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Article(id=1320881146452357618, tenantId=1146029695717560320, journalId=1260987677001138203, issueId=1320880625310085394, articleNumber=null, orderNo=null, doi=10.13386/j.issn1002-0306.2025090236, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=null, receivedDate=1758470400000, receivedDateStr=2025-09-22, revisedDate=null, revisedDateStr=null, acceptedDate=null, acceptedDateStr=null, onlineDate=1792852206099, onlineDateStr=2026-10-24, pubDate=1788192000000, pubDateStr=2026-09-01, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1792852206099, onlineIssueDateStr=2026-10-24, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1792852206099, creator=13701087609, updateTime=1792852206099, updator=13701087609, issue=Issue{id=1320880625310085394, tenantId=1146029695717560320, journalId=1260987677001138203, year='2026', volume='47', issue='17', pageStart='1', pageEnd='596', issueExtLink='null', onlineDate='null', pubDate='1788192000000', pubDateStr='2026-09-01', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=-1, specialIssue=null, createTime=1792852081848, creator='13701087609', updateTime=1792852081848, updator='13701087609', preIssue=null, nextIssue=null, articleTotal=null, ext=null, issueFiles=null, downloadFileDto=null}, startPage=223, endPage=232, ext={EN=ArticleExt(id=1320881146792096243, articleId=1320881146452357618, tenantId=1146029695717560320, journalId=1260987677001138203, language=EN, title=Screening and Identification of High Chitinase Producing Strains, Optimization of Fermentation Conditions and Analysis of Enzymatic Properties, columnId=1261336275769016441, journalTitle=Science and Technology of Food Industry, columnName=Bioengineering, runingTitle=null, highlight=null, articleAbstract=

To enhance the value-added utilization of chitin derived from crustacean waste, this study collected samples from the bottom of a shrimp farm in Guangxi. High-yield chitinase-producing strains were isolated through preliminary and secondary screening, followed by taxonomic identification. The optimal fermentation conditions were determined using single-factor experiments combined with orthogonal designs. Subsequently, the enzymatic properties and hydrolysis products of the chitinase produced by the selected strain were characterized. Results showed that initial screening on chitin-containing agar plates yielded nine strains capable of forming clear zones, among which strain GXUN-J3 exhibited the highest chitinase activity (297.24±10.77 U/L) and was identified as belonging to the genus Streptomyces sp. Under optimized fermentation conditions—6% (w/v) chitin, 0.25% (w/v) bean powder, an initial pH of 7.0, a fermentation temperature of 25 ℃, a liquid volume of 40 mL per 150 mL flask, and an inoculum size of 5% (v/v)—the chitinase activity reached 1026.72±18.69 U/L, representing a remarkable increase of 3.51-fold compared to the original process. Enzyme characterization revealed optimal activity at 50 ℃ and pH5.0. Among the metal ions tested, Mg2+ and Fe3+ significantly enhanced enzyme activity, whereas Fe2+, Mn2+, and Cu2+ exhibited significant inhibitory effects (P<0.05). Additionally, the chemical agents of EDTA, SDS, and methanol markedly suppressed enzymatic activity (P<0.05). Thin-layer chromatography (TLC) analysis demonstrated that the hydrolysis products primarily consisted of chitin dimer and N-acetyl-D-glucosamine, suggesting that this enzyme functions as an exo-chitinase. This study successfully established a process for producing chitinase and preparing chitin oligosaccharide using Streptomyces strain GXUN-J3, offering a promising approach for high-value utilization of crustacean waste.

, authors=Ligang ZHANG, Sijing PAN, Yuling WEI, Jiling LI, Dongwei PAN, Hongyan ZHANG, Naikun SHEN*, authorsList=Ligang ZHANG, Sijing PAN, Yuling WEI, Jiling LI, Dongwei PAN, Hongyan ZHANG, Naikun SHEN, authorCompany=null, correspAuthors=Naikun SHEN, authorNote=null, correspAuthorsNote=null, copyrightStatement=Copyright © 2026 Science and Technology of Food Industry. All rights reserved., copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=null, pdfFileSize=null, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=null, mapNumber=null, fund=null), CN=ArticleExt(id=1320881150541804032, articleId=1320881146452357618, tenantId=1146029695717560320, journalId=1260987677001138203, language=CN, title=高产几丁质酶菌株的筛选鉴定、发酵条件优化及酶学性质分析, columnId=1261336277547401341, journalTitle=食品工业科技, columnName=生物工程, runingTitle=null, highlight=null, articleAbstract=

为提升甲壳类废弃物中几丁质的资源化利用价值，本研究从广西海虾养殖场底部淤泥中采集样品，经初筛、复筛获得高产几丁质酶菌株并进行鉴定，再进一步通过单因素及正交优化设计确定最佳发酵参数，最后对菌株所产几丁质酶的酶学性质及酶解产物进行研究。结果表明：从几丁质固体平板上初筛获得9株透明圈较大菌株，进一步复筛获得1株高产几丁质酶（297.24±10.77 U/L）的菌株GXUN-J3，鉴定为链霉菌属（Streptomyces sp.）；条件优化获得该菌产几丁质酶的最佳工艺为：几丁质6%（w/v），大豆粉浓度0.25%（w/v），初始pH7.0，发酵温度25 ℃，装液量40 mL/150 mL，接种量5%（v/v），酶活可达1026.72±18.69 U/L，是优化前的3.51倍；酶学性质结果表明，该菌株所产几丁质酶的最适反应温度为50 ℃，最适反应pH为5.0，金属离子中Mg2+和Fe3+对酶活有激活作用，而Fe2+、Mn2+、Cu2+则有显著抑制作用（P<0.05）；化学试剂EDTA、SDS、甲醇有显著抑制作用（P<0.05）。酶解几丁质产物经薄层层析（thin layer chromatography，TLC）鉴定为几丁二糖和N-乙酰-D-氨基葡萄糖，表明该酶具有外切几丁质酶特性。本研究建立了基于链霉菌GXUN-J3的几丁质酶与几丁寡糖制备工艺，为甲壳类废弃物的高值化利用提供了研究基础。

, authors=张莉刚, 潘思静, 韦玉玲, 李吉玲, 潘东炜, 张红岩, 申乃坤*, authorsList=张莉刚, 潘思静, 韦玉玲, 李吉玲, 潘东炜, 张红岩, 申乃坤, authorCompany=null, correspAuthors=申乃坤, authorNote=

张莉刚（2001−），男，硕士研究生，研究方向：微生物资源开发与利用，E-mail：

, correspAuthorsNote=
申乃坤（1980−），男，博士，教授，研究方向：微生物资源挖掘及代谢工程改造研究，E-mail：。
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张莉刚（2001−），男，硕士研究生，研究方向：微生物资源开发与利用，E-mail：

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张莉刚（2001−），男，硕士研究生，研究方向：微生物资源开发与利用，E-mail：

