xylanase is the primary enzyme for degrading xylan and boasts great development potential， being widely applied in the industrial， agricultural， pharmaceutical， food and other fields. Microorganisms are the major source of xylanase， and xylanases from different sources vary greatly， yet the common drawback of low enzyme activity exists universally. Therefore， screening high-yield xylanase-producing strains is of great significance for resource recycling. This paper briefly elaborated on the classification and structure of xylanase， the mutagenesis breeding methods of xylanase-producing strains， as well as the cloning and heterologous expression of xylanase genes， and revealed the hydrolysis mechanism of xylanase and its expression in bacterial and fungal expression systems， aiming to provide a reference for the research on xylanase production.

Key words: xylanase, mutagenesis breeding, xylanase activity, heterologous expression, expression system

摘要：

木聚糖作为植物半纤维素的主要成分，是一种复杂的多聚五碳糖，具有含量丰富、廉价和可再生等特点，但其存在难降解、被利用率低、易造成资源浪费和环境污染等问题。木聚糖酶是降解木聚糖的主要酶类，具有极大的发展潜力，广泛应用于工业、农业、医药、食品等领域。微生物是木聚糖酶的主要来源，不同来源的木聚糖酶也存在着较大差异，但是普遍存在酶活力低下的问题，因此筛选高产木聚糖酶菌株对资源的再利用具有重要意义。简述了木聚糖酶的分类与结构、木聚糖酶菌株的诱变选育方法及木聚糖酶基因的克隆和异源表达，揭示了木聚糖酶的水解机理及其在细菌和真菌表达系统中的表达，以期为木聚糖酶的生产研究提供参考。

关键词: 木聚糖酶, 诱变育种, 木聚糖酶活力, 异源表达, 表达系统

CLC Number:

Q539+.3

Jiazeng GAO, Yunshu XIAO, Wenzheng YAN, Yongli LI, Zhanying LIU, Jianhua HU. Research Progress on Screening of High-yield Xylanase-producing Strains[J]. Current Biotechnology, 2026, 16(1): 10-17.

高家增, 肖蕴澍, 闫文正, 李永丽, 刘占英, 胡建华. 高产木聚糖酶菌株选育的研究进展[J]. 生物技术进展, 2026, 16(1): 10-17.

Figures/Tables 5

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菌株	诱变方法	结果	参考文献
球毛壳霉菌Z30-56	紫外诱变	酶活9850 U·mL^-1，较最初菌株提高了53.7%	[12]
短小芽胞杆菌M-11-2	紫外诱变	酶活500~600 U·mL^-1，是最初菌株酶活的1.5倍	[13]
黑曲霉ARTP-82	常压常温等离子体诱变	最适反应温度45 ℃、pH 7.0，酶活175.33 U·mL^-1，较最初菌株提高了120.8%	[14]
菌疏棉状嗜热霉菌W5-133	微波诱变	较最初菌株提高了66.8%	[15]
枯草芽孢杆菌	稀土选育	酶活133.79 U·mL^-1，较最初菌株提高了10.48%	[16]
克里布所类芽胞杆菌2A82s-13	紫外诱变、常压常温等离子体诱变	酶活135.25±0.40 U·mL^-1，3轮紫外诱变提高了66.8%，2轮ARTP诱变进一步提高了31.2%	[17]
黑曲霉X1U4-1	紫外、硫酸二乙酯及紫外-硫酸二乙酯复合诱变	酶活938 3.18 U·g^-1，较最初菌株提高了3.8%	[18]
黑曲霉	紫外诱变、快中子辐照诱变、硫酸二乙酯诱变、亚硝酸钠诱变、亚硝基胍诱变	酶活分别是最初菌株的2.18、1.72、1.51、1.46、1.38倍	[19]

菌株	诱变方法	结果	参考文献
球毛壳霉菌Z30-56	紫外诱变	酶活9850 U·mL^-1，较最初菌株提高了53.7%	[12]
短小芽胞杆菌M-11-2	紫外诱变	酶活500~600 U·mL^-1，是最初菌株酶活的1.5倍	[13]
黑曲霉ARTP-82	常压常温等离子体诱变	最适反应温度45 ℃、pH 7.0，酶活175.33 U·mL^-1，较最初菌株提高了120.8%	[14]
菌疏棉状嗜热霉菌W5-133	微波诱变	较最初菌株提高了66.8%	[15]
枯草芽孢杆菌	稀土选育	酶活133.79 U·mL^-1，较最初菌株提高了10.48%	[16]
克里布所类芽胞杆菌2A82s-13	紫外诱变、常压常温等离子体诱变	酶活135.25±0.40 U·mL^-1，3轮紫外诱变提高了66.8%，2轮ARTP诱变进一步提高了31.2%	[17]
黑曲霉X1U4-1	紫外、硫酸二乙酯及紫外-硫酸二乙酯复合诱变	酶活938 3.18 U·g^-1，较最初菌株提高了3.8%	[18]
黑曲霉	紫外诱变、快中子辐照诱变、硫酸二乙酯诱变、亚硝酸钠诱变、亚硝基胍诱变	酶活分别是最初菌株的2.18、1.72、1.51、1.46、1.38倍	[19]

