CN1019315B - 从含有戊聚糖的小麦和其它谷类淀粉生产葡萄糖浆的方法 - Google Patents
从含有戊聚糖的小麦和其它谷类淀粉生产葡萄糖浆的方法Info
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Abstract
通过用侧孢属处理改善从不纯小麦或其它谷类淀粉中获得的葡萄糖浆的滤过率。通过在分离淀粉前加入木聚糖也可改善淀粉与不纯谷类淀粉的其它成分的分离。
Description
本发明涉及从含有戊聚糖的未纯化的小麦和其它谷类淀粉中制备葡萄糖浆和使这样的淀粉与其它谷类成分,例如谷朊分离。
纤维素和淀粉是碳水化合物最丰富的来源。因为淀粉比纤维素进入人的消化系统要容易得多,所以作为食料它有悠久的历史。它也是一种重要的工业原料。
原则上在酸的催化作用下可使淀粉解聚,但这个途径导致极不完全的解聚和相当大量的副产物的形成。因此淀粉的酸解一直受到日益的关注。
已知天然淀粉含有两种类型由葡萄糖单位组成的大分子。一种类型的分子称为直链淀粉,是线性的并仅由α,1-4连接的葡萄糖单位组成。淀粉含25%的直链淀粉。第二种类型的分子,支链淀粉,是多分支的并含有α,1-4及α,1-6连接的葡萄糖单位。α,1-6键的总含量一般小于5%。
在现代工业淀粉降解中,两种类型的酶都用。α-淀粉酶用于使淀粉液化(或稀化)为平均聚合度约为7-10的糊精,而淀粉葡萄糖苷酶用于最后的糖化作用,结果形成一种高葡萄糖含量(92-96%)的糖浆。
象小麦和大麦这样的谷类含有增加谷类水提取物的粘度和降低谷
类水提取物滤过率的树胶,谷类水提物包含用上述方式制成的葡萄糖浆和精制淀粉本身。这样的树胶主要由谷朊组成,但也含有一些戊聚糖。戊聚糖的结构比通常所显示的具有1,4-β-D-吡喃木糖和单1,2-或1,3-α-L-阿拉伯呋喃糖侧基的长链(阿拉伯糖单位与木糖单位之比为1∶2)的结构更复杂;见附图1,取自于H.Neukom,L.Providoli,H.Gremli and P.A.Jui,Cereal Chem.,44,238(1967)。
戊聚糖的性质随着肽,阿魏酸和阿拉伯半乳聚糖存在与否而变化。由于戊聚糖的高分子量和一些与蛋白和其它成分的相互连锁,总戊聚糖的约2/3是不溶性的。它们有极高的保水力并产生非常大的废滤饼。当可溶性戊聚糖的阿拉伯呋喃糖侧基被水解时,可观察到非取代木聚糖的缔合和沉淀作用。
各种各类的平均戊聚糖含量如下(见“Handbuch der Lebensmittelchemie”,Vol.5,P.32,1967,Springer Verlag):
谷粒 戊聚糖(%干重)
大麦(包括壳) 10.3
小麦 7.4
黑麦 10.6
燕麦(包括壳) 7.5
玉米 6.2
大米 2.0
小米 2.0
为了改进从未纯化的小麦淀粉中得到的葡萄糖浆的滤过率,已做
了用木聚糖酶处理糖浆的尝试。木聚糖酶是一种可水解存在于戊聚糖中的木聚糖的酶。
在Starch 36,135(1984)中,描述的一种真菌起源的β-葡萄糖酶,这种酶具有戊聚糖活性。建议用这种酶处理来自小麦淀粉工业的废水。
英国专利2,150,933号说明书描述了一种通过爱默生青霉的发酵所得到的戊聚糖酶。据说这种酶能够催化木聚糖的降解并且尤其可用于降低淀粉浆的粘度而增进淀粉的回收率。
根据本发明,用下列方法从含有戊聚糖的不纯谷类淀粉中生产具有改进的滤过率和/或较低粘度的葡萄糖浆,该方法包括使上述不纯淀粉受到侧孢属木聚糖酶的作用使戊聚糖水解并受到水解作用使淀粉转化为葡萄糖。
因此从未纯化的小麦淀粉中制备葡萄糖浆可通过用除含α-淀粉酶和/或淀粉葡萄糖苷酶以外也含有侧孢属木聚糖酶的酶混合物水解淀粉得到改进。
