耐盐米曲霉制曲及复合酶分泌条件的研究

该文研究了耐盐米曲霉制曲的产酶特性,并且通过对耐盐米曲霉在不同作用条件下制得的曲料的蛋白酶活力和淀粉酶活力的变化分析,探讨了不同原料配比、水分添加量、制曲温度和蒸料时间等因素对耐盐米曲霉制曲效果的影响,为米曲霉在工业生产中的研究和应用提供理论依据.研究表明,耐盐米曲霉制曲产生的中性蛋白酶和碱性蛋白酶的酶活较高,酸性蛋白酶和淀粉酶酶活较低.复合酶分泌的最佳工艺条件为:原料配比为豆粕:麸皮=2:3,加水量为120％,蒸料时间为30min,30℃制曲42h,此条件下酸性蛋白酶和淀粉酶活力有明显的提高.     

淀粉酶废液在酒精生产中的应用研究

将中温α-淀粉酶和糖化酶的发酵废液添加到利用木薯粉生产酒精中,通过实验研究酶废液的添加对酒精产量以及对发酵过程中酿酒酵母的影响.实验证明,添加酶废液可以提高0.6％的酒精产量;在酒精发酵过程中,对酵母生长的负作用不明显.     

松香基功能高分子稀土离子配合物固定化淀粉酶

分别以聚马来松香己二醇酯、马来松香乙二醇丙烯酯聚合物和马来松香乙二醇丙烯酯- 丙烯酸共聚物为载体,稀土离子为桥键配离子固定化淀粉酶。测定固定化淀粉酶的性能,探讨固定化酶反应机理。结果表明,稀土离子作为桥键配离子的固定化淀粉酶中,PMGAE Y(III)En 和PMGAEDy(III)En 效果较好;最适宜温度均为60℃,最适宜pH 值均为6.03;重复使用4 次后,活性分别为31.49、29.76mg/g·5min。此外,建立了固定化酶活性与功能高分子微孔面积及酸值间的数学关系式。     

PS0312 菌株发酵产淀粉酶及温度与pH 值对酶活力的影响

PS0312 菌株是具有特殊生物学特性的青霉菌株。以三角瓶固体培养研究不同条件与菌株产淀粉酶的关系,以及温度与pH 值对酶活力的影响。结果表明：PS0312 菌株以麸皮30.04%、大豆饼粉3.70%、谷壳3.70% 及55.56% 蒸馏水组成的培养基固体发酵湿麸曲淀粉酶产量最高。单因子试验结果表明：以培养基pH3、108 个/mL的种子液接种量1.85%、培养温度28℃、培养时间96h 产淀粉酶量最大。PS0312 菌株产淀粉酶在pH2.0～10.0 内具较高活性,酶活大小与pH 值的关系成双峰形;pH3 的条件下酶活性最高,相对酶活100%;pH9 的条件下酶活次之,相对酶活84.98%。酶反应最适温度为60℃,90℃条件下相对酶活为39.06%。研究表明：PS0312 菌株发酵产淀粉酶是一种在强酸、强碱条件下都具有较高的酶活性和耐高温的特殊的酸性、中温淀粉酶,可在较宽的温度与pH 值范围下应用。     

鲫鱼肠道细菌菌群初步分析

从健康鲫鱼肠道分离出62 株细菌菌株,革兰氏染色分析结果表明,其中18 株为革兰氏阳性菌株,44 株为革兰氏阴性菌株。实验分析各菌株产纤维素酶和产淀粉酶的情况。筛选到26 株产淀粉酶菌株,占筛选菌株的41.94%,没有从鲫鱼肠道内筛选到产纤维素酶菌株。使用16S rDNA 基因序列检测,确定相关菌株分别属于Aeromonas、Shewanella、Pseudomonas 等。分析产酶活性较高的菌株F2 的致病性和产酶活力,确定其不是鲫鱼致病菌,其分泌性淀粉酶在pH7、温度32℃时表现出最大酶活力。     

A review of malting and malt processing for whisky distillation

This paper encompasses a re‐evaluation of published literature and data regarding wort attenuation in malt distilleries raising questions and discussing how the conventional wisdom has changed over time and what questions still need to be answered. Current knowledge is summarized in the following four points: (a) Under normal malting conditions, starch granules are partially degraded by a combination of α‐amylase and α‐glucosidase. This complex can open up the granule at specific sites on the surface and create characteristic ‘pin‐hole’ lesions, which may be widened by secondary hydrolysis by α‐ and β‐amylase, limit dextrinase and α‐glucosidase (maltase). (b) All of these diastatic enzymes can survive mild kilning, probably by forming heat stable complexes on and within the starch granules and can continue a complete degradation of starch when mashed at ambient temperatures with glucose as the end product. (c) At normal mashing temperatures, starch granules gelatinize and dissolve with a concomitant rapid degradation to glucose, maltose, maltotriose and dextrins ranging from degree of polymerization (DP) 4 to > DP20. If there is immediate wort boiling after run‐off, this is the final composition of starch derived carbohydrates according to the conventional paradigm. (d) All malt worts also contain a small amount of panose, isopanose as well as glucosyl maltodextrins, based on a core of 6₂‐α‐glucosyl maltose (panose) or 6‐α‐maltosyl glucose (isopanose), which are remnants of the α‐amylase/glucosidase degradation of granular starch. These dextrins are resistant to the action of debranching enzymes and their concentration may vary between 4 and 8% of the malt extract, depending on the degree of modification of the host starch granules. They may be created at the active sites of this enzyme complex when the granule is gelatinized. In a conventional mash of unboiled distilling wort, the spectrum of wort dextrins produced from gelatinized starch is reduced to true ‘limit’ dextrins of DP4–8 by continued α‐amylolysis during early fermentation. These dextrins will contain side chains of either maltose or maltotriose residues surrounding the α‐1,6‐glucosidic linkage and can be debranched by limit dextrinase during late fermentation, leaving only the above glucosyl maltodextrins dextrins in the spent wash. Copyright © 2016 The Institute of Brewing & Distilling     

He-Ne激光和NTG复合诱变米曲霉提高其蛋白酶和淀粉酶酶活力

以分离自豆酱中的米曲霉(Aspergillus oryzae)HDF-C14为出发菌株,采用He-Ne激光和亚硝基胍复合诱变的方法获得高产蛋白酶和淀粉酶的突变株HDF-C14-HN5,并将其应用到豆酱发酵中,测定酱曲发酵时蛋白酶和淀粉酶的酶活力。所得成曲中干基蛋白酶酶活力最高可达1572.64U/g,淀粉酶酶活力最高可达2815.23U/g。此生产性发酵实验可以为该菌株投入工业化生产提供技术支撑。     

PLG-007 and Its Active Component Galactomannan-α Competitively Inhibit Enzymes That Hydrolyze Glucose Polymers

PLG-007 is a developmental therapeutic compound that has been clinically shown to reduce the magnitude of postprandial glucose excursions and has the potential to be an adjunct treatment for diabetes and inflammatory-related diseases. The present investigation is aimed at understanding the molecular mechanism of action of PLG-007 and its galactomannan (GM) components GMα and GMβ (in a 1:4 mass ratio, respectively) on enzyme (i.e., α-amylase, maltase, and lactase) hydrolysis of glucose polymers using colorimetric assays and ¹³C HSQC NMR spectroscopy