CN101631474A - 新型可缓慢消化的贮存碳水化合物 - Google Patents
新型可缓慢消化的贮存碳水化合物 Download PDFInfo
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Abstract
本发明涉及可缓慢消化的贮存碳水化合物(淀粉、糖原),其具有至少8.5%的支化度和包括至少10%的DP5~7的支链成分。所述可缓慢消化的碳水化合物可通过用糖原分支酶处理天然来源的底物(糖原、淀粉)来制造,所述糖原分支酶源自小浜红嗜热盐菌、海洋红嗜热盐菌、耐辐射异常球菌或地热异常球菌。
Description
技术领域
本发明涉及可缓慢消化的贮存碳水化合物的制备,更具体地涉及使用糖原分支酶的可缓慢消化的淀粉或糖原的制备。
背景技术
淀粉作为葡萄糖的聚合物,是人体内能量的主要来源之一。在消化过程中,在小肠内淀粉的葡萄糖转移到血液中,导致血液中的葡萄糖水平升高。作为对这种葡萄糖水平升高的反应,身体产生更大量的胰岛素来将葡萄糖作为糖原贮存在肝脏和肌肉中。
小肠中淀粉的消化特性分为三类:可快速消化的淀粉、可缓慢消化的淀粉和不消化的淀粉(抗性淀粉)。可快速消化的淀粉和可缓慢消化的淀粉通过所谓血糖反应,即葡萄糖释放到血液中的速度来区分。抗性淀粉在小肠中不消化,但在大肠中发酵。Englyst等给出了淀粉分类的详细概述(Englyst H.,Kingman S.M.,Cummings J.H.(1992),″Classification and measurement ofnutritionally important starch fractions″,Eur.J.Clin.Nutr.46:33-50)。
可快速消化的淀粉将葡萄糖快速释放到血液中。数种健康负面因素已归因于这种快速释放及随后的胰岛素水平的升高。对一些人群来说,具有快速血糖反应的饮食与II型糖尿病有关(Salmeron等,(1997)JAMA277:472-477)。另外,已将可快速消化的淀粉与肥胖的发生相关联。葡萄糖的快速释放及所导致的胰岛素快速增多使人饥饿并急于摄入更多的食物。结果,FAO/WHO的新报告提倡在高血脂和肥胖患者以及健康人群中选择缓慢反应的淀粉,尽管胰岛素反应也是重要方面。
对于鸟类,已表明可缓慢消化的淀粉改善了蛋白质和氨基酸的消化效率(Poultry world,2003年10月)。这对哺乳动物特别是人类是重要的,并且认为氨基酸的吸收增加会减轻进食不足的状况。
在运动饮料中,葡萄糖的释放是重要因素,尽管与健康不直接相关。关于称作的运动饮料的商业信息描述了将蛋白质水解产物用于葡萄糖聚合物以提高血糖反应。这种提高将增强运动体力之间的恢复。但是,为了准备要求长时间段体力的运动,希望葡萄糖缓慢释放,以给身体更长的时间来燃烧葡萄糖并防止在肌肉和肝脏内不必要的贮存葡萄糖。
一些淀粉天然就含有比其他淀粉更高比例的可缓慢消化的淀粉。一种此类淀粉是来自剪股草属埃塞俄比亚画眉草(Agrostis teff),一种埃塞俄比亚谷物的淀粉,这种谷物被制成许多埃塞俄比亚人的食物,因此被认为对埃塞俄比亚运动员马拉松赛跑成绩有贡献(www.sporteff.nl)。
US 2003/0005922中说明了随着淀粉支化度增大,消化性降低,尽管这类产品之前已在EP-A-0418945中说明。因此,在US 2005/0159329中为了制备具有所需性能的产品引入了额外的酶促β-淀粉酶步骤。其它专利文件也说明了将分支酶用于将淀粉转变成具有较低粘度的稳定非凝胶产物。在US2004/0014961中,这是通过用来自脂肪嗜热芽孢杆菌(B.stearothermophilus)的分支酶或胰淀粉酶处理淀粉并将所得产物分级来实现。在US2002/0065410、JP 2001/031574和DE 10237442中,将淀粉酶(α-淀粉酶、β-淀粉酶或两者)用于获得高支化淀粉。在WO 00/22140中,已说明了提供高支化淀粉的来自奈瑟球菌属(Neisseria)的新的酶。但是,这些专利申请中没有一个说明这些淀粉的支链成分和α-极限糊精含量的作用及它们对消化性的影响。
发明内容
本发明涉及一种新的可缓慢消化的贮存碳水化合物,具有至少8.5~9%的支化度,优选至少10%,更优选至少11%。所述可缓慢消化的贮存碳水化合物优选具有约60~约150kD的分子量。此外,优选所述贮存碳水化合物能被人类或动物肠道酶水解,相同条件下其水解速度不大于麦芽糖水解速度的0.9倍,优选0.1~0.9倍之间,更优选0.3~0.7倍之间。
本发明的一部分还提供一种通过用分支酶处理天然来源的贮存碳水化合物制造可缓慢消化的贮存碳水化合物的方法,所述可缓慢消化的贮存碳水化合物具有至少9%、优选至少10%、更优选至少11%和最优选至少12%的支化度,即α-1,6糖苷键的量。所述酶优选为具有E.C.2.4.1.18所述活性并源自微生物的酶,所述微生物优选来自红嗜热盐菌属和/或异常球菌属或异常球菌-栖热菌类,更优选从由小浜红嗜热盐菌(RhodoThermus obamensis)、海洋红嗜热盐菌(Rhodothermus marinus)、耐辐射异常球菌(Deinococcusradiodurans)或地热异常球菌(Deinococcus geothermalis)构成的组中选择的微生物。
此外,在所述方法中,所述天然来源是指含有贮存碳水化合物的植物材料,即包含淀粉的植物材料,优选根或块茎,更优选马铃薯块茎。
优选地,所述来自天然来源的淀粉至少包括90%的支链淀粉。
本发明另一个实施方式是用上述方法制备的可缓慢消化的贮存碳水化合物。
本发明又一部分是这种可缓慢消化的贮存碳水化合物作为食品或喂养产品的应用,特别用于糖尿病人食品、婴儿食品、特殊的膳食配方和/或运动食品和饮料。优选地,该可缓慢消化的贮存碳水化合物以至少10wt%的量加入所述食品、喂养产品或饮料中。
附图说明