也可用木聚糖酶从得自含有戊聚糖的谷类的小麦或其它面粉中回收淀粉,在小麦的湿磨法中,机械地使谷蛋白与其它成分(淀粉浆)分离。淀粉浆分成一个密集的纯化淀粉下层和上层的粘液物。这种含有小淀粉粒,半纤维素和蛋白的粘液部分被称为隔离胶,渣滓或淤渣。半纤维素部分含有木糖(大约60%),阿拉伯糖(大约38%)和葡萄糖(大约2%)。
通过使小麦淀粉浆经过一个连续离心机,生产者可分离较纯的浓缩物或“A”淀粉流,而小谷粒及溶胀的破损谷粒和戊聚糖复合体形成不纯的或“B”淀粉流。在经过连续离心机之前先用侧孢属木聚糖酶预处理小麦淀粉浆,然后通过戊聚糖的水解和渣滓粘度的降低提高“A”
优质淀粉的产率。
用于本发明的木聚糖酶是一种从担子菌纲侧孢属,特别是两型孢侧孢中所获得的木聚糖内切酶,在“真菌学研究”(Studies in Mycology),24,1(1984)中,J.A.Stalpers在“侧孢属的修饰”一文中描述了这种酶。
最好使用从两型孢侧孢取得的木聚糖酶制剂。当使用来自于两型孢侧孢菌株ATCC 24562的木聚糖酶制剂时,可获得非常满意的结果,这种菌株可从美国典型培养物保藏中心获得,它和CBS 484.76菌株是一样的,CBS 484.76菌株可从荷兰,Baarn,霉菌培养物中心获得。这些菌株最适于本发明的目的。
可用于本发明的其它木聚糖酶制剂是具有与能从两型孢侧孢菌株ATCC 24562(或CBS 484.76)中获得的木聚糖酶基本相同特性的酶。包括从含有由上述侧孢属菌株ATCC 24562(或CBS 484.76)产生的木聚糖酶的基因编码的转化宿主微生物中获得的制剂。
通过在含有纤维素,果胶酵母提取物和各种盐的培养基上培养,两型孢侧孢产生一种木聚糖内切酶。木聚糖内切酶可水解戊聚糖链中的1,4-β-木糖键。从技术上看,一般内切型酶更好,因为它可非常迅速地水解高分子量多糖。外切型酶为了达到同样的技术结果需要较长的时间和较高的酶浓度。
在我们同一天提交的基于1985年11月3日的欧洲专利申请85202016.3号的相关的未决专利申请中,揭示了一种测定木聚糖内切酶活性的方法。在此通过参考合并为本申请。
适用于本发明的侧孢属木聚糖酶的浓缩物可用下列方式获得。用已知的方法在一个无菌罐和培养基中进行发酵。培养基含有纤维素,果
胶,酵母提取物和适量的盐。用两型孢侧孢的纯培养物接种。在20℃~37℃,最好是约32℃的恒温下实现发酵作用,PH保持在3.0~6.0范围内,最好是4.0~4.5。可分批或连续发酵。在此过程中伴随着木聚糖酶活性。没有必需通过加入含木聚糖的物质(例如玉米棒或面粉)诱导酶的产生,并且这种产物的增加主要促进木聚糖外切酶的形成,木聚糖外切酶不太适用于本发明。当达到所需的酶活性时,收集麦芽浆,过滤并通过真空浓缩或超滤浓缩。浓缩物可以液体制剂或喷物干燥的粉末形式出售。木聚糖内切酶可水解戊聚糖内的1,4-β-木糖键。
用一种含有±1%木聚糖的底物用粘度测定法研究了未纯化酶产物的性质(见附图2和3)。最适pH为4.7,但在pH3.0~6.0之间相对活性在50%以上。最适温度为55℃,但在65℃相对活性仍为50%以上。Comtat等人研究了这种侧孢属木聚糖酶的纯化(见J.Comtat,K.Ruel,J.-P.Joseleau and F.Barnoud,纤维素酶解专题论文集,S.I.T.R.A.,Helsinki,Finland,351(1975);J.Comtat and J.-P.Joseleau,Carbohydr.Res.,95,101(1981))。