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Science and Technology of Food Industry, 2023, 44（12）: 116−123., articleTitle=null, refAbstract=null), Reference(id=1320881545997562353, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, doi=null, pmid=null, pmcid=null, year=null, volume=null, issue=null, pageStart=null, pageEnd=null, url=null, language=null, rfNumber=39, rfOrder=57, authorNames=null, journalName=null, refType=null, unstructuredReference=HE X X, YU M, WU Y H, et al. Two highly similar chitinases from marine Vibrio species have different enzymatic properties[J]. 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注：A：菌落形态图（ISP2培养基）；B：革兰氏染色图（400×）；C：扫描电镜图（2000×）。

, figureFileSmall=uxs7dXs4SO7oCcO3T2n3Mw==, figureFileBig=d0B0iLjsXjO5zYMT5y3eTA==, tableContent=null), ArticleFig(id=1320881535985758630, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=EN, label=Fig.3, caption=Phylogenetic tree constructed based on the 16S rRNA sequence of strain GXUN-J3, figureFileSmall=PonYXHOzy4rq/TgYi9wtng==, figureFileBig=yddOiA9NZuuEmNvjH95KfQ==, tableContent=null), ArticleFig(id=1320881536040284583, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=CN, label=图3, caption=基于菌株GXUN-J3的16S rRNA序列构建的系统发育树, figureFileSmall=PonYXHOzy4rq/TgYi9wtng==, figureFileBig=yddOiA9NZuuEmNvjH95KfQ==, tableContent=null), ArticleFig(id=1320881536103199144, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=EN, label=Fig.4, caption=Optimization of culture medium composition and fermentation parameters for chitinase biosynthesis in Streptomyces strains, figureFileSmall=5A9EpYRgmlZrX7LMrUPWbg==, figureFileBig=k5Q6MpzIEZTaNYyVKkWM4g==, tableContent=null), ArticleFig(id=1320881536166113705, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=CN, label=图4, caption=培养基组分与培养条件对链霉菌菌株几丁质酶合成的优化分析

注：A：碳源；B：几丁质浓度；C：氮源；D：大豆粉浓度；E：培养温度；F：培养基初始pH；G：装液量；H：接种量；不同字母代表组间存在差异显著（P<0.05），图5同。

, figureFileSmall=5A9EpYRgmlZrX7LMrUPWbg==, figureFileBig=k5Q6MpzIEZTaNYyVKkWM4g==, tableContent=null), ArticleFig(id=1320881536241611178, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=EN, label=Fig.5, caption=Effects of different conditions on enzyme activity and stability, figureFileSmall=JyhHlc+ZIsyGGWolJ1oKYQ==, figureFileBig=N409HXECpr8mgFc9IQYuvg==, tableContent=null), ArticleFig(id=1320881536321302955, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=CN, label=图5, caption=不同条件对酶活性及稳定性的影响

注：A：温度；B：温度稳定性；C：pH；D：pH稳定性；E：金属离子；F：生化试剂；G：底物种类；H：底物浓度。

, figureFileSmall=JyhHlc+ZIsyGGWolJ1oKYQ==, figureFileBig=N409HXECpr8mgFc9IQYuvg==, tableContent=null), ArticleFig(id=1320881536405189036, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=EN, label=Fig.6, caption=Characterization of chitinase-catalyzed hydrolysates by thin-layer chromatographic analysis, figureFileSmall=n9+eLUZqIGzrk4+Zg2PRdg==, figureFileBig=NkL5Ab0XkingkRCve2/WTg==, tableContent=null), ArticleFig(id=1320881536497463725, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=CN, label=图6, caption=基于薄层色谱分析的几丁质酶酶解产物表征

注：NACOS：几丁寡糖混合标准品；DP1：N-乙酰-D-氨基葡萄糖；DP2：几丁二糖；DP3：几丁三糖；DP4：几丁四糖；DP5：几丁五糖。

, figureFileSmall=n9+eLUZqIGzrk4+Zg2PRdg==, figureFileBig=NkL5Ab0XkingkRCve2/WTg==, tableContent=null), ArticleFig(id=1320881536577155502, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=EN, label=Table 1, caption=

Factor and level designed of orthogonal test

, figureFileSmall=null, figureFileBig=null, tableContent=
因素水平
123
A：粉末几丁质浓度（%，w/v）6.07.08.0
B：大豆粉浓度（%，w/v）0.200.250.30
C：温度（℃）252831
D：接种量（%，v/v）345
), ArticleFig(id=1320881536644264367, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=CN, label=表1, caption=

正交试验因素水平设计

, figureFileSmall=null, figureFileBig=null, tableContent=
因素水平
123
A：粉末几丁质浓度（%，w/v）6.07.08.0
B：大豆粉浓度（%，w/v）0.200.250.30
C：温度（℃）252831
D：接种量（%，v/v）345
), ArticleFig(id=1320881536723956144, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=EN, label=Table 2, caption=

Determination of chitinase activity in rescreened strains

, figureFileSmall=null, figureFileBig=null, tableContent=
菌株圈径比（D/d）酶活（U/L）
GXUN-J31.84±0.17a297.24±10.77a
GXUN-3-91.55±0.09bc222.02±10.01b
GXUN-J21.31±0.12d121.43±8.76c
GXUN-3-81.51±0.11bc118.71±4.94c
GXUN-3-61.47±0.14c99.68±4.43d
GXUN-1-81.62±0.19b93.34±0.82d
GXUN-J11.81±0.16a57.09±5.01e
GXUN-2-61.09±0.14e34.43±2.60f
), ArticleFig(id=1320881536799453617, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=CN, label=表2, caption=

复筛菌株的几丁质酶活性测定

, figureFileSmall=null, figureFileBig=null, tableContent=
菌株圈径比（D/d）酶活（U/L）
GXUN-J31.84±0.17a297.24±10.77a
GXUN-3-91.55±0.09bc222.02±10.01b
GXUN-J21.31±0.12d121.43±8.76c
GXUN-3-81.51±0.11bc118.71±4.94c
GXUN-3-61.47±0.14c99.68±4.43d
GXUN-1-81.62±0.19b93.34±0.82d
GXUN-J11.81±0.16a57.09±5.01e
GXUN-2-61.09±0.14e34.43±2.60f
), ArticleFig(id=1320881536866562482, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=EN, label=Table 3, caption=

Biochemical and physiological profiling of bacterial strains

, figureFileSmall=null, figureFileBig=null, tableContent=
项目名称结果碳源结果
革兰氏染色+麦芽糖++++
过氧化氢酶+葡萄糖++++
淀粉水解酶−果糖+++
纤维素水解酶+蔗糖−
酪蛋白水解酶+棉子糖++
明胶液化试验+木糖−
VP、MR−甘油+++
硫化氢试验+甘露糖+++
硝酸盐产气−海藻糖−
温度耐受性20~40 ℃甘醇−
NaCl耐受性0~4%肌醇−
pH耐受性5.0~8.0半乳糖−
), ArticleFig(id=1320881536937865651, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=CN, label=表3, caption=