图1的曲线图表示了与来自马铃薯的支链淀粉相比,通过用来自5种不同细菌源的酶处理得到的淀粉的支链分布(即支链中的葡萄糖残基数量)。“R.H 9.6”是小浜红嗜热盐菌,“APEC AARD”是高支链淀粉(不含直链淀粉)马铃薯淀粉。
图2表示了用于支化淀粉制备的流程图。具体细节参见下文。
具体实施方式
微生物和动物(包括人类)中含有分支酶,也称作糖原分支酶(由glgB基因编码)。它在糖原中产生α-1,6-糖苷键,从而由葡萄糖基的正常α-1,4-糖苷键结合的品种形成支链,这构成了糖原的“骨架”。相似的酶存在于植物中,例如淀粉分支酶,该酶起到相同的作用(在支链淀粉(淀粉的两种葡萄糖聚合物中的一种)中形成α-1,6-糖苷键)。但是,已表明糖原分支酶能将淀粉用作它们酶活性的底物。
适应于本发明中的底物的淀粉包括从源自任何天然来源的所有淀粉。此处所用的天然淀粉定义为自然界中发现的淀粉。其它适宜的淀粉源自于通过杂交育种、易位、倒位、转化或任何其它遗传或染色体工程的方法以改变天然淀粉的植物。与淀粉相近,糖原也可用作底物,且表明了糖原也可被本发明的酶转变成可缓慢消化的糖原。在本申请中,淀粉和糖原都将称作“贮存碳水化合物”。
常规的淀粉来源是谷类、植物的块茎、根和果实。这些淀粉通常含有直链淀粉和支链淀粉的混合物。这些来源还可以是更多普通来源的所谓“蜡样”变体,其中“蜡样”是指植物产生包含少于10%直链淀粉的淀粉;这些淀粉还被指定为“支链淀粉”。优选蜡样淀粉,因为他们通常已包含比非蜡样淀粉更高的支化度(约4%)。但是,具有高含量直链淀粉的淀粉也能利用本发明,因为预期它们用分支酶改性后更稳定,且它们的加工将更容易。
糖原的常规来源是各种动物,包括哺乳动物的肌肉和肝脏(不那么常见的还有肾和脾),同时诸如细菌、真菌和酵母菌等微生物也能形成糖原的来源。
由于支链淀粉支化增加,它具有与麦芽糖相当的离体消化速度(即麦芽糖消化速度的0.9~1.0倍之间)。这种消化作用根据所谓Englyst法(Englyst,H.N.等,1992,Eur.J.Clin.Nutr.46:33-50)在试管分析中测定,或在离体肠道模拟系统中测定(TIM-1,Minekus,M.等,1995,Alt.Lab.Animals23:197-209)。发现的支链淀粉的消化速度还通过用源自细菌超嗜热菌(Vander Maarel等,2003,Biocat.Biotransform.21:199-207)和脂肪嗜热芽孢杆菌(Takata H.等,1994,Appl.Environ.Microbiol.60-3096-3104)的分支酶处理天然淀粉得到。从用来自这些细菌的酶处理得到的淀粉分析可知它们具有约5~7%的支化度。此外,在这些分子中制得的支链尺寸较大(中值DP-聚合度-每个支链约9~15个葡萄糖基)。
目前表明用来自另一种来源的分支酶,可能得到大于8.5%的支化度。这种增加的支化对贮存碳水化合物的消化性具有有利影响,如以下实验部分所示。进一步表明,聚合度(即支链的链长)较低的区域在增加,且淀粉含有至少10%的侧链的链长为5~7个葡萄糖基(DP 5~7),优选至少15%为DP 5~7,更优选至少20%为DP5~7,同时链长的中值已降至约6~12个葡萄糖基的中值,同时由耐辐射变异球菌的酶制得的淀粉具有约6~7个葡萄糖基的中等链长。后一种淀粉的特征为不仅具有非常高的支化度(11~12%),而且还具有非常低的淀粉分子分子量,在约60kDa的数量级。
特别适用于本发明的酶是来自微生物的酶,其中微生物属于红嗜热盐菌科和异常球菌科或异常球菌-栖热菌类,更优选选自由小浜红嗜热盐菌、海洋红嗜热盐菌、耐辐射异常球菌或地热异常球菌构成的组中的微生物。
此外,本发明还涵盖了仍保留形成α-1,6-糖苷键功能的上述那些酶的同源酶。
在此意义上,同源是指同源酶具有与上述酶大于70%的序列同源性的氨基酸序列,优选大于80%,更优选大于90%,最优选大于95%的序列同源性。
为了计算同一性(或同源性)百分比,可使用采用默认参数的BLAST运算法则(Altschul等,1997 Nucl.Acids Res.25:3389-3402),或,选择采用默认参数的GAP运算法则(Needleman and Wunsch,1970 J.Mol.Biol.48:443-453),它们两者都包含在维斯康星遗传软件包(Genetics ComputerGroup(GCG),575 Science,麦迪逊,威斯康星州,美国)中。BLAST搜索假定可将蛋白质模拟为随机序列。但是,许多实际的蛋白质包括非随机序列区域,这些非随机区域可能是富含一个或多个氨基酸的均聚物序列、短重复序列或区域。这种复杂度低的区域可在无关的蛋白质之间比对,即使蛋白质的其它区域完全不同。可使用一些低复杂度滤过程序来减少这种低复杂度比对。例如,可单独使用或组合使用SEG(Wooten和Federhen,1993 Comput.Chem.17:149-163)和XNU(Claverie和States,1993 Comput.Chem.17:191-201)低复杂度滤过程序。
如此处所用,上下文中两种蛋白质序列(或核苷酸序列)的“序列同一性”或“同一性”或“同源性”是指两种序列中的残基,它们在特定对比范围内最大对应来比对时是相同的。当使用关于蛋白质的序列同一性百分比时,认为不相同的残基位置通常因保守氨基酸取代基而不同,其中氨基酸被取代为其他具有相似化学性能(例如电荷或疏水性)的氨基酸残基,因而不改变分子的功能性性质。如果序列在保守取代基上不同,可上调序列同一性百分比以校正取代基的保守性质。在这种保留取代基上不同的序列称为具有“序列相似性”或“相似性”。进行这些调整的手段是本领域技术人员公知的。通常,这包括将保守取代基作为部分错配而不是全部错配来评分,从而提高序列同一性百分比。因此,例如,如果相同的氨基酸给出1分,而非保守取代基给出0分,保守取代基给出0~1之间的分。例如根据Meyers和Miller(Computer Applic.Biol.Sci.4:11-17,1988)算法计算保留取代基的分值。