在研究具有内切和外切木聚糖酶活性的酶对由未纯化小麦淀粉制成的葡萄糖浆滤过率的影响时,发现Sumizym AC(来自Shin Nihon的黑曲霉纤维素酶),Drum果胶酶(来自Gist-brocades的黑曲霉drum果胶酶)和侧孢属木聚糖酶活性都很强。用Sumizym AC获得的结果多取决于酶的浓度,而用侧孢属木聚糖酶获得的结果则不然。看来Sumizym AC仅由于其外切酶活性而有效,侧孢属仅由于其内切酶活性而有效。
显然在低浓度下获得侧孢属木聚糖酶的总效力。Drum果胶酶和
Sumizym AC具有大致相同的效力,但Drum果胶酶引起较多的葡萄糖转化。
侧孢属木聚糖内切酶和爱默生青霉木聚糖内切酶可通过增加同样量的来自黑曲霉产物的木聚糖外切酶活性进行比较。爱默生青霉木聚糖酶和木聚糖外切酶混合物的作用比侧孢属木聚糖酶和木聚糖外切酶混合物的作用小。
下列实施例说明本发明。
实施例1
B型小麦淀粉的液化,糖化和
过滤的标准程序
用来自Roquette Freres,参考号为LAB833的B型小麦淀粉作底物,它含有约1.2-1.5%的蛋白质和3-4%的戊聚糖。
A、液化过程
按照下列方法在一个液化试验设备中用含有30%D.S.的井水(160ppm Ca++)使小麦淀粉液化:
在105-106℃下6分钟
在95℃下2小时
我们使用了每克D.S含6单位的Maxamyl,一种来自Gist-Brocades的地衣芽孢杆菌α-淀粉酶。用NaOH将pH校正到6.4。在较高的D.S.下是不可能液化的,因为浆液很粘。
B、糖化过程
将液化淀粉的pH校正到4.2。用25000AGI/KgD.S的Amigase GM(一种来自Gist-Brocades的黑曲霉淀粉葡萄糖苷酶)进行最
初的试验。为了避免淀粉退减作用对过滤试验的干扰选择了这种额外用量。用17500AGI/kg D.S.的常量实现了最终试验。
在糖化开始时将过滤酶和Amigase一起加入。
在60℃下3天以后测试滤过率。
C、过滤试验和分析
使用一种通过水循环维持在60℃,配备有滤布,Dicalite 4258 Sz(Kieselguhr)的Seitz实验室过滤器。在30%D.S下将15g Dicalite 4258 S2分散到150ml葡萄糖浆中形成预涂滤层。在1巴大气压下过滤糖化淀粉并测定每单位时间滤液的体积,从下式可得到滤过率:
15分钟后的滤液体积-1分钟后滤液体积=每分钟滤液的体积
14
过滤后,在20℃用毛细管粘度计测定粘度并且HPLC分析可用于糖的测定。
实施例2
加入侧孢属木聚糖酶
改进液化小麦淀粉的过滤
通过用于玉米淀粉浆的传统方法使含有2-3%戊聚糖的B型小麦淀粉液化,包括具有α-淀粉酶的固体淀粉的1°液化和生成的具有淀粉葡萄糖苷酶的液化淀粉的2°糖化。这样产生一种高葡萄糖含量的浆液。在糖化阶段除淀粉葡萄糖苷酶之外还引入侧孢属木聚糖酶。
在60℃和4.2-4.5的pH下培育3天之后,在标准条件下进行过滤试验。在图4中所给出的结果表明侧孢属木聚糖酶可降低糖浆粘度,从而改进滤过率。
实施例3
侧孢属木聚糖酶和Sumizym AC
对液化B型小麦淀粉过滤的活性
按实施例1的条件,用25000AGI/kg D.S.
酶 %D.S.的用量 每分钟滤液体积
空白(只有AG) - 7.8ml
侧孢属木聚糖酶
稀释到500u/g 0.05 15.6ml
稀释到500u/g 0.1 15.2ml
稀释到500u/g 0.2 16.3ml
Sumizym AC 0.005 15.3ml
Sumizym AC 0.01 18.3ml
Sumizym AC 0.02 21.8ml
Sumizym AC 0.05 24.5ml
用Sumizym AC所获得的结果大大取决于酶的浓度,
但用侧孢属木聚糖苷酶所获得的结果则不然。
实施例4
侧孢属木聚糖酶+Sumizym或Drum
果胶酶混合物对液化B型
小麦淀粉的活性
按实施例1的条件,用25000AGI/kg D.S.
