CN112409933A - 一种鱼源明胶及纳米纤维膜的生产方法 - Google Patents
一种鱼源明胶及纳米纤维膜的生产方法 Download PDFInfo
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Abstract
本发明属于生物材料领域,涉及一种鱼源明胶及纳米纤维膜的生产方法;步骤为:将鲟鱼鳔解冻,清洗,搅碎,过筛,以超声波依次辅助工业酒精和六号溶剂油脱脂,压滤,风干,得到脱脂鱼鳔;放入热水,连续搅拌浸提,离心取上清液,经喷雾干燥得到鱼源明胶,再溶于乙酸‑水溶液,静电纺丝得到纳米纤维,与硅胶和戊二醛独立放于真空干燥箱中蒸汽交联,即得纳米纤维膜。明胶的提取避免了当前用时长、能耗多、污染大的技术缺陷,实现了明胶的清洁高效生产;明胶的产率、感官、理化和功能指标优于市售商业明胶;纳米纤维膜光滑平整,孔隙率高,亲水性强,机械性能佳,且生物安全性、降解性和相容性好,可应用于食品、医药、环境、能源及生物材料等领域。
Description
技术领域
本发明属于生物材料领域,具体涉及一种鱼源明胶的清洁提取及纳米纤维膜的高效制备。
技术背景
明胶是一种重要的天然高分子物质,广泛应用于食品、医药、化妆品、生物材料等领域。当前明胶主要来源于畜禽,但人与畜禽共患病的频繁发生,使其安全性越来越让人担忧;同时,宗教习俗也使其应用和贸易受到了一定限制。我国是一个渔业大国,每年上千万吨的加工废弃物造成了严重的资源浪费和环境污染,若以此为原料生产可以替代传统畜禽来源的明胶,不仅可以提高明胶制品的生物安全性,而且能够促进渔业可持续发展和国家生态文明建设。
根据原料预处理方法,明胶可分为酸法(A型)明胶和碱法(B型)明胶,其生产均存在预处理时间长、生产效率低、水电消耗大、环境污染重等缺点,且酸碱作用会导致胶原蛋白分子共价键大量断裂,过度破坏胶原蛋白亚基完整性,进而影响明胶理化功能特性和应用潜力。若能建立无酸碱预处理的清洁提取方法,对我国明胶产业的发展将具有重要现实意义。
纳米纤维是指直径在1~100nm的纤维,具有直径小、比表面积大、空隙率高等特点,具备小尺寸、表面、量子隧道等效应,拥有力学、光学、热学、磁学、生物学等特性。当前研究人员已研制出了腈纶、尼龙、聚丙烯醇、聚已内酯、聚乳酸、醋酸纤维素、丝素蛋白等多种纳米纤维及薄膜,并尝试应用于食品、医药、环境、能源、化工、生物材料等领域。但目前,无酸碱预处理的明胶清洁提取方法和以鱼源明胶为基材的纳米纤维膜高效制备技术尚未见报道。
发明内容
针对上述现有技术存在的不足,本发明创建了一种无酸碱预处理的鱼源明胶清洁提取方法,建立了一种以鱼源明胶为基材的纳米纤维膜高效制备技术,可应用于食品、医药、环境、能源、化工、生物材料等领域。
为了实现以上目的,本发明采取以下技术方案:
本发明首先提供一种鱼源明胶的制备方法,具体步骤如下:
(1)原料预处理:将鲟鱼鳔解冻,清洗,搅碎,经筛网过滤,得到鱼鳔颗粒;加入工业酒精,进行超声波辅助脱脂;压滤后,得到的鱼鳔颗粒再加入六号溶剂油,进行第二次超声波辅助脱脂;最后压滤,风干,得到脱脂鱼鳔;
(2)明胶提取:将步骤(1)得到的脱脂鱼鳔放入热水,连续搅拌浸提;然后离心,取上清液,经喷雾干燥,得到白色粉末,即为鱼源明胶。
优选的,步骤(1)中所述鱼鳔颗粒与工业酒精或六号溶剂油的用量比均为1kg:3~5L。
优选的,步骤(1)中所述超声波辅助脱脂的条件均为:强度20~30W/L,时间6~12h,温度25~40℃;所述筛网的目数为7~12目。
优选的,步骤(2)中所述脱脂鱼鳔与热水的用量比1kg:7~10L,所述热水的温度为50~55℃,所述浸提的时间为30~60min。
优选的,步骤(2)中所述离心的条件为:离心力10000~20000g,时间30~60min;所述喷雾干燥的条件为:进气温度180~200℃,排气温度100~120℃。
此外,本发明还提供一种以鱼源明胶为基材的纳米纤维膜的制备方法,具体步骤如下:
纳米纤维膜制备:将所得鱼源明胶溶于乙酸-水溶液,进行静电纺丝于铝箔,得到纳米纤维;再将纳米纤维和戊二醛、硅胶独立放入同一真空干燥箱,通过抽真空和加热进行蒸汽交联,得到鱼源明胶纳米纤维膜。
优选的,所述乙酸-水溶液的乙酸浓度为20~25%(v/v),所述明胶在乙酸-水溶液中的浓度25~30%(w/v)。
优选的,所述静电纺丝的条件为:进料1~2μL/min,电压15~20kV,针头20~22号,针尖与收集器距离12~18cm,湿度30~50%;所述交联的条件为:温度50~60℃,时间1~3h,真空度-0.09~-0.08Mpa。
优选的,所述纳米纤维、戊二醛和硅胶的用量比为1kg:5-7L:30-50kg。
本发明的有益效果
1.在原料方面,本发明以鱼鳔为原料生产明胶,既避免了传统畜禽明胶的不安全因素和宗教习俗限制,又实现了鱼鳔的资源化和高值化利用。
2.在明胶方面,本发明避免了当前耗时长、能耗多、污染大的原料酸碱预处理工序,建立了一种无酸碱预处理的鱼源明胶清洁提取方法,且该明胶的得率和感官、理化、功能指标均优于当前市售商业明胶。
3.在纳米纤维膜方面,本发明以鱼源明胶为基材,先以静电纺丝法制备纳米纤维,再以戊二醛蒸汽交联生产纳米纤维膜,该膜光滑平整,孔隙率高,亲水性强,机械性能佳,且生物安全性、降解性和相容性优于现有纳米纤维膜。
附图说明
图1为实施例1制备鱼源明胶的SDS-PAGE图谱。
图2为实施例1制备鱼源明胶的红外光谱。
图3为实施例1制备鱼源明胶的拉曼光谱。
图4为实施例1制备鱼源明胶的流变学行为。
图5为实施例1制备鱼源明胶的表观黏度。
图6为明胶冻干样品(左起第一列)、脱水凝胶(左起第二列)和纳米纤维膜(左起第三列)的微观结构。
其中,SG是指实施例1得到的鱼源明胶,PG、BG和FG分别是指购于Sigma-Aldrich公司的猪皮(A型)、牛皮(B型)和冷水鱼皮(B型)明胶。
具体实施方式
结合以下实例,对本发明进行进一步详细说明。
实施例1:
(1)将100kg鲟鱼鳔解冻,清洗,搅碎,过10目筛;加入工业酒精400L,在35℃以25W/L的超声波辅助脱脂9h;压滤后,在同等超声波辅助条件下再次以六号溶剂油脱脂9h;最后压滤,自然风干,即得脱脂鱼鳔30kg;
(2)将步骤(1)所得脱脂鱼鳔放入250L的52℃热水中,连续缓慢搅拌45min,然后15000g离心45min,取上清液,在进气温度190℃和排气温度110℃条件下喷雾干燥,即得感官、理化和功能特性俱佳的鱼源明胶23kg;
纳米纤维膜制备:将步骤(2)所得的鱼源明胶1kg溶于3.7L的22%(v/v)乙酸-水溶液;在进料1.5μL/min、电压18kV、针头21号、针尖与收集器距离15cm、湿度40%的条件下进行静电纺丝于铝箔,得到纳米纤维;再将纳米纤维和6L戊二醛、40kg硅胶独立放入同一真空干燥箱,相互之间不接触,在温度55℃、真空度-0.085MPa的条件下进行蒸汽交联2h,即得外观、理化、机械和生物性能俱佳的鱼源明胶纳米纤维膜。
实施例2:
(1)将100kg鲟鱼鳔解冻,清洗,搅碎,过12目筛;加入工业酒精300L,在25℃以30W/L的超声波辅助萃取脱脂12h;压滤后,在同等超声波辅助条件下再次以六号溶剂油萃取脱脂12h;最后压滤,自然风干,即得脱脂鱼鳔31kg;
(2)将步骤(1)所得脱脂鱼鳔放入210L的55℃热水中,连续缓慢搅拌60min,然后20000g离心30min,取上清液,在进气温度200℃和排气温度120℃条件下喷雾干燥,即得感官、理化和功能特性俱佳的鱼源明胶23kg。
纳米纤维膜制备:将步骤(2)所得的鱼源明胶1kg溶于4L的25%(v/v)乙酸-水溶液;在进料2μL/min、电压20kV、针头22号、针尖与收集器距离18cm、湿度30%的条件下进行静电纺丝于铝箔,得到纳米纤维;再将纳米纤维和7L戊二醛、50kg硅胶独立放入同一真空干燥箱,相互之间不接触,然后在温度60℃、真空度-0.08MPa的条件下进行蒸汽交联1h,即得外观、理化、机械和生物性能俱佳的鱼源明胶纳米纤维膜。