特别优选的是如上定义的同源酶,它们具有增强的热稳定性,即对高温的耐受性增强和/或最适温度增高。
属于糖苷水解酶族13的分支酶(参见http://afmb.cnrs-mrs.fr/CAZY /fam/GH13.html)具有四个保守区域,一些分析必需的保守残基位于其中(参见van der Maarel等,2002,J.Biotechnology 94:137-155)。族GH13与糖苷水解酶族70和77一起形成所谓的α-淀粉酶族,其中所有酶都共用这些保守结构域。由几个最近的出版物已知这些保守区域和它们直接相邻区域中的变异对酶活性、特异性和形成在由这些酶制得产品中的糖苷键有显著影响。Leemhuis等(Biochemistry,2004,43:13204-13213)表明在游动放线菌SE50/110的acerviosyl转移酶中,当将存在于保守区域1中的G104转变成H时,该酶变成葡聚糖转移酶类似酶。这种突变还引入了环糊精形成活性。另一个实例为在路氏乳杆菌121的reuteransucrase中与催化的Asp紧邻的区域4中引入的突变将这种酶转变成葡聚糖蔗糖酶(通过该突变制得产品中的1,6-糖苷键的量为85%,而野生型酶制得含有约50%1,6-糖苷键的产品)(Kralj等,Biochemistry 2005,44,9206-9216)。
使用分支酶的酶解处理用技术人员公知的技术进行。酶的用量取决于酶来源、淀粉来源以及诸如pH和温度等工艺参数的活性。通常使用50~400U/g的干重量。一个单位(U)定义为使直链淀粉-碘化物复合物在660nm处每分钟的吸收值减少1%的酶用量。关于pH和温度,用于现有技术领域和本发明中的酶具有各种优化的值。对于淀粉酶解处理的工业应用,优选使用在60℃以上或更高温度下具有活性,或者至少能在较高温度下存活的酶或其突变体。通常,导致温度稳定性提高的突变是那些使邻近氨基酸残基之间的相互作用量增大的突变(氢键、范德华相互作用、静电相互作用、疏水相互作用)或者是包含形成硫桥的硫侧基的一个或两个氨基酸(诸如半胱氨酸)的具体引入(参见ao.J.Fitter,2005.Structural and dynamical featurescontributing to thermostability in alpha-amylases,Cell Mol Life Sci,62:1925-1937;Kim YW等,2003,Directed evolution of Thermusmaltogenicamylase toward enhanced thermal resistance.Appl.Environ.Microbiol.69:4866-4874)。
在以下表1中,列出了所得淀粉的支化百分比、分子量和几种分支酶的最适宜温度,而表6和图1示出了用所述分支酶处理的淀粉的支链聚合度的分布曲线。
酶解处理可通过加热淀粉淤浆或通过喷射蒸煮预先胶凝或不用预先胶凝来进行。使用胶凝的方法对本领域技术人员是公知的,例如在“J.L.Doublier.Rheological studies on starch.Flow behaviour of wheat starch pastes.Starch/33(1981)415-420;P.De Meuter,J.Amelrijckx,H.Rahier,B.Van Mele”中所述。浓缩的无定形淀粉体系的等温结晶作用通过调制式差示扫描量热法测定(J.Polym.Sci.:Part B:Polym.Phys.,37(1999)2881-2891)。
表1.与蜡样和正常马铃薯淀粉相比的不同支化产物的支化度。支化度通过用异淀粉酶或通过用异淀粉酶和支链淀粉酶的组合用于水解1,6-糖苷键来测定。应注意当使用异淀粉酶/支链淀粉酶组合时,耐辐射异常球菌支化产物的支化度增加。
酶来源 | 支化度%(只用异淀粉酶) | 支化度%(使用异淀粉酶/支链淀粉酶) | Mw(kDa) | 优化的温度(℃) |
超耐热菌 | 6.3 | nd | 125 | 80 |
脂肪嗜热芽杆菌 | 6.4 | nd | 146 | 55 |
海洋红嗜热盐菌 | 9.5 | 9.5 | 135 | 65 |
地热异常球菌 | 8.5 | 8.8 | 96 | 37* |
耐辐射异常球菌 | 10 | 11.5 | 62 | 37* |
蜡样马铃薯淀粉 | 3.9 | 未测出 | ||
正常马铃薯淀粉 | 3.1 | 3.2 | ||
酵母菌 | 4.5 | 未测出 | 1000 | 37 |
*在55℃时有活性
nd=未检测
糊化使淀粉溶解,从而使它更容易接近酶。或者,淀粉可如“C.Mercier,P.Feillet.Medification of carbohydrate components by extrusion-cooking ofcereal products.Cereal Chem.,52(1975)283-297”中所述,在挤出机工艺中用酶加工;如“R.J.Nicholls,I.A.M.Appelqvist,A.P.Davies,S.J.Ingman,P.J.Lillford.Glass transition and fracture behaviour of gluten and starches within theglassy state.J.Cereal Sci.,21(1995)25-36”中所述在加热的低湿粉末中用酶加工;中或通过转鼓式干燥来加工(P.Colonna,J.L.Doublier,J.P.Melcion,F.de Monredon,C.Mercier.Extrusion cooking and drum drying of wheat starch.I.Physical and macromolecular modifications.Cereal Chem.,61(1984)538-543)。优选地,酶促转化在可能达到最大干燥固体竞争的条件下进行。这种转化的常规温度为10~90℃之间,特别是在50~80℃之间。通常,调节反应进行的pH为3.0~6.0之间。这些转化符合渐近时间曲线,且在所有淀粉基本转化之前,反应可具有长持续时间。但是,为了有效转化,约1~36小时,更优选2~24小时的反应时间就足够了。可选择地,在完成转化之后,可用本领域公知技术灭活用于转化的酶,诸如将pH降至低于pH3.0或通过例如喷射蒸煮升高温度。