菌株生理生化特征分析

, figureFileSmall=null, figureFileBig=null, tableContent=
项目名称结果碳源结果
革兰氏染色+麦芽糖++++
过氧化氢酶+葡萄糖++++
淀粉水解酶−果糖+++
纤维素水解酶+蔗糖−
酪蛋白水解酶+棉子糖++
明胶液化试验+木糖−
VP、MR−甘油+++
硫化氢试验+甘露糖+++
硝酸盐产气−海藻糖−
温度耐受性20~40 ℃甘醇−
NaCl耐受性0~4%肌醇−
pH耐受性5.0~8.0半乳糖−
), ArticleFig(id=1320881537017557428, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=EN, label=Table 4, caption=

Results of orthogonal test

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试验号ABCD酶活力（U/L）
11111767.00±20.01
21232680.58±34.27
31323828.81±45.98
42133485.53±33.97
52221686.58±45.20
62312658.97±10.08
73122617.56±23.41
83213795.21±16.16
93331645.17±16.22
K12276.391870.082221.172098.74
K21831.072162.362132.951957.11
K32057.932132.951811.272109.55
R148.4497.43136.6450.81
主次顺序A>C>B>D
最佳组合A1B2C1D3
), ArticleFig(id=1320881537093054901, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=CN, label=表4, caption=

正交试验结果

, figureFileSmall=null, figureFileBig=null, tableContent=
试验号ABCD酶活力（U/L）
11111767.00±20.01
21232680.58±34.27
31323828.81±45.98
42133485.53±33.97
52221686.58±45.20
62312658.97±10.08
73122617.56±23.41
83213795.21±16.16
93331645.17±16.22
K12276.391870.082221.172098.74
K21831.072162.362132.951957.11
K32057.932132.951811.272109.55
R148.4497.43136.6450.81
主次顺序A>C>B>D
最佳组合A1B2C1D3
), ArticleFig(id=1320881537168552374, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=EN, label=Table 5, caption=

Variance analysis result of orthogonal test

, figureFileSmall=null, figureFileBig=null, tableContent=
方差来源平方和自由度均方F值P值
修正模型258528.305a832316.0381436.081284<0.001
截距12670698.45112670698.4514147.002<0.001
几丁质浓度99164.58107249582.2905355.359282<0.001
大豆粉浓度51796.47601225898.23828.915725<0.001
温度93095.44132246547.7206651.971145<0.001
接种量14471.8067527235.9033758.07898170.003
误差16121.6184618895.6454702
总计12945348.3727
修正后总计274649.923626
), ArticleFig(id=1320881537227272631, tenantId=1146029695717560320, journalId=1260987677001138203, articleId=1320881146452357618, language=CN, label=表5, caption=

正交试验方差分析结果

, figureFileSmall=null, figureFileBig=null, tableContent=
方差来源平方和自由度均方F值P值
修正模型258528.305a832316.0381436.081284<0.001
截距12670698.45112670698.4514147.002<0.001
几丁质浓度99164.58107249582.2905355.359282<0.001
大豆粉浓度51796.47601225898.23828.915725<0.001
温度93095.44132246547.7206651.971145<0.001
接种量14471.8067527235.9033758.07898170.003
误差16121.6184618895.6454702
总计12945348.3727
修正后总计274649.923626
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高产几丁质酶菌株的筛选鉴定、发酵条件优化及酶学性质分析
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张莉刚 , 潘思静 , 韦玉玲 , 李吉玲 , 潘东炜 , 张红岩 , 申乃坤 *
食品工业科技 | 生物工程 2026,47(17): 223-232
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食品工业科技 |生物工程 2026 , 47 (17) : 223 -232
高产几丁质酶菌株的筛选鉴定、发酵条件优化及酶学性质分析
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张莉刚 , 潘思静, 韦玉玲, 李吉玲, 潘东炜, 张红岩, 申乃坤*
作者信息
  • 广西民族大学海洋与生物技术学院，广西多糖材料与改性重点实验室，广西南宁 530006
通讯作者:
申乃坤（1980−），男，博士，教授，研究方向：微生物资源挖掘及代谢工程改造研究，E-mail：。
作者简介:

张莉刚（2001−），男，硕士研究生，研究方向：微生物资源开发与利用，E-mail：

Screening and Identification of High Chitinase Producing Strains, Optimization of Fermentation Conditions and Analysis of Enzymatic Properties
Ligang ZHANG , Sijing PAN, Yuling WEI, Jiling LI, Dongwei PAN, Hongyan ZHANG, Naikun SHEN*
Affiliations
  • School of Marine Sciences and Biotechnology, Guangxi Minzu University, Guangxi Key Laboratory for Polysaccharide Materials and Modifications, Nanning 530006, China
出版时间: 2026-09-01 doi: 10.13386/j.issn1002-0306.2025090236
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摘要
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为提升甲壳类废弃物中几丁质的资源化利用价值，本研究从广西海虾养殖场底部淤泥中采集样品，经初筛、复筛获得高产几丁质酶菌株并进行鉴定，再进一步通过单因素及正交优化设计确定最佳发酵参数，最后对菌株所产几丁质酶的酶学性质及酶解产物进行研究。结果表明：从几丁质固体平板上初筛获得9株透明圈较大菌株，进一步复筛获得1株高产几丁质酶（297.24±10.77 U/L）的菌株GXUN-J3，鉴定为链霉菌属（Streptomyces sp.）；条件优化获得该菌产几丁质酶的最佳工艺为：几丁质6%（w/v），大豆粉浓度0.25%（w/v），初始pH7.0，发酵温度25 ℃，装液量40 mL/150 mL，接种量5%（v/v），酶活可达1026.72±18.69 U/L，是优化前的3.51倍；酶学性质结果表明，该菌株所产几丁质酶的最适反应温度为50 ℃，最适反应pH为5.0，金属离子中Mg2+和Fe3+对酶活有激活作用，而Fe2+、Mn2+、Cu2+则有显著抑制作用（P<0.05）；化学试剂EDTA、SDS、甲醇有显著抑制作用（P<0.05）。酶解几丁质产物经薄层层析（thin layer chromatography，TLC）鉴定为几丁二糖和N-乙酰-D-氨基葡萄糖，表明该酶具有外切几丁质酶特性。本研究建立了基于链霉菌GXUN-J3的几丁质酶与几丁寡糖制备工艺，为甲壳类废弃物的高值化利用提供了研究基础。