实施例3:
(1)将100kg鲟鱼鳔解冻,清洗,搅碎,过7目筛;加入工业酒精500L,在40℃以20W/L的超声波辅助萃取脱脂6h;压滤后,在同等超声波辅助条件下再次以六号溶剂油萃取脱脂6h;最后压滤,自然风干,即得脱脂鱼鳔30kg;
(2)将步骤(1)所得脱脂鱼鳔放入300L的50℃热水中,连续缓慢搅拌30min,然后10000g离心60min,取上清液,在进气温度180℃和排气温度100℃条件下喷雾干燥,即得感官、理化和功能特性俱佳的鱼源明胶22kg;
纳米纤维膜制备:将步骤(2)所得的鱼源明胶1kg溶于3.4L的20%(v/v)乙酸-水溶液;在进料速度1μL/min、电压15kV、针头20号、针尖与收集器距离12cm、湿度50%的条件下进行静电纺丝于铝箔,得到纳米纤维;再将纳米纤维和5L戊二醛、30kg硅胶独立放入同一真空干燥箱,相互之间不接触,然后在温度50℃、真空度-0.09MPa的条件下进行蒸汽交联3h,即得外观、理化、机械和生物性能俱佳的鱼源明胶纳米纤维膜。
性能测试
选择实施例1得到的鱼源明胶(SG)及纳米纤维膜进行后续性能测试。
测试方法:
以购自Sigma-Aldrich公司的猪皮(PG,A型)、牛皮(BG,B型)、冷水鱼皮(FG,B型)明胶为参照,检测如下指标。
(1)分子结构
采用邻苯二甲醛法测定水解度(DH);根据公式计算平均分子量(AMW):AMW=ACL×90,ACL=100/DH,其中ACL为平均链长;采用5%分离胶与3%浓缩胶不连续电泳系统获得SDS-PAGE图谱;将样品于110℃的6M盐酸中水解24h后,利用氨基酸自动分析仪检测氨基酸组成;利用中红外光谱仪KBr压片法获得红外光谱;应用拉曼光谱仪在1064nm激发波长下获得拉曼光谱。
(2)理化特性
利用pH计测定明胶溶液(1%)的酸碱度;分光光度计(1cm光路)检测明胶溶液(6.67%)的透射比;色度计分析明胶溶液(2%)的色泽。
(3)功能特性
将1份大豆油和3份明胶溶液(0.1%)混合,18000rpm均质2min,通过分光光度法检测乳化性(EAI)及稳定性(ESI);将明胶溶液(0.5%)在18000rpm均质1min,通过测量液体和气泡体积计算起泡性(FE)及稳定性(FS)。
(4)凝胶特性
利用质构仪测定凝胶强度(GS);离心法测定凝胶持水性(WHC);旋转流变仪测定凝胶流变学行为,包括升温和降温储能模量(G′h和G′c)、升温和降温损耗模量(G″h和G″c)、胶凝温度(Tg)、胶融温度(Tm)和表观黏度(Vis)。
(5)微观结构
利用扫描电镜观察冻干明胶(2%)、脱水凝胶(6.67%)和纳米纤维膜结构。
测试结果:
(1)分子结构
从图1可以看出,SG肽链较为集中,至少含有两条α链(α1和α2)及二聚体(β链),与I型胶原蛋白相似。SG中还存在少量的其它肽链,但其含量远低于PG、BG和FG。此外,SG的平均分子量为9.84kDa,远低于胶原蛋白(约300kDa),但显著高于PG(4.45kDa)、BG(5.68kDa)和FG(3.52kDa)。
从表1可以看出,SG中甘氨酸含量最高(约1/3),丙氨酸、脯氨酸、谷氨酸和羟脯氨酸含量相对较高,而半胱氨酸、蛋氨酸、组氨酸、酪氨酸和赖氨酸含量较低,色氨酸未检出。SG中亚氨基酸(脯氨酸和羟脯氨酸)含量为18.24%,高于FG(16.96%),但低于BG(23.29%)和PG(22.96%)。
从图2可以看出,与其它明胶相比,SG酰胺A峰出现在较高频率(3306cm-1),表明较少的NH基团参与了氢键的形成;酰胺B峰发生在较低波数(2932cm-1),说明肽链间存在较多的CH2基团交联;酰胺I峰和II峰频率较高(1645cm-1和1550cm-1),表明分子间较高的交联度;酰胺III峰与三股螺旋结构有关,其更高的振幅表明了更有序的分子结构。
从图3可以看出,SG酰胺I峰和II峰信息与红外光谱一致。值得注意的是,SG的931cm-1峰振幅明显高于其它明胶,表明了其较高的分子量。