在酶转化和可选择地灭活后,通过挤出或喷雾干燥、急骤干燥、空气干燥、冷冻干燥、真空干燥、传送带干燥、转鼓式干燥或本领域中用于干燥淀粉的任何其他公知的方法来分离淀粉。优选地,通过喷雾干燥来分离淀粉。转化程度通常由右旋糖当量(DE)来计量,其大致为淀粉中已断裂的糖苷键的部分。用这种方法制得的食品包括:
●麦芽糖糊精,轻度水解(DE 10-20)的淀粉产品,用作温和味道填料和增稠剂;
●多种玉米糖浆(DE 30~70),用作多种加工食品中的增甜剂和增稠剂的粘溶液;
●右旋糖(DE 100),商用萄萄糖,由淀粉完全水解制得;
●高果糖糖浆,通过用葡萄糖异构酶处理右旋糖溶液,直至葡萄糖基本被转化成果糖制得。在美国,高果糖玉米糖浆是甜饮料中所用的主要增甜剂,因为果糖味道比葡萄糖更甜,所以可以使用较少的增甜剂。
所得淀粉特征为DE小于3。图2为淀粉酶解处理的常规处理原理的流程图。开始通过约20%干重淀粉的淤浆(优选从喷射式蒸煮锅(140℃ 5秒)穿过的去硬化水中的马铃薯淀粉)形成。然后,加入酶并在适宜条件(pH、温度)下进行反应达充足的时间。优选高温(例如50℃~70℃之间),因为这抑制微生物污染物开始生长。反应后,将改性淀粉溶液通过喷射式蒸煮锅(130℃5秒)以使酶灭活,在缓冲罐中收集材料。最后,将改性淀粉喷雾干燥。
制得的改性淀粉可理想地用作食品和喂养应用中的可缓慢消化的淀粉。现今,淀粉用于许多食品和喂养应用中,例如作为主食复合物,作为用于面包店产品(面包、蛋糕、饼干、点心、糖块等)制造及用于乳制品(乳酪、布丁等)、汤和沙司的制造的粘结剂、填料、增粘剂或胶凝剂。
含有较短支链的高支化贮存碳水化合物的另一个优点是降低的粘度以及凝胶形成性能。在制备上述食品和喂养产品的工艺中,以及也使用淀粉的非食品工艺中,诸如纺织工业(用于纺纱过程中使纱增强)、造纸工业,以及用于纸涂层,在这些工艺中经常使用中间产物的加热和冷却,包括涂布的淀粉,已知的是现有技术的淀粉酶分子和淀粉的支链淀粉的长侧链相互作用,从而形成不可逆凝胶。现有技术的淀粉的性能导致在这种工艺中的适用性降低。本发明的高支化贮存碳水化合物未表现出这些相互作用,或只最低限度地表现这些相互作用,从而将导致不可逆凝胶形成更少,由此导致这些淀粉在上述工艺中的适用性增大。
实施例
本专利申请中所述酶的基因序列及其相应的氨基酸序列可在美国国立生物信息中心(NCBI)蛋白质数据库中找到(http://www.ncbi.nlm.nih.gov/ entrez/query.fcgi?CMD=search&DB=protein)。氨基酸序列具有以下入藏登记号:
小浜红嗜热盐菌:NCBI入藏登记号Q93HU3
地热异常球菌:NCBI入藏登记号ABF45281(Q1IZQ3)
耐辐射异常球菌:NCBI入藏登记号AE000513(Q9RTB7)
脂肪嗜热芽杆菌:NCBI入藏登记号AAA22482(P30538)。
基于以上给出的序列信息,本领域技术人员能得到编码这些酶的DNA并将该DNA用于异源表达系统中。还可能将酶从上述微生物的培养菌中分离。
超嗜热菌基因的克隆已在van der Maarel等的“Biocatalysis andBiotransformation,2003,21:199-207”中说明。
实施例1
改性淀粉的生产
由常规食品级马铃薯淀粉和蜡样马铃薯淀粉,通过在68℃下每克淀粉与400U的分支酶活性共孵育20小时来制得最大支化产物。淀粉浆通过将淀粉悬浮于每升包含0.2883g CaCl2·2H2O的软化水中并在100℃的水浴中边搅拌边加热20分钟制得;随后将所得淀粉溶液在121℃压煮20分钟。将底物冷却到所需孵育温度后加入分支酶。20小时后,通过将培养混合物加热至100℃停止反应。随后,支化葡聚糖用乙醇沉淀然后干燥得到。加入乙醇至90%的最终浓度,然后缓和混合乙醇/淀粉悬浮液50分钟。然后将改性淀粉在滤纸上过滤。保留在滤纸上的材料用100%乙醇洗涤并接着悬浮在100%的乙醇中。然后再将所得淀粉过滤并在37℃干燥。
由超嗜热菌酶制得的支化葡聚糖具有5.3%的平均支化度,同时由小浜红嗜热盐菌酶制得的产物具有9.5%的支化度。
酶活性分析
分支酶活性量通过测定碘/碘化物/直链淀粉复合物因分支酶反应而在640nm处的吸收值变化来判定。测试程序如下:
在适宜温度(超嗜热菌80℃,小浜红嗜热盐菌60℃)下,将150μl的0.125%直链淀粉溶液(Sigma A0512,III型,马铃薯)与50μl在适宜稀释剂(10~15U/ml)中的酶共孵育15分钟。使用未加入酶的直链淀粉溶液作为参照。在冰上简单冷却样品(1~3秒)且涡流后将它们置于室温中。取出15μl样品并将其与150μl碘溶液(每升中940g CaCl2,1g KI,0.1g I2)在聚氯乙烯微量滴定板(ICN)中混合。5~10分钟后,测定640nm处的消光度。由吸收的降低,根据以下公式计算酶活性:
活性=以U为单位的活性/ml酶
A=吸收/消光
ΔAbep=A直链淀粉-Abep
V=体积(ml)
V总=V酶+V底物
VF=酶稀释因子
支化度分析
支化度通过用酶异淀粉酶去支化后测定形成的还原端基量来分析。