木聚糖酶基因来源	最适pH	最适温度/℃	表达菌株	表达载体	比酶活/(U·mg^-1)	参考文献
极端温度温泉宏基因组	7.0	80	E. coli BL21(DE3)	pET-23a(+)	-	[25]
帕特里克念珠菌	5.5	60	E. coli BL21(DE3)	pET-28a(+)	1 358.00	[26]
沙福芽孢杆菌	7.0	60	E. coli BL21(DE3)	pET15b16S	-	[27]
芽孢杆菌SC1	9.0	55	E. coli BL21(DE3)	pET-28a(+)	4 594.00	[28]
美国国家生物技术信息中心	5.0	35	E. coli BL21(DE3)	pET-28a(+)	9 742.50	[29]
纤维分解粘细菌溶糖曲霉 JOP 1030-1 T. reesei XynⅡ蛋白的氨基酸 1-189 高高芽孢杆菌JYY-02 链霉菌 L2001 糖解曲霉JOP1030-1 厌氧芽孢杆菌	6.0 5.5 5.5 6.5 6.0 6.0 7.0	50 55 55 50 50 50 65	E. coli BL21(DE3) E. coli BL21(DE3) E. coli BL21(DE3) E. coli Rosetta(DE3) E. coli BL21(DE3) E. coli BL21(DE3) E. coli BL21(DE3)	pET-29a(+) pET-28a(+) pET-NTMST pET-15b pET-28a(+) pET-28a(+) pET-28a(+)	3 643.52 1 567.20 6 678.00 1 105.00 2 010.55 198.10 284.60	[30] [31] [32] [33] [34] [35] [36]

木聚糖酶基因来源	最适pH	最适温度/℃	表达菌株	表达载体	比酶活/(U·mg^-1)	参考文献
极端温度温泉宏基因组	7.0	80	E. coli BL21(DE3)	pET-23a(+)	-	[25]
帕特里克念珠菌	5.5	60	E. coli BL21(DE3)	pET-28a(+)	1 358.00	[26]
沙福芽孢杆菌	7.0	60	E. coli BL21(DE3)	pET15b16S	-	[27]
芽孢杆菌SC1	9.0	55	E. coli BL21(DE3)	pET-28a(+)	4 594.00	[28]
美国国家生物技术信息中心	5.0	35	E. coli BL21(DE3)	pET-28a(+)	9 742.50	[29]
纤维分解粘细菌溶糖曲霉 JOP 1030-1 T. reesei XynⅡ蛋白的氨基酸 1-189 高高芽孢杆菌JYY-02 链霉菌 L2001 糖解曲霉JOP1030-1 厌氧芽孢杆菌	6.0 5.5 5.5 6.5 6.0 6.0 7.0	50 55 55 50 50 50 65	E. coli BL21(DE3) E. coli BL21(DE3) E. coli BL21(DE3) E. coli Rosetta(DE3) E. coli BL21(DE3) E. coli BL21(DE3) E. coli BL21(DE3)	pET-29a(+) pET-28a(+) pET-NTMST pET-15b pET-28a(+) pET-28a(+) pET-28a(+)	3 643.52 1 567.20 6 678.00 1 105.00 2 010.55 198.10 284.60	[30] [31] [32] [33] [34] [35] [36]

木聚糖酶基因来源	最适pH	最适温度/℃	表达菌株	表达载体	比酶活/(U·mg^-1)	参考文献
热稳定粘褶菌	4.5~5.0	75	P. pastoris GS115	pPIC9	1 205.00	[45]
毛壳菌属CQ31菌株	6.5	85	P. pastoris GS115	pPIC9K	2 489.00	[46]
硫磺曲霉JCM01963菌株	5.0	70	P. pastoris	pPICZαA	80.71	[47]
三浦盐乳杆菌	6.5	45	P. pastoris	pPICZαA	1 021.65	[48]
黑曲霉BCC14405 菌株	6.0	45	P. pastoris KM71	pPICZαA	3 852.00	[49]
毛壳菌属CQ31菌株嗜热毁丝霉厌氧瘤胃微生物烟曲霉Z5 嗜热菌丝体米黑根毛霉CAU432 尖孢镰刀菌Fo47	7.0 5.0 5.5 7.4 6.0 7.0 5.0	70 60 40 70 50 65 45	A. niger P. pastoris X33 P. pastoris P. pastoris X33 P. pastoris P. pastoris P. pastoris X33	pEASY-Blunt pPICZαA pPIC9K pPICZaa pPICZαA pPIC9K pPICZɑA-FXYL	2 540.00 179.07 56.02 - 1 533.71 7 915.50 -	[50] [51] [52] [53] [54] [55] [56]

Research Progress on Screening of High-yield Xylanase-producing Strains

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