第一种酶 D.S.用量% 第二种酶 D.S.用量% 每分钟滤液体积
空白 - - - 7.5ml
稀释到
500u/g
的侧孢属
木聚糖酶 0.005 - - 12.9ml
0.01 - - 14.0ml
0.02 - - 14.8ml
0.05 - - 15.5ml
0.05 Sumizym AC 0.005 18.5ml
″ 0.01 21.0ml
″ 0.02 20.8ml
″ Drum果胶酶 0.005 17.8ml
″ 0.01 20.5ml
″ 0.02 21.4ml
在低浓度下可获得侧孢属木聚糖酶的总效力。与这种木聚糖内切酶一起使用时,来自Drum果胶酶和Symizym AC的木聚糖外切酶具有大致相同的效力,但Drum果胶酶可引起更多的葡萄糖转化。
实施例5
在液化B型小麦淀粉过滤时
侧孢属木聚糖酶+Sumizym AC
或Drum果胶酶混合物的
葡萄糖产量和活性
按实施例1的条件,用25000AGI/kg D.S.
第一种酶 D.S. 第二种酶 D.S. 每分钟滤 粘度 葡萄糖产量
用量% 用量% 液体积 (mpa/s) (%)
(ml)
空白 - - - 6.40 6.8 -
(用AG)
稀释到
500u/g
的侧孢属
木聚糖酶 0.01 - - 11.20 4.45 -
″ ″ Drum 0.005 14.80 3.71 91.49
果胶酶
″ ″ ″ 0.075 15.20 3.72 90.67
″ ″ ″ 0.01 16.4 3.71 90.40
″ ″ ″ 0.0125 16.8 3.69 90.02
″ ″ Sumi- 0.01 17.5 3.59 91.96
zym AC
这个试验进一步证实对Drum果胶酶的葡萄糖产量的高的转化作用。为了比较与Sumizym AG一起进行试验。
实施例6
同样增加木聚糖外切酶活性的
侧孢属木聚糖酶和爱默生青霉
β-葡聚糖酶的活性
第一种酶 D.S. 第二种酶 D.S. 每分钟滤 粘度 葡萄糖产量
用量% 用量% 液体积 (mpa/s) (%)
(ml)
空白 - - - 3.5 6.83 93.13
(用AG)
稀释到
500u/g
的侧孢属
木聚糖酶 0.01 - - 9.9 4.40 92.17
Drum 0.005 15.2 4.22 90.97
果胶酶
″ ″ Sumi- 0.0035 15.4 4.12 91.58
zym AC
爱默生
青霉β-
葡聚糖酶 0.02 - - 9.0 4.67 92.28
Drum
″ ″ 果胶酶 0.005 11.7 4.35 90.96
Sumi- 0.0035 11.8 4.22 91.74
″ ″ zym AC
这些试验表明与侧孢属木聚糖酶+木聚糖外切酶混合物比较爱默生青霉β-葡聚糖酶木聚糖内切酶+木聚糖外切酶混合物的较低的协同作用。
Claims (3)
1、由含有戊聚糖的不纯谷类淀粉生产具有改进的滤过率和/或较低的粘度的葡萄糖浆的方法,该方法包括使所述不纯的谷物淀粉受到两型孢侧孢木聚糖酶和α-淀粉酶和/或淀粉葡萄糖苷酶的作用使戊聚糖水解并且经水解作用使淀粉转化为葡萄糖。
2、按照权利要求1的方法,其中所述木聚糖酶得自于两型孢侧孢ATCC24562。
3、按照权利要求1或2的方法,其中木聚糖酶与黑曲霉木聚糖外切酶混合使用。
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EP (1) | EP0228732B1 (zh) |
JP (1) | JPH074181B2 (zh) |
KR (1) | KR950000444B1 (zh) |
CN (1) | CN1019315B (zh) |
AT (1) | ATE50599T1 (zh) |
CA (1) | CA1272150A (zh) |
DE (1) | DE3669176D1 (zh) |
DK (1) | DK171881B1 (zh) |
ES (1) | ES2013994B3 (zh) |
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US5320960A (en) * | 1992-04-03 | 1994-06-14 | Genencor International, Inc. | Method of preparing solution enriched in xylanase using low molecular weight alcohol, organic salt and inorganic salt |
US5472864A (en) * | 1984-04-19 | 1995-12-05 | Genencor International, Inc. | Method of preparing solution enriched in EG III using low molecular weight alcohol, organic salt and inorganic salt |
CA1280704C (en) * | 1985-12-03 | 1991-02-26 | Paul Ducroo | Production of beer |
US4973581A (en) * | 1987-02-20 | 1990-11-27 | Ajinomoto Company, Inc. | Glucan derivatives having tumoricidal activity |
BE1002740A6 (nl) * | 1989-01-09 | 1991-05-21 | Amylum | Werkwijze voor het afscheiden van zetmeel uit een reststroom van de zetmeelbereiding en aldus verkregen zetmeel. |
US5200215A (en) * | 1988-04-20 | 1993-04-06 | Nabisco, Inc. | Enzyme treated low moisture content comestible products |
US5035902A (en) * | 1989-06-12 | 1991-07-30 | Labatt Brewing Company Limited | Foam stabilizing proteinase |
AT394730B (de) * | 1990-05-08 | 1992-06-10 | Voest Alpine Ind Anlagen | Verfahren zur herstellung exo- und endocellulasefreier xylanase |