分析进行如下:将100mg样品与10ml软化水混合,然后将该混合物在100℃的炉中加热1小时,同时通过转动混合。在将其冷却至35℃后等待15分钟,用1M乙酸调节pH至4.5。然后加入0.875U异淀粉酶溶液(Megazyme,威克洛,爱尔兰)并接着在35℃孵育20小时。通过将反应混合物沸腾2分钟来停止反应,将样品在3600rpm离心分离(MSE离心机)30分钟。用Nelson-Somogyi测定法测定上层清液中的还原糖量(G.Spiro:Analysis ofsugars found in glycoproteins,in Methods Enzymol.8(Ed.E.F.Neufeld,V.Ginsburg)Academic Press,1966)。
支链组成
支化葡聚糖的支链组成通过用异淀粉酶去支化接着用HPLC分析低聚糖来测定。
支化葡聚糖通过添加微生物去分支酶异淀粉酶去支化。将待分析样品的pH用1M乙酸调节至4.5,加入0.875U异淀粉酶溶液(Megazyme)接着在40℃孵育1小时。反应通过将反应混合物沸腾2分钟来终止。在HPLC分析之前,将样品在80%DMSO中稀释五倍,在90℃加热120分钟,同时旋转混合以得到澄清溶液并随后用0.45μm Millex过滤器(Millipore,Billerica,摩洛哥,美国)过滤。然后直链低聚糖用装有20μl注射环、CarboPac Pa-1保护柱和Pa-1柱、四元梯度泵、使用氦气的洗脱液脱气装置和含有黄金电极的脉冲电流检测器的含有脉冲电流检测器的高效离子交换色谱(HPAEC-PAD;Dionex,Sunnyvale,加利福尼亚,美国)分析。电极电势编程如下:0~0.4秒0.1V,然后0.41~0.61秒0.7V,最后0.61~1.00秒0.1V;0.2~0.4秒集成信号。
Englyst测定
用Englyst分析法(Englyst,H.N.,Kingman,S.M.,and J.H.Cummings.1992.Classification and measurement of nutritionally important starch fractions.Eur.J.Clin.Nutr.46:33-50),可估定快速降解淀粉和缓慢降解淀粉的量。在试管中模拟人体胃部和小肠,通过将样品与胰酶、转化酶和淀粉葡萄糖苷酶(amyloglucosidase)的混合物共孵育,测定20分钟(快速降解淀粉,RDS)和120分钟(缓慢降解淀粉,SDS)后转化产物的量。同时,测定作为由α-淀粉酶和AMG得到的葡萄糖量的淀粉总量(TG)。由淀粉总量与降解淀粉量之差计算抗性淀粉量。就高支化葡聚糖而言,淀粉葡萄糖苷酶的使用(水解支化点)对分析有不利影响。因此,将Englyst法作轻微修改:在孵育混合物中省去淀粉葡萄糖苷酶和转化酶,并改变转化淀粉量的分析。已转化的淀粉量定义为制得的至多麦芽五糖的麦芽低聚糖(maltooliogosaccharide)总量。对所用Englyst法的第二改变为在其中使用更低剂量的胰酶及更多的样品。所有样品用GOPOD法通过离子交换HPLC(不检测支化产物)以及通过HPAEC-PAD(检测直链和支链产物)进行葡萄糖分析。
分析
制备“像被吃过一样的”样品。这通过将5ml水加入0.6g淀粉中,将其在100℃加热10分钟,并冷却至37℃来进行。在该溶液中加入10ml阿拉伯糖/胃蛋白酶/瓜尔溶液(20g/L的阿拉伯糖在25%的含有0.05M氯化钠的饱和硼酸中的溶液,其中加入有5g/L胃蛋白酶[Sigma no P-7000]和瓜尔胶[Sigma no G-4129])并将该溶液在37℃孵育30分钟。加入5ml乙酸钠(0.5M)和5个玻璃球后,将整个悬浮液缓和混合并置于37℃平衡。然后在试管中将5ml酶溶液(3g胰酶[Sigma npo P-7545]加入120ml超纯水中,混合均匀并以1500×g离心,然后将4ml淀粉葡萄糖苷酶[Novozyme的AMG 400L LP型]和6ml转化酶[Merck no 390203D]加入到90ml上层清液中)加入试管中的悬浮液中,然后在37℃将其水平置于震荡水浴中同时以100rpm混合。每20分钟,从各个试管取出0.2ml样品然后将其加入4ml无水乙醇中。孵育结束时,将这些试管彻底混合以分离所有颗粒,然后将它们置于装有沸水的水浴中30分钟。短暂混合后,将这些试管置于冰水上15分钟。将10ml氢氧化钾(7M)加入这些试管中,然后将该溶液在冰水中孵育30分钟,同时以100rpm混合。
从各个试管中取出0.2ml样品,并加入1 ml乙酸(1M)和40μl淀粉葡萄糖苷酶溶液(1∶7稀释的Novozyme的AMG400L LP型)。将该样品在70℃孵育30分钟然后置于沸水中10分钟。然后将这些试管在冰水中冷却至室温并在各个试管中加入1 2ml无水乙醇。后一种样品中的葡萄糖量表示上述酶孵育后剩下的葡萄糖总量。
各样品中的葡萄糖量测定如下:将样品在1500×g下第一离心分离5分钟,根据生产商说明将葡萄糖作为标准,葡萄糖量用GOPOD测定法(Megazyme,K-Gluc)在上层清液中测定。
结果
支化产物
由小浜红嗜热盐菌和超嗜热菌酶制得的支化葡聚糖产物分别具有9~9.5%和5.3~5.5%的支化度。这些支化葡聚糖的支链分布表明了至多DP30范围内的差异。特别表明小浜红嗜热盐菌产物比超嗜热菌产物具有更多较短支链(参见表6和图1)。
消化性
对超嗜热菌产物(5.3%支化)和小浜红嗜热盐菌产物(9.5%支化)进行详细的Englyst分析。在120分钟的时间区间内,每20分钟取出样品并测定游离葡萄糖量。其结果示于表2中。这些结果表明在第一个20分钟内用作10%干固体悬浮物的约90%的小浜红嗜热盐菌产物转变成葡萄糖。超嗜热菌产物一定程度上降解更快(在第一个20分钟内95%)。40分钟后两种产物几乎完全降解。在第一个20分钟内,麦芽糖完全转化为葡萄糖。在第一个20分钟内,蜡样马铃薯淀粉样品转化了96%,并在40分钟后完全降解。当将小浜红嗜热盐菌产物用作50%干固体溶液时,在第一个20分钟内只有67%降解。120分钟后,这些产物也完全降解。