表1明胶的氨基酸组成(残基数/1000个残基)
(2)理化特性
从表2可以看出,SG的pH值为6.87,低于A型的PG(7.90),但高于B型的BG(5.26)和FG(4.96)。SG在450nm(40.56%)和620nm(59.07%)的透射比(T)均最低,但仍符合美国药典(USP36-NF31)和中国食品安全标准(GB6783-2013)。SG亮度(L*,95.79)与FG相似,但高于PG和BG;红度(a*,–0.06)最高,而黄度(b*,1.18)最低;总色差(ΔE,3.38)最低,表明SG的白度最高。
表2明胶的理化特性
(3)功能特性
从表3可以看出,SG的乳化活性指数(EAI)最高(171.76m2/g),但乳化稳定性指数(ESI)最低(30.09min);起泡活性(FE)为203.00,与FG相似,但低于PG和BG;起泡稳定性(FS)为26.92,高于FG,但低于PG和BG。
表3明胶的功能特性
(4)凝胶特性
从表4可以看出,SG的凝胶强度(GS)和持水性(WHC)分别达到853.23g和92.37%,均高于其它明胶。结合图4可知,SG的胶凝温度(Tg)和胶融温度(Tm)分别为16.88℃和21.80℃,均低于PG和BG。SG的储能模量(G′)为2186.35Pa,高于PG,但低于BG;损耗模量(G″)为74.54Pa,高于PG和BG。结合图5可知,SG的表观黏度(Vis)为28.60mPa·s,低于BG,但高于PG和FG。
表4明胶的凝胶特性
(5)微观结构
从图6可以看出,冻干明胶呈现不规则的多孔网状结构。脱水凝胶呈现致密多孔的海绵结构,但SG凝胶孔洞更均匀光滑,规则有序,表明其更好的凝胶品质。纳米纤维膜中的纳米纤维表面光滑,直径均匀,连续性好,无串珠结构,但SG纤维直径更低(约75nm),孔径更小,且无纤维间交联现象。
综上所述:实施例1得到的鱼源明胶:1)平均分子量为9.84kDa,具有I型胶原蛋白相似的分子结构;2)pH为6.87,白度为3.38,透射比符合美国药典和中国食品安全标准;3)乳化活性指数为171.76m2/g,稳定性指数为30.09min;起泡性为203.00,稳定性为26.92;4)凝胶强度为853.23g,持水性为92.37%,胶凝温度为16.88℃,胶融温度为21.80℃,储能模量为2186.35Pa,损耗模量为74.54Pa,表观黏度为28.60mPa·s;5)凝胶孔洞均匀光滑,规则有序;纳米纤维表面光滑,直径均匀(约75nm),连续性好,无串珠结构,无纤维间交联现象。
说明:以上实施例仅用以说明本发明而并非限制本发明所描述的技术方案;因此,尽管本说明书参照上述的各个实施例对本发明已进行了详细的说明,但是本领域的普通技术人员应当理解,仍然可以对本发明进行修改或等同替换;而一切不脱离本发明的精神和范围的技术方案及其改进,其均应涵盖在本发明的权利要求范围内。
Claims (9)
1.一种鱼源明胶的制备方法,其特征在于,具体步骤如下:
(1)原料预处理:将鲟鱼鳔解冻,清洗,搅碎,经筛网过滤,得到鱼鳔颗粒;加入工业酒精,进行超声波辅助脱脂;压滤后,得到的鱼鳔颗粒再加入六号溶剂油,进行第二次超声波辅助脱脂;最后压滤,风干,得到脱脂鱼鳔;
(2)明胶提取:将步骤(1)得到的脱脂鱼鳔放入热水,连续缓慢搅拌浸提;然后离心,取上清液,经喷雾干燥,得到白色粉末,即为鱼源明胶。
2.根据权利要求1所述的一种鱼源明胶的制备方法,其特征在于,步骤(1)中所述鱼鳔颗粒与工业酒精或六号溶剂油的用量比均为1kg:3~5L。
3.根据权利要求1所述的一种鱼源明胶的制备方法,其特征在于,步骤(1)中所述超声波辅助脱脂的条件均为:强度20~30W/L,时间6~12h,温度25~40℃;所述筛网的目数为7~12目。
4.根据权利要求1所述的一种鱼源明胶的制备方法,其特征在于,步骤(2)中所述脱脂鱼鳔与热水的用量比1kg:7~10L,所述热水的温度为50~55℃,所述浸提的时间为30~60min。