CH683843A5 (fr) * | 1992-03-10 | 1994-05-31 | Brasserie Du Cardinal Fribourg | Procédé de fabrication d'une bière sans alcool ayant les propriétés organoleptiques d'une bière blonde de type lager. |
US5665585A (en) * | 1992-09-03 | 1997-09-09 | Alko-Yhiot Oy | Recombinant production of glucoamylase P in trichoderma |
EP0941359A1 (en) * | 1996-11-21 | 1999-09-15 | Novo Nordisk A/S | Use of carbohydrate-binding domain in starch processing |
US6031155A (en) * | 1997-06-05 | 2000-02-29 | Cameron-Mills; Verena | Arabinoxylan degradation |
EP1392815B1 (en) * | 2001-02-21 | 2013-06-26 | Syngenta Participations AG. | Enzymes having alpha amylase activity and methods of use thereof |
US20040115779A1 (en) * | 2002-03-19 | 2004-06-17 | Olsen Hans Sejr | Fermentation process |
AU2004254640B2 (en) | 2003-07-02 | 2010-08-26 | Bp Corporation North America Inc. | Glucanases, nucleic acids encoding them and methods for making and using them |
US20070148741A1 (en) | 2003-12-19 | 2007-06-28 | Novozymes A/S | Mashing process |
WO2005118769A1 (en) * | 2004-06-03 | 2005-12-15 | Novozymes A/S | Mashing process and enzyme composition useful therein |
MX369001B (es) | 2006-08-04 | 2019-10-24 | Basf Enzymes Llc | Glucanasas, acidos nucleicos que las codifican, y metodos para hacerlas y usarlas. |
DE102008060446A1 (de) * | 2008-12-04 | 2010-06-10 | Krones Ag | Verfahren zum Ermitteln der Filtrierbarkeit von Bier |
CN110511946A (zh) | 2012-03-30 | 2019-11-29 | 巴斯夫爱酶孜有限公司 | 编码纤维素酶的基因 |
GB201308853D0 (en) | 2013-03-12 | 2013-07-03 | Verenium Corp | Genes encoding xylanase |
WO2019116182A1 (en) | 2017-12-15 | 2019-06-20 | Nestec S.A. | Process for sugar modulation |
CN113136274A (zh) * | 2021-03-31 | 2021-07-20 | 内蒙古燕谷坊全谷物产业发展有限责任公司 | 一种燕麦啤酒的制备方法 |
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US2821501A (en) * | 1953-12-08 | 1958-01-28 | Ca Nat Research Council | Recovery of starch |
US3366483A (en) * | 1966-09-26 | 1968-01-30 | Baxter Laboratories Inc | Chillproofing fermented malt beverages with extracts of the growth products of mold microorganisms |
GB1446203A (en) * | 1973-02-28 | 1976-08-18 | Novo Industri As | Preparation of an enzyme product |
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CA1272150A (en) | 1990-07-31 |
JPH074181B2 (ja) | 1995-01-25 |
CN86108125A (zh) | 1987-08-12 |
FI864898A0 (fi) | 1986-12-01 |
FI93859C (fi) | 1995-06-12 |
ATE50599T1 (de) | 1990-03-15 |
FI864898A (fi) | 1987-06-04 |
KR870006076A (ko) | 1987-07-09 |
IE59504B1 (en) | 1994-03-09 |
DE3669176D1 (de) | 1990-04-05 |
DK578686D0 (da) | 1986-12-02 |
DK578686A (da) | 1987-06-04 |
DK171881B1 (da) | 1997-07-28 |
GR3000462T3 (en) | 1991-06-28 |
US4746517A (en) | 1988-05-24 |
EP0228732A1 (en) | 1987-07-15 |
PT83861A (en) | 1987-01-01 |
JPS62259554A (ja) | 1987-11-11 |
KR950000444B1 (ko) | 1995-01-20 |
EP0228732B1 (en) | 1990-02-28 |
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