由表3可看出,80%降解了的小浜红嗜热盐菌作为短低聚糖回收。对于超嗜热菌产物和蜡样马铃薯淀粉,约90%降解了的材料作为短低聚糖回收。只有80%已转化的小浜红嗜热盐菌材料作为至多DP5的低聚糖回收,而对于超嗜热菌产物和蜡样马铃薯淀粉,94%~97%可回收。这些结果表明要求相对较高的支化度来获得更少的降解。基于这些观察,初步结论为需要大于9%的支化度以提供更低的降解性。
另外,在通过α-淀粉酶的淀粉消化之后,紧接着麦芽糖和麦芽三糖之后形成所谓α极限糊精(参见Beers等,1995,Crit.Rev.Biochem.Mol.Biol.30:197-262)。支化产物的α极限糊精含量可从表3得出。在该表中,DP 1~3的形成作为总碳水化合物的百分比给出。HPLC分析显示了DP4或更高的低聚糖都是非直链的,暗示它们都包含至少一个α-(1,6)-葡萄糖支化点,因此为α极限糊精。因此,α极限糊精等于100%减去DP 1~3含量,这得到了对于Paselli SA2(它近似模仿了未改性淀粉)20%的α极限糊精含量以及对于超嗜热菌、小浜红嗜热盐菌和耐辐射异常球菌分别为36%、43%和58%。因此,本发明的淀粉还可定义为可缓慢消化的贮存碳水化合物,具有至少8.5~9%的支化度,优选至少10%,更优选至少11%,以及至少35%的α极限糊精,优选至少40%,更优选至少45%,且最优选至少50%。
表2.不同类型支化葡聚糖及一些具有及时制得的游离葡萄糖量的参照产物的标准Englyst分析结果。
表3.与参照产品(Paselli SA2)相比,用不同微生物分支酶制得的支化产品的离体消化结果。离体测定法是基于Englyst等说明的方法(如上),但改变所加酶合剂的量。按时形成的小低聚糖量用所述用于支链组成的Dionex HPLC法测定。
表4.用不同测定法在多种淀粉中检测支化%
注:普通正常马铃薯淀粉来自AVEBE,批号40389。
表6.支链分布
DP | 马铃薯淀粉 | RH 9.6 | 地热异常球菌 | 耐辐射异常球菌** | 超嗜热菌 | 脂肪嗜热芽孢杆菌 | 产果胶酶 |
1 | 0 | 0 | 0 | 0 | 0 | 0 | 0 |
2 | 0 | 0 | 0 | 0 | 0 | 0 | 0 |
3 | 0 | 0.1 | 0 | 0.2 | 0 | 0.1 | 0 |
4 | 0 | 1.2 | 0.2 | 1.1 | 0.1 | 0.2 | 0 |
5 | 0 | 3.8 | 0.9 | 4.9 | 0.2 | 0.4 | 0.1 |
6 | 0.6 | 6.5 | 5.3 | 12 | 1.2 | 3 | 2.3 |
7 | 0.5 | 4.8 | 8.3 | 10.7 | 1.1 | 3.7 | 2 |
8 | 0.3 | 8.6 | 7.6 | 8.8 | 2.2 | 2.7 | 1 |
9 | 0.6 | 9.5 | 8.1 | 6.9 | 5.9 | 2.8 | 1.2 |
10 | 1.2 | 10 | 10 | 5.3 | 6.7 | 4.5 | 1.7 |
11 | 1.9 | 8.1 | 8.7 | 3.8 | 6.7 | 7.7 | 2.4 |
12 | 2.4 | 6.2 | 6.9 | 2.7 | 6.5 | 7.1 | 2.7 |
13 | 2.7 | 4.7 | 5.1 | 1.8 | 6 | 5.6 | 2.9 |
14 | 2.9 | 3.5 | 4.2 | 1.4 | 5.9 | 5.5 | 3.4 |
15 | 2.8 | 2.8 | 3 | 0.9 | 5.2 | 4.7 | 3.1 |
16 | 2.7 | 2.4 | 2.5 | 1.3 | 4.8 | 3.9 | 3.1 |
17 | 2.7 | 2.3 | 2.2 | 1.1 | 4.2 | 2.9 | 3 |
18 | 2.6 | 2.2 | 1.9 | 0.9 | 3.6 | 2.5 | 2.8 |
19 | 2.5 | 2 | 1.6 | 0.9 | 3.2 | 2.2 | 2.5 |
20 | 2.4 | 1.7 | 1.4 | 0.6 | 2.9 | 2 | 2.3 |
21 | 2.3 | 1.5 | 1.2 | 0.3 | 2.7 | 1.9 | 2.2 |
22 | 2.2 | 1.5 | 1.1 | 0.4 | 2.6 | 1.9 | 2 |
23 | 2 | 1.2 | 1.1 | 0.5 | 2.8 | 1.7 | 1.8 |
24 | 1.8 | 1.2 | 0.9 | 0.5 | 2.3 | 1.5 | 1.5 |
25 | 1.5 | 1.1 | 1.3 | 0.3 | 2.2 | 1.5 | 1.4 |
26 | 1.5 | 1 | 0.8 | 0.5 | 2.2 | 1.4 | 1.3 |
27 | 1.3 | 0.8 | 0.7 | 0.2 | 1.9 | 1.2 | 1.2 |
28 | 1.2 | 0.7 | 0.6 | 0.2 | 1.6 | 1.1 | 1 |
29 | 1.1 | 0.6 | 0.5 | 0.1 | 1.5 | 0.9 | 0.9 |
30 | 0.9 | 0.5 | 0.4 | 0.1 | 1.3 | 0.8 | 0.8 |
31 | 0.8 | 0.4 | 0.3 | 0.2 | 1.2 | 0.7 | 0.8 |
32 | 0.8 | 0.4 | 0.3 | 0 | 1.1 | 0.6 | 0.7 |
33 | 0.7 | 0.3 | 0.2 | 0 | 1 | 0.6 | 0.7 |
34 | 0.7 | 0.3 | 0.2 | 0 | 0.9 | 0.5 | 0.7 |
35 | 0.7 | 0.2 | 0.1 | 0 | 0.8 | 0.5 | 0.7 |
36 | 0.6 | 0.2 | 0.1 | 0 | 0.7 | 0.4 | 0.7 |
37 | 0.6 | 0.1 | 0.1 | 0 | 0.6 | 0.4 | 0.7 |