5.根据权利要求1所述的一种鱼源明胶的制备方法,其特征在于,步骤(2)中所述离心的条件为:离心力10000~20000g,时间30~60min;所述喷雾干燥的条件为:进气温度180~200℃,排气温度100~120℃。
6.根据权利要求1~5任一方法所制备的鱼源明胶生产纳米纤维膜的方法,其特征在于,具体步骤如下:
将所得鱼源明胶溶于乙酸-水溶液,进行静电纺丝于铝箔,得到纳米纤维;再将纳米纤维和戊二醛、硅胶独立放入同一真空干燥箱,通过抽真空和加热进行蒸汽交联,得到鱼源明胶纳米纤维膜。
7.根据权利要求6所述的方法,其特征在于,所述乙酸-水溶液的乙酸浓度为20~25%(v/v),所述明胶在乙酸-水溶液中的浓度25~30%(w/v)。
8.根据权利要求6所述的方法,其特征在于,所述静电纺丝的条件为:进料1~2μL/min,电压15~20kV,针头20~22号,针尖与收集器距离12~18cm,湿度30~50%;所述交联的条件为:温度50~60℃,时间1~3h,真空度-0.09~-0.08Mpa。
9.根据权利要求6所述的方法,其特征在于,所述纳米纤维、戊二醛和硅胶的用量比为1kg:5-7L:30-50kg。
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CN113279086A (zh) * | 2021-05-07 | 2021-08-20 | 东部湾(扬州)生物新材料有限公司 | 聚乳酸复合超短无卷曲纤维原丝制备方法 |
CN115262013A (zh) * | 2022-08-05 | 2022-11-01 | 海南大学 | 一种水产胶原蛋白纳米纤维及其溶液气纺制备方法 |
Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101708344A (zh) * | 2009-11-27 | 2010-05-19 | 天津大学 | 纳米纤维人工血管及制备方法 |
CN104060401A (zh) * | 2014-07-04 | 2014-09-24 | 东华大学 | 一种释放维生素a的明胶纳米纤维膜的静电纺制备方法 |
CN109517868A (zh) * | 2018-12-12 | 2019-03-26 | 江苏大学 | 一种延缓衰老的鱼源胶原蛋白肽的制备方法 |
-
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- 2020-10-21 CN CN202011142131.5A patent/CN112409933B/zh active Active
Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101708344A (zh) * | 2009-11-27 | 2010-05-19 | 天津大学 | 纳米纤维人工血管及制备方法 |
CN104060401A (zh) * | 2014-07-04 | 2014-09-24 | 东华大学 | 一种释放维生素a的明胶纳米纤维膜的静电纺制备方法 |
CN109517868A (zh) * | 2018-12-12 | 2019-03-26 | 江苏大学 | 一种延缓衰老的鱼源胶原蛋白肽的制备方法 |
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CN113279086A (zh) * | 2021-05-07 | 2021-08-20 | 东部湾(扬州)生物新材料有限公司 | 聚乳酸复合超短无卷曲纤维原丝制备方法 |
CN115262013A (zh) * | 2022-08-05 | 2022-11-01 | 海南大学 | 一种水产胶原蛋白纳米纤维及其溶液气纺制备方法 |
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