几丁质酶  /  链霉菌  /  条件优化  /  酶学性质  /  几丁寡糖

To enhance the value-added utilization of chitin derived from crustacean waste, this study collected samples from the bottom of a shrimp farm in Guangxi. High-yield chitinase-producing strains were isolated through preliminary and secondary screening, followed by taxonomic identification. The optimal fermentation conditions were determined using single-factor experiments combined with orthogonal designs. Subsequently, the enzymatic properties and hydrolysis products of the chitinase produced by the selected strain were characterized. Results showed that initial screening on chitin-containing agar plates yielded nine strains capable of forming clear zones, among which strain GXUN-J3 exhibited the highest chitinase activity (297.24±10.77 U/L) and was identified as belonging to the genus Streptomyces sp. Under optimized fermentation conditions—6% (w/v) chitin, 0.25% (w/v) bean powder, an initial pH of 7.0, a fermentation temperature of 25 ℃, a liquid volume of 40 mL per 150 mL flask, and an inoculum size of 5% (v/v)—the chitinase activity reached 1026.72±18.69 U/L, representing a remarkable increase of 3.51-fold compared to the original process. Enzyme characterization revealed optimal activity at 50 ℃ and pH5.0. Among the metal ions tested, Mg2+ and Fe3+ significantly enhanced enzyme activity, whereas Fe2+, Mn2+, and Cu2+ exhibited significant inhibitory effects (P<0.05). Additionally, the chemical agents of EDTA, SDS, and methanol markedly suppressed enzymatic activity (P<0.05). Thin-layer chromatography (TLC) analysis demonstrated that the hydrolysis products primarily consisted of chitin dimer and N-acetyl-D-glucosamine, suggesting that this enzyme functions as an exo-chitinase. This study successfully established a process for producing chitinase and preparing chitin oligosaccharide using Streptomyces strain GXUN-J3, offering a promising approach for high-value utilization of crustacean waste.