38 | 0.7 | 0.1 | 0 | 0 | 0.6 | 0.4 | 0.7 |
39 | 0.7 | 0.1 | 0 | 0 | 0.6 | 0.4 | 0.8 |
40 | 0.7 | 0.1 | 0 | 0 | 0.5 | 0.3 | 0.8 |
dp33-40 | 5.8 | 1.7 | 1 | 0 | 5.9 | 3.8 | 5.8 |
>dp40 | 14.1 | 0.6 | 0 | 0 | 3.5 | 2.8 | 14.1 |
Claims (11)
1、一种可缓慢消化的贮存碳水化合物,具有至少8.5~9%,优选至少10%,更优选至少11%的支化度,且具有包括至少10%,优选至少15%且更优选至少20%的DP5~7的支链成分。
2、根据权利要求1所述的可缓慢消化的贮存碳水化合物,其特征为具有约60~约150kD的分子量。
3、根据权利要求1或2所述的可缓慢消化的贮存碳水化合物,其中所述贮存碳水化合物可被人体或动物肠道酶水解,所述水解速度不大于相同条件下麦芽糖水解速度的0.9倍,优选0.1~0.9倍之间,更优选0.3~0.7倍之间。
4、一种制造可缓慢消化的贮存碳水化合物的方法,通过用分支酶处理天然来源的贮存碳水化合物,所述可缓慢消化的贮存碳水化合物具有至少9%,优选至少10,更优选至少11%的支化度,且具有包括至少10%,优选至少15%,更优选至少20%的DP5~7支链成分。
5、根据权利要求4所述的方法,其中所述分支酶是源自微生物的酶,优选是具有E.C.2.4.1.18所述活性的酶,优选是源自红嗜热盐菌和/或异常球菌科或异常球菌-栖热菌类的微生物的酶或它们的任何同源或突变体酶,更优选是源自选自由小浜红嗜热盐菌、海洋红嗜热盐菌、耐辐射异常球菌或地热异常球菌组成的组中的微生物的酶或它们任何同源或突变体酶,最优选是耐辐射异常球菌或小浜红嗜热盐菌,或源自耐辐射异常球菌或小浜红嗜热盐菌的酶。
6、根据权利要求4或5所述的方法,其中所述天然来源为含淀粉的植物材料,优选根或块茎,更优选马铃薯块茎。
7、根据权利要求3~5中任意一项所述的方法,其中所述天然来源的贮存碳水化合物至少包括90%的支链淀粉。
8、由根据权利要求4~7中任意一项所述方法制备的可缓慢消化的贮存碳水化合物。
9、根据权利要求1~3或权利要求8所述的可缓慢消化的贮存碳水化合物作为食品或喂养产品的应用,优选用于糖尿病人食品、婴儿食品,特殊的膳食配方和/或运动食品和饮料。
10、根据权利要求9所述的应用,其特征是所述可缓慢消化的贮存碳水化合物以至少10wt%的量加入到所述食品、喂养产品或饮料中。
11、源自微生物的糖原分支酶在制备可缓慢消化的贮存碳水化合物中的应用,其所述可缓慢消化的贮存碳水化合物具有至少8.5~9%,优选至少10%,更优选至少11%的支化度,且具有包括至少10%、优选至少15%、最优选至少20%的DP5~7的支链成分;所述酶为源自选自由红嗜热盐菌和/或异常球菌科或异常球菌-栖热菌类构成的组中的微生物的酶,更优选为源自选自由小浜红嗜热盐菌、海洋红嗜热盐菌、耐辐射异常球菌或地热异常球菌构成的组中的微生物的酶,或所述酶的具有糖原分支活性的任何同源或突变体酶。
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ATE455173T1 (de) * | 1998-10-09 | 2010-01-15 | Bayer Bioscience Gmbh | Nucleinsäuremoleküle codierend ein verzweigungsenzym aus bakterien der gattung neisseria sowie verfahren zur herstellung von alpha-1,6-verzweigten alpha-1,4-glucanen |
FR2792941B1 (fr) * | 1999-04-30 | 2001-07-27 | Roquette Freres | Polymeres solubles de glucose branches et leur procede d'obtention |
JP2001031574A (ja) * | 1999-07-16 | 2001-02-06 | Sanmatsu Kogyo Ltd | 血糖値上昇抑制剤 |
US20020065410A1 (en) * | 1999-12-02 | 2002-05-30 | Antrim Richard L. | Branched starches and branched starch hydrolyzates |
DE50210039D1 (de) * | 2001-08-22 | 2007-06-06 | Supramol Parenteral Colloids | Hyperverzweigtes amylopektin zum einsatz in verfahren zur chirurgischen oder therapeutischen behandlung von säugern oder in diagnostizierverfahren, insbesondere zur verwendung als plasmavolumenexpander |
US6929817B2 (en) * | 2002-05-14 | 2005-08-16 | National Starch & Chemical Investment Holding Corporation | Slowly digestible starch product |
FR2840612B1 (fr) * | 2002-06-06 | 2005-05-06 | Roquette Freres | Polymeres solubles de glucose hautement branches et leur procede d'obtention |
AU2003232182A1 (en) * | 2002-06-17 | 2003-12-31 | Novozymes A/S | Methods for producing dextrins using enzymes |
DE10237442B4 (de) * | 2002-08-16 | 2004-08-19 | Fresenius Kabi Deutschland Gmbh | Hochverzweigte, niedrig substituierte Stärkeprodukte |
CA2514551A1 (en) * | 2003-01-28 | 2004-08-12 | Purdue Research Foundation | Slowly digestible starch |
FR2864088B1 (fr) * | 2003-12-19 | 2006-04-28 | Roquette Freres | Polymeres solubles de glucose hautement branches |
-
2006
- 2006-12-29 EP EP06077345A patent/EP1943908A1/en not_active Withdrawn
-
2007
- 2007-12-28 AU AU2007339488A patent/AU2007339488A1/en not_active Abandoned
- 2007-12-28 US US12/521,591 patent/US20100099864A1/en not_active Abandoned
- 2007-12-28 CN CN200780050480A patent/CN101631474A/zh active Pending
- 2007-12-28 EP EP07851966A patent/EP2111123A2/en not_active Withdrawn
- 2007-12-28 JP JP2009543974A patent/JP2010514443A/ja active Pending
- 2007-12-28 WO PCT/NL2007/050708 patent/WO2008082298A2/en active Application Filing
- 2007-12-28 CA CA002674090A patent/CA2674090A1/en not_active Abandoned
- 2007-12-28 BR BRPI0720600-3A2A patent/BRPI0720600A2/pt not_active IP Right Cessation
Cited By (10)
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CN102741296A (zh) * | 2010-02-02 | 2012-10-17 | 罗盖特公司 | 用于腹膜透析的支化的可溶性葡萄糖聚合物 |
CN102741296B (zh) * | 2010-02-02 | 2016-03-02 | 罗盖特公司 | 用于腹膜透析的支化的可溶性葡萄糖聚合物 |
CN106572677A (zh) * | 2014-05-08 | 2017-04-19 | 艾维贝合作公司 | 包含高支化淀粉(hbs)的耐咀嚼糖和用于提供所述耐咀嚼糖的方法 |
WO2019114020A1 (zh) * | 2017-12-11 | 2019-06-20 | 江南大学 | 一种改善淀粉慢消化性能的改性方法 |
WO2019174137A1 (zh) * | 2018-03-16 | 2019-09-19 | 江南大学 | 一种提高淀粉液化产物透明度的方法 |
US11124816B2 (en) | 2018-03-16 | 2021-09-21 | Jiangnan University | Method for improving the transparency of starch liquefaction |
CN108949861A (zh) * | 2018-08-13 | 2018-12-07 | 江南大学 | 一种制备慢消化糊精的方法 |
US11214629B2 (en) | 2018-08-13 | 2022-01-04 | Jiangnan University | Method for preparing short-clustered dextrin |
CN110791541A (zh) * | 2019-10-25 | 2020-02-14 | 江南大学 | 一种降低淀粉消化率的方法及其应用 |
CN115103860A (zh) * | 2019-12-18 | 2022-09-23 | 瑞典淀粉生产者协会 | 转化淀粉和包含所述转化淀粉的食品 |
Also Published As
Publication number | Publication date |
---|---|
WO2008082298A2 (en) | 2008-07-10 |
BRPI0720600A2 (pt) | 2014-03-18 |
EP1943908A1 (en) | 2008-07-16 |
JP2010514443A (ja) | 2010-05-06 |
US20100099864A1 (en) | 2010-04-22 |
EP2111123A2 (en) | 2009-10-28 |
CA2674090A1 (en) | 2008-07-10 |
AU2007339488A1 (en) | 2008-07-10 |
WO2008082298A3 (en) | 2008-08-21 |
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