chitinase  /  Streptomyces  /  optimization of conditions  /  enzymatic properties  /  chitooligosaccharides
张莉刚, 潘思静, 韦玉玲, 李吉玲, 潘东炜, 张红岩, 申乃坤. 高产几丁质酶菌株的筛选鉴定、发酵条件优化及酶学性质分析. 食品工业科技, 2026 , 47 (17) : 223 -232 . DOI: 10.13386/j.issn1002-0306.2025090236
Ligang ZHANG, Sijing PAN, Yuling WEI, Jiling LI, Dongwei PAN, Hongyan ZHANG, Naikun SHEN. Screening and Identification of High Chitinase Producing Strains, Optimization of Fermentation Conditions and Analysis of Enzymatic Properties[J]. Science and Technology of Food Industry, 2026 , 47 (17) : 223 -232 . DOI: 10.13386/j.issn1002-0306.2025090236
正文
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几丁质（chitin）又称甲壳素，是一种自然界含量丰富的天然高分子多糖，其结构类似于纤维素，由N-乙酰-D-氨基葡萄糖（N-acetyl-D-glucosamine，GlcNAc）通过β-1,4糖苷键连接形成，广泛存在于甲壳类动物外壳、昆虫外骨骼及真菌细胞壁中[1−2]。近年来，随着水产加工业的快速发展，每年可产生约1×106吨富含几丁质的甲壳类废弃物[3]。目前，少部分虾蟹壳经化学或生物法脱蛋白、脱矿后得到几丁质，几丁质再经化学法脱乙酰得到壳聚糖，进一步酶水解得到壳寡糖，广泛应用于农用、食品及医药等行业[4]。但多数甲壳类废弃物被直接丢弃或简单粉碎利用，造成了严重的环境污染和资源浪费[5]。而几丁寡糖保留了几丁质天然乙酰基结构，相较于壳寡糖，其生物学效应和应用前景更为显著[6]。已有研究证实，几丁寡糖具有抗氧化、抗肿瘤、免疫调节及植物防御诱导等功能[7−10]。因此，开发甲壳类生物质定向转化几丁寡糖技术，对实现海洋废弃物高值化利用具有重要战略意义。
传统工业制备几丁寡糖主要依赖强酸（如氢氟酸、硝酸）或强氧化剂（如过氧化氢）的化学法处理，该过程不仅能耗高、产物结构难以调控（常形成多聚体混合物），且伴随环境污染物及低分子量副产物的生成[11]。而酶法催化凭借其环境兼容性、底物专一性和催化精准性等优势，已成为绿色制备几丁寡糖的新兴策略。通过酶促反应定向裂解β-1,4糖苷键，可精准制备具有明确聚合度的几丁寡糖，这对开发高生物活性且水溶性优良的几丁质衍生物具有重要应用价值。
几丁质酶是特异性水解几丁质糖苷键以生成几丁寡糖或单糖的酶类统称，在细菌、真菌、病毒、昆虫、植物及动物等多种生物体内广泛存在，依据作用位点差异，几丁质酶可分为内切酶与外切酶两类[12]。内切几丁质酶随机切割几丁质长链内部位点，生成几丁寡糖；外切几丁质酶包含几丁二糖外切酶和β-N-乙酰氨基葡萄糖苷酶，前者作用于几丁质长链非还原端，切割产生N-乙酰-D-氨基葡萄糖二聚体（GlcNAc）2，后者则将内切几丁质酶生成的寡糖分解为GlcNAc，进而代谢供能。虽有报道显示部分几丁质酶可单独将几丁质水解为GlcNAc，但此类酶数量较少。绝大多数几丁质酶仅具单一活性，几丁质完全降解为GlcNAc需两种以上几丁质酶协同作用[13]。近年来，诸多产几丁质酶菌株被报道，如弧菌属（Vibrio sp.）、芽孢杆菌属（Bacillus sp.）等[14]。Du等[15]研究表明，类芽孢杆菌属（Paenibacillus sp.）所产几丁质酶的最适pH为4.5、最适温度为50 ℃，酶解产物为GlcNAc和（GlcNAc）2；Guo等[16]报道橙色微杆菌（Micromonospora aurantiaca）所产几丁质酶在pH5.0、温度55 ℃时活性最佳，水解产物为GlcNAc和（GlcNAc）2；Asmani等[17]则发现高地芽孢杆菌（Bacillus altitudinis KA15）产生的几丁质酶最适pH为5.5、最适温度为85 ℃，最终水解产物是（GlcNAc）2-（GlcNAc）5的混合物。尽管几丁质生物转化技术已取得显著进展，但现存菌株大多存在酶活性低、稳定性差以及转化效率较低等问题，这极大地限制了其工业化应用[18]。筛选与开发高效降解几丁质的菌株，对于实现甲壳类废弃物资源的高值化利用以及推动绿色生物制造而言意义重大。
本研究旨在筛选出高产几丁质酶的菌株，并进行鉴定及产酶条件优化，进一步对菌株产酶性质及产物进行分析，为生物法或酶法降解制备几丁寡糖提供理论与实验依据。
1　材料与方法
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1.1　材料与仪器
将采集自广西北海南美白对虾底泥样品装入无菌样品袋后，于4 ℃条件下带回实验室进行产几丁质酶菌株分离；粉末几丁质、酵母提取物、Chelex-100　上海源叶生物科技有限公司；N-乙酰-D-氨基葡萄糖（优级纯）　上海阿拉丁生化科技有限公司；其他均为国产分析纯。
1%（m/v）胶体几丁质的制备：称取10 g粉末几丁质，加176 mL浓盐酸搅拌均匀，4 ℃静置24 h，8000 r/min离心5 min，取沉淀用去离子水反复洗至中性，最后用去离子水定容至1000 mL，4 ℃保存备用。
LB培养基（g/L）：胰蛋白胨10.0，酵母提取物5.0，NaCl 10.0，pH自然；ISP2培养基（g/L）：麦芽糖10.0，葡萄糖4.0，酵母提取物4.0，pH自然；胶体几丁质固体培养基（g/L）：胶体几丁质4.0，（NH4）2SO4 2.0，K2HPO4 0.7，KH2PO4 0.3，MgSO4·7H2O 0.5，FeSO4·7H2O 0.01，琼脂20.0，pH自然；产几丁质酶基础发酵培养基（g/L）：粉末几丁质10.0，（NH4）2SO4 2.0，K2HPO4 0.7，KH2PO4 0.3，MgSO4·7H2O 0.5，FeSO4·7H2O 0.01，pH自然。
BSG-250恒温培养箱　上海博讯医疗生物仪器股份有限公司；H1850台式高速离心机　湖南湘仪实验室仪器开发有限公司；Epoch酶标仪　美国伯腾公司；MQD-S3NR振荡培养箱　上海旻泉仪器有限公司；Master PCR仪　德国艾本德公司。
1.2　实验方法
1.2.1　菌株的筛选
1.2.1.1　初筛
取采集样品10 g与40 mL无菌水混合，置于35 ℃、200 r/min振荡30 min，稀释涂布至LB培养基，35 ℃培养72 h后挑选单菌落接至胶体几丁质固体培养基，于30 ℃条件下培养3~7 d后测量透明圈直径（D）和菌落直径（d），计算圈径比值（D/d），根据D/d值大小初步筛选出产几丁质酶能力较强的菌株。
1.2.1.2　复筛
将产透明圈的菌株接种至基础发酵培养基，于30 ℃、200 r/min条件下振荡培养72 h后，测定菌株产几丁质酶活，复筛获得高产几丁质酶的菌株。
几丁质酶活测定：取1 mL发酵液，以12000 r/min离心5 min后，取400 μL上清液与400 μL浓度为1%的胶体几丁质充分混合，置于50 ℃恒温水浴15 min，反应完成后，迅速将其转移至沸水浴中处理10 min；水冷后，以12000 r/min离心5 min，取200 μL上清液，加入300 μL DNS试剂，再进行8 min的沸水浴处理。水冷后，取200 μL溶液在540 nm波长处测定吸光值，以煮沸灭活的发酵液作为空白对照。酶活力单位（U）定义为：在上述反应条件下，每分钟催化产生1 μmol N-乙酰-D-氨基葡萄糖所需的酶量。同时，以N-乙酰-D-氨基葡萄糖绘制标准曲线。
1.2.2　菌株的鉴定
1.2.2.1　形态学鉴定
将菌株接种于ISP2固体培养基，置于28 ℃恒温培养箱中培养96 h后进行革兰氏染色，利用光学显微镜进行观察；通过斜面插片法在三区划线后的ISP2固体培养基中进行插片，35 ℃，培养48 h，将盖玻片取出，用新鲜的2.5%戊二醛固定90 min，分别用30%、50%、70%、100%无水乙醇脱色15 min，放入干燥器内干燥，喷铂，于扫描电子显微镜下观察。
1.2.2.2　生理生化鉴定
基于形态学鉴定结果，实验菌株的系统分类学分析通过形态培养特征及生理生化特性测定完成，具体方法参照《链霉菌鉴定手册》及相关文献[19]。
1.2.2.3　分子生物学鉴定
将ISP2培养基中的单菌落转移至含35 µL Chelex-100的300 µL微量离心管中，经涡旋振荡30 s后，于金属浴中99 ℃加热40 min，之后12000 r/min离心5 min收集上清液，以16S rRNA通用引物（27F和1541R）作为扩增引物，以上述上清液作为PCR模版参照梁颖等[20]的方法进行PCR扩增。反应程序：98 ℃预变性5 min；95 ℃变性1 min，55 ℃退火1 min，72 ℃延伸90 s，35个循环；72 ℃终延伸10 min，4 ℃保存。将PCR扩增产物送测，测序结果进行多序列比对后构建系统发育树。
1.2.3　单因素实验
产几丁质酶工艺优化在150 mL三角瓶中进行，在装液量30 mL/150 mL，接种量1%（v/v），发酵初始pH7.0，发酵温度28 ℃，转速200 r/min条件下，研究不同因素对菌株GXUN-J3产几丁质酶的影响。最适碳源及浓度：以基础发酵培养基为对照，分别利用1%（w/v）的不同碳源（葡萄糖、木薯淀粉、麦芽糖、果糖、乳糖）替代基础发酵培养基中的几丁质成分，其它因素不变，根据酶活结果确定最适碳源，再进行碳源浓度优化（1%、2%、3%、4%、5%、6%、7%、8%，w/v）；最适氮源及浓度：以基础发酵培养基为对照，分别加入0.2%（w/v）的不同氮源（牛肉粉、胰蛋白胨、大豆粉、硝酸铵、氯化铵、硫酸铵），其它因素不变，根据酶活结果确定最适氮源后再进行浓度优化（0、0.05%、0.1%、0.15%、0.20%、0.25%、0.3%，w/v）；最适培养温度：基础发酵培养基接种后分别置于25、28、31、34和37 ℃培养，其它因素不变，根据酶活结果确定最适发酵温度；最适发酵初始pH：分别调整基础发酵培养基的初始pH为5.5、6.0、6.5、7.0、7.5和8.0，其他发酵因素不变，根据酶活结果确定最适发酵初始pH；最适装液量：分别调整基础发酵培养基的装液量为30、40、50、60、70、80 mL/150 mL，其它因素不变，根据酶活结果确定最适装液量；最适接种量：将接种量分别调整为1%、2%、3%、4%、5%（v/v）接种至基础发酵发酵培养基，其它因素不变，根据酶活结果确定最适接种量。
1.2.4　正交试验
根据单因素结果选取对几丁质酶活影响显著的4个因素（碳源浓度、氮源浓度、发酵温度、接种量）开展四因素三水平正交试验，正交表设计见表1。以几丁质酶活力作为优化指标，探究菌株GXUN-J3发酵产几丁质酶的最佳工艺条件，并对获得最优条件进行验证。
1.2.5　菌株GXUN-J3产几丁质酶粗酶液酶学性质分析
1.2.5.1　几丁质酶粗酶液的制备
取菌株GXUN-J3发酵液，于4 ℃，12000 r/min离心10 min，收集上清。向上清中缓慢加入硫酸铵粉末并持续搅拌，使其硫酸铵饱和度达到50%，于4 ℃静置过夜。次日，于4 ℃，10000 r/min离心30 min，所得沉淀为几丁质酶粗产物。用pH7.0的磷酸盐缓冲液溶解沉淀，得到粗酶液，4 ℃保存备用[20]。
1.2.5.2　温度对酶活性及稳定性的影响
将反应体系分别置于30、40、50、60、70 ℃的温度条件下反应15 min，测定不同温度下几丁质酶活力大小，确定最佳反应温度。同时，将粗酶液在上述温度梯度下恒温孵育2 h，测定酶活力，以最高酶活力为100%，计算不同温度下的相对酶活，观察其温度稳定性。
1.2.5.3　pH对酶活性及稳定性的影响
取pH4.0、5.0、6.0、7.0、8.0的柠檬酸-磷酸缓冲液，与粗酶液按1:1的体积比混合，在最适温度下测定几丁质酶活力，确定最适反应pH。将粗酶液置于上述pH缓冲液中，在最适温度下恒温孵育2 h，测定酶活力，以最高酶活力为100%，计算不同pH条件下的相对酶活，观察其pH稳定性。
1.2.5.4　金属离子及生化试剂对酶活性的影响
将粗酶液分别置于终浓度为5 mg/mL和10 mg/mL的Fe2+、Mg2+、Fe3+、K+、Mn2+、Zn2+、Cu2+、Na+金属离子溶液中孵育2 h，测定几丁质酶活力，以未加金属离子时的酶活为100%，计算添加不同金属离子后的相对酶活。
将粗酶液分别置于终浓度为5和10 mg/mL的乙二胺四乙酸（ethylenediaminetetraacetic acid，EDTA）、十二烷基硫酸钠（sodium dodecyl sulfate，SDS）、二甲基亚砜（dimethyl sulfoxide，DMSO）、聚山梨酯 80（polysorbate 80，Tween 80）、甲醇、乙醇、丙酮、异丙醇生化试剂溶液中孵育2 h，测定几丁质酶活力，以未加生化试剂时的酶活为100%，计算添加不同生化试剂后的相对酶活。
1.2.5.5　酶的底物特异性
将粗酶液分别与浓度为10 mg/mL的胶体几丁质、粉末几丁质、片状几丁质、粉末壳聚糖、虾壳粉等底物反应，测定几丁质酶活力，以最高底物酶活100%，计算其他底物的相对酶活，观察其底物特异性。
将粗酶液分别与1%、2%、3%、4%、5%、6%（w/v）的胶体几丁质反应，测定几丁质酶活力，以最高底物浓度酶活为100%，计算其他底物浓度的相对酶活，观察其底物浓度对酶活的影响。
1.2.5.6　薄层层析法（thin layer chromatography，TLC）测定酶解产物
以10 g/L胶体几丁质为底物，按1:1（v/v）与粗酶液混合，在50 ℃分别反应0、0.5、1、2、4、6、12、24 h。反应后沸水浴10 min，再以12000 r/min离心10 min，取上清在硅胶板上点样。以几丁寡糖为标样，将硅胶板放入层析缸，加入展层剂（冰乙酸:正丁醇:水:氨水=13:26:13:2，v/v）缓慢展开。当层析液距硅胶板上边缘1 cm时，结束层析。取出硅胶板，50 ℃烘干10 min，均匀喷涂显色剂（二苯胺:丙酮:苯胺:磷酸=1:50:1:5），110 ℃烘干10 min显色。通过酶解产物与标样几丁寡糖在硅胶板上的分离位置比对，判断该几丁质酶为内切型或外切型。
1.3　数据处理
所有实验均设置三个生物学重复，实验结果以“平均值±标准差”表示。数据经Microsoft Excel 2019进行处理，随后采用IBM SPSS Statistics 21.0进行显著性分析和正交方差分析，用GraphPad Prism 8进行图形绘制。
2　结果与分析
收起
2.1　产几丁质酶菌株的筛选、鉴定
从采集的海虾养殖场底部淤泥中共筛选到9株可在胶体几丁质固体平板上产明显透明圈的菌株，菌株GXUN-J3的D/d最大为1.84±0.17（图1、表2），将其接种到几丁质发酵培养基中进行摇瓶复筛。以N-乙酰-D-氨基葡萄糖标准品绘制标准曲线，y=2.4088x-0.1477，R2=0.9971。菌株在几丁质基础发酵培养基中复筛结果如表2所示，菌株GXUN-J3展现出显著（P<0.05）高于其他菌株的几丁质酶活性（297.24±10.77 U/L），故将其确定为后续研究的菌株。
将菌株GXUN-J3在ISP2平板上进行划线接种，于28 ℃培养2周。培养后，菌落呈现粉红色，表面干燥、不透明，隆起且紧密附着于培养基，难以挑取（图2A），该菌株革兰氏染色呈阳性（图2B），在测试培养基上分泌金黄色色素，形成具有广泛分支的基质菌丝体和气生菌丝。气生菌丝进一步分化为表面光滑的圆柱形孢子，排列成直孢子链（图2C）。
生理生化特性鉴定结果（表3）显示，其生长温度范围为20~40 ℃，可耐受的pH范围为5.0~8.0，能在0~4%（w/v）NaCl的环境中生长；过氧化氢酶、纤维素水解酶、酪蛋白水解酶、明胶液化及硫化氢试验呈阳性，而VP、MR、硝酸盐产气和淀粉水解酶试验呈阴性。该菌株能够以麦芽糖、葡萄糖、果糖、棉子糖、甘油和甘露糖作为唯一碳源进行生长，但无法利用蔗糖、木糖、海藻糖、甘醇、肌醇和半乳糖等碳源。
16S rRNA序列比对表明，其与杨浦链霉菌（Streptomyces yangpuensis fd2-tb）的相似度高达99%；进一步构建系统发育树结果显示菌株GXUN-J3与S. yangpuensis fd2-tb亲缘关系最为接近（图3）。综合形态学、生理生化及16S rRNA序列分析结果，可将菌株GXUN-J3鉴定为链霉菌属（Streptomyces sp.）。
几丁质酶在几丁寡糖工业化生产中应用潜力巨大。当前，利用微生物产几丁质酶水解几丁质来生产几丁寡糖，是一种高效且环保的方法，已有研究表明几丁质酶已在多种生物体中被发现，如寡养单胞菌属（Stenotrophomonas sp.）[21]、嗜麦芽窄食单胞菌（Stenotrophomonas maltophilia）[22]和淀粉酶链霉菌（Streptomyces diastaticus）[23]等。本研究中，筛选获得的高产几丁质酶的菌株GXUN-J3，其几丁质酶活性显著高于已报道的大部分菌株，显示出较强的产酶能力，在工业生产几丁寡糖上有较好的应用潜力。
2.2　单因素实验
碳源优化结果表明（图4A），与其他碳源相比，粉末几丁质为碳源时，酶活力最高，这可能是由于几丁质酶作为一种诱导酶在几丁质的诱导下才能大量表达[5]；进一步浓度优化结果表明，当粉末几丁质添加量为7%（w/v）时，菌株产酶活力最高，可达947.77 U/L（图4B）。最适氮源及浓度优化结果表明（图4C、图4D），该菌株产酶的最适氮源为0.25%（w/v）大豆粉，有研究表明与其它氮源相比，大豆粉更容易被利用，推测可能是因为大豆粉不仅能提供必要的氮元素，还提供了很多必需的生长因子[21]。发酵温度优化结果如图4E所示，当发酵温度低于28 ℃时，随着温度较高，酶活迅速升高，28 ℃时达到最大为300.78 U/L；但当温度高于28 ℃时，酶活随温度升高而迅速降低。因此，菌株GXUN-J3发酵产酶的最适温度为28 ℃，这与大部分链霉菌的报道一致，链霉菌发酵产酶的最适温度在25~30 ℃[23]。当发酵初始pH低于7.0时，随着pH升高，菌株GXUN-J3产几丁质酶活性迅速升高，初始pH为7.0时达到最大为301.02 U/L；但当pH高于7.0时，酶活随pH升高而迅速降低，推测可能是过高或过低的pH会影响菌株的生长进而导致酶活的降低。因此，确定菌株GXUN-J3发酵产酶的最适初始pH为7.0（图4F）。装液量优化结果表明，当装液量为30~40 mL/150 mL时，酶活随装液量增加而升高；但装液量高于40 mL/150 mL时，酶活随装液量升高而显著下降（P<0.05），可能是装液量太高时，培养基中溶氧供应不足，导致菌体生长受到影响，从而导致产酶效率大幅下降[14]。因此，确定菌株GXUN-J3产酶的最适装液量为40 mL/150 mL（图4G）。当接种量为1%~4%（v/v）时，菌株GXUN-J3产几丁质酶活力随接种量增加而升高；但当接种量高于4%（v/v）时，酶活会迅速下降，可能是由于过高的接种量会急剧消耗培养基中的氧气和营养物质，从而导致菌株的酶活力降低[17]。因此，确定菌株GXUN-J3发酵产几丁质酶的最适接种量为4%（v/v）（图4H）。
2.3　正交试验
根据单因素优化结果可知，碳源浓度、氮源浓度、发酵温度、接种量、初始pH和装液量均对几丁质酶活具有显著影响（P<0.05），但初始pH和装液量对酶活有负效应。因此，本研究选取对酶活具有正效应的4个因素（碳源浓度、氮源浓度、发酵温度、接种量）开展四因素三水平正交试验。结果如表4所示，通过极差分析（R值）与方差分析（表5）确定各因素主效应，确定最优参数组合为：6%（w/v）的粉末几丁质（A1）、0.25%（w/v）的大豆粉（B2）、培养温度25 ℃（C1）及5%（v/v）的接种量（D3），对正交试验获得最佳条件进行验证实验，测得酶活为1026.72±18.69 U/L，较初始条件（297.24±10.77 U/L）提升2.51倍。
产几丁质酶的菌株在实际应用中常面临酶活低、稳定性差等难题。以几丁质酶活力为关键指标，通过优化发酵工艺来提高菌株产酶的活性，有望显著提升几丁质废弃物的生物转化效率，为资源化利用提供技术支持。张瑶心等[24]对无色杆菌属（Achromobacter sp.）ZWW8进行研究，经单因素条件优化后，其胞外上清酶活力达33.9 U/L，为优化前的8倍。严佳佳[25]针对弧菌属（Vibro sp.）Y-8中的两个几丁质酶Chi1和Chi2开展研究，经发酵工艺优化后，Chi1酶活力从70 U/L提升至135 U/L，为优化前的1.92倍；Chi2酶活力从73 U/L提升至123 U/L，为优化前的1.73倍。本研究对GXUN-J3的发酵条件进行单因素、正交试验优化后，酶活可达1026 U/L，较优化前提高2.51倍。为GXUN-J3菌株产几丁质酶的进一步开发利用提供了数据支持，也为酶法降解虾壳废弃物生产几丁寡糖的深入探究提供了实验依据。
2.4　菌株GXUN-J3产几丁质粗酶液的酶学性质
2.4.1　最适反应温度和温度稳定性
如图5A所示，当反应温度在30~50 ℃时，几丁质酶活随温度升高而逐渐增大，50 ℃时达到最大；但当温度高于50 ℃，酶活随反应温度升高而迅速降低。在低温条件下（<30 ℃），酶与底物分子间运动速率的降低可能导致催化效率下降；而高温环境（>50 ℃）下引起了酶分子高级结构的改变，从而导致酶变性失活，酶活降低。热稳定性分析结果（图5B）显示，该酶在30~50 ℃孵育2 h后仍保持85%以上的活性，当处理温度超过50 ℃时，酶活性下降至初始值的50%以下，几丁质酶的热稳定性与其结构密切相关，其一级结构和二级结构并不会因高温环境而产生变化，但高温条件下三级结构和四级结构会遭到破坏，最终导致几丁质酶活力的丧失[26]。
已有研究表明，多数几丁质酶的最适反应温度范围为40~60 ℃，如苏云金芽孢杆菌（Bacillus thuringiensis）Bt028菌株产几丁质酶最适温度60 ℃[27]。本研究中GXUN-J3菌株产几丁质酶的最适温度为50 ℃，且在30~50 ℃孵育2 h后仍具有较高的活性。此温度响应特性与鱼源假交替单胞菌（Pseudoalteromonas piscicida）C923菌株所产酶类似，后者在低于45 ℃时稳定性显著优于高温条件[28]。
2.4.2　最适反应pH和pH稳定性
pH对酶活性影响结果如图5C所示，该酶在pH为4.0~8.0时，都对几丁质具有一定的降解活性，但当pH为5.0，酶活性最高，因此，该粗酶液最适pH为5.0；pH稳定性实验表明（图5D），在pH6.0~7.0缓冲体系中孵育2 h后，相对酶活维持在90%以上，显示出该酶在pH6.0~7.0范围内具有良好的pH稳定性，但当pH<6.0和>7.0时，相对酶活显著下降（P<0.05），酶的稳定性较差，可能是因为pH偏高或者偏低时会影响酶分子活性部位上有关基团的解离状态，导致酶分子高级结构的构象变化，最终引起催化功能的失活[29]。与蜡样芽孢杆菌（Bacillus cereus）B120菌株产酶的最适pH8.0不同[30]，本研究分离的几丁质酶在pH5.0时活性最高，且在pH6.0~7.0范围内维持较高稳定性。该特性表明该酶更适宜在中性偏酸环境中催化底物反应，进一步印证了不同菌株产酶的最适pH存在显著差异。
2.4.3　金属离子对几丁质酶活力的影响
图5E显示不同金属离子对几丁质酶活性的影响，在5 mg/mL和10 mg/mL浓度下，大部分金属离子均能干扰几丁质酶的活性。具体而言，Mg2+和Fe3+能显著提高酶活力（P<0.05），相比于低浓度的Mg2+和Fe3+来说，高浓度的Mg2+和Fe3+对该酶活的影响更加显著，相对酶活力分别可达112.12%、133.30%，其中Fe3+的激活作用与B. thuringiensis Bt028菌株产酶特性具有一致性[27]，金属离子可能通过与酶蛋白形成稳定复合物或者参与活性中心构象调控酶活性，在激活效应中，金属离子可作为辅因子稳定活性中心结构，同时通过结合变构位点增强酶-底物亲和力[31]。5 mg/mL和10 mg/mL的Fe2+、Mn2+、Cu2+能显著抑制酶活力（P<0.05），其中10 mg/mL的Cu2+则对酶活性的抑制尤为严重，相对酶活力降低到原来的38.62%，这与陈苏南等[32]的报道一致，Cu2+是大多数几丁质酶的抑制剂，其原因可能是金属螯合作用可能改变酶的三级结构，降低催化位点的底物识别效率。
2.4.4　生化试剂对几丁质酶活力的影响
不同生化试剂对几丁质酶活性的影响如图5F所示，DMSO、Tween80、乙醇、丙酮、异丙醇对几丁质酶有一定的抑制效果，而EDTA、SDS、甲醇的抑制效果更加显著（P<0.05）；在5 mg/mL和10 mg/mL浓度的EDTA影响下，相对酶活力降低为原来的91.54%、82.84%，表明该酶可能属于金属依赖性酶类，其螯合作用导致必需金属离子的流失，这与Guo等[33]报道的EDTA对几丁质酶的抑制作用相似；10 mg/mL的SDS和甲醇对该几丁质酶的抑制效果分别可达75.43%和21.48%，SDS作为离子型表面活性剂能与蛋白质结合使蛋白质变性而沉淀，甲醇则可能通过破坏酶蛋白的氢键网络，诱导局部结构域变性失活[34]，生化试剂对该酶活的具体作用机制有待进一步深入研究。这些调控效应提示在工业化应用中需充分考虑环境因子对酶活性的影响。
2.4.5　底物特异性和最适底物浓度对几丁质酶活力的影响
如图5G所示，几丁质酶对胶体几丁质显示出高度底物特异性，其酶活力较粉末几丁质提升1.3倍，而片状几丁质、粉末壳聚糖和虾壳粉的酶活力仅为胶体几丁质底物的1.58%、0.82%和2.79%，这与Xie等[35]报道的几丁质酶Chi23相似，由于天然几丁质致密的晶体结构，绝大多数几丁质酶对天然几丁质都表现出有限的几丁质酶活力，胶体底物的高催化效率推测源于粉末几丁质通过酸性预处理工艺破坏β-1,4糖苷键的三维晶体结构，形成具有更高比表面积的无定形胶体形态，更易于酶分子识别并结合其底物结合位点，对片状几丁质和虾壳粉酶活较低的原因可能是片状几丁质的高结晶度及虾壳粉的复杂基质阻碍酶-底物结合，对粉末壳聚糖几乎没有活性可能是基于外切酶的特异性催化机制，该酶对壳聚糖底物缺乏有效催化能力[36]。由图5H可知，在1%~5%浓度梯度范围内，酶促反应初速度与底物浓度呈典型双曲线关系，浓度超过5%后，反应速率趋于稳定，符合米氏动力学的底物饱和特征。
2.5　菌株GXUN-J3产几丁质粗酶液的酶解产物测定
薄层色谱分析显示（图6），菌株GXUN-J3分泌的几丁质酶对胶体几丁质底物呈现典型外切酶作用模式，随反应时间延长（0~120 min），水解产物中寡糖组分呈持续积累趋势，其中几丁二糖的生成量在120 min内显著增加并达到平台期，同时有少量N-乙酰-D-氨基葡萄糖的存在，酶学特性分析表明，该酶系通过β-1,4糖苷键的外切模式催化底物降解，终产物构成符合外切几丁质酶的典型特征。
微生物几丁质酶根据其作用方式不同，可分为内切几丁质酶和外切几丁质酶；内切酶通过随机切割β-1,4糖苷键，将几丁质分子降解为低分子量N-乙酰氨基葡萄糖寡聚物。外切酶根据催化特性差异分为两类：I型外切酶从非还原端连续水解产生（GlcNAc）2，II型外切酶则特异性水解寡聚物生成GlcNAc单体[37]。现有研究表明微生物来源的几丁质酶以外切型为主，谢啟发等[38]报道厦门加莱菌（Gallaecimonas xiamenensis）分泌的几丁质酶可特异性水解胶体几丁质生成（GlcNAc）2和GlcNAc，He等[39]研究发现轮虫弧菌（Vibrio rotiferianus Chi1557）几丁质酶对胶体几丁质具有外切酶活性，主要产物为（GlcNAc）2，本研究中GXUN-J3菌株所产几丁质酶同样呈现典型外切酶特性，与文献报道的微生物几丁质酶作用模式一致，外切型几丁质酶作为几丁质降解体系的核心组分，在农业病虫害生物防治、功能性寡糖生物制备及甲壳类废弃物资源化利用等领域展现出重要应用潜力，本研究结果为GXUN-J3菌株的工业化产酶工艺优化及甲壳类生物质废弃物的高值化利用提供了理论支撑。
3　结论
收起
本研究成功从广西海虾养殖场淤泥中筛选出一株高产几丁质酶的链霉菌GXUN-J3，通过单因素及正交试验优化其发酵条件，最优条件下几丁质酶酶活可达1026.72 U/L，是优化前酶活的3.51倍。酶学性质分析表明，该菌株所产几丁质酶的最适反应条件为50 ℃、pH5.0，且具有典型外切酶特性，可高效水解几丁质生成几丁二糖与N-乙酰-D-氨基葡萄糖；金属离子中Mg2+与Fe3+对酶活有激活作用，而化学试剂EDTA、SDS及部分金属离子则显著抑制酶活性。本研究不仅为几丁质酶的高效制备提供了优良菌株和工艺参数，也为甲壳类废弃物的资源化利用奠定了理论基础，在农业、食品及医药等领域的几丁寡糖绿色制造中具有潜在应用价值。

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2026年第47卷第17期
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doi: 10.13386/j.issn1002-0306.2025090236
  • 接收时间：2025-09-22
  • 首发时间：2026-10-24
  • 出版时间：2026-09-01
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  • 收稿日期：2025-09-22
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    广西民族大学海洋与生物技术学院，广西多糖材料与改性重点实验室，广西南宁 530006

通讯作者:

申乃坤（1980−），男，博士，教授，研究方向：微生物资源挖掘及代谢工程改造研究，E-mail：。
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2种不同金属材料的力学参数
科
Family		 属数
Number of
genus		 种数
Number of
species		 占总种数比例
Percentage of
total species (%)		 属
Genus		 种数
Number of
species		 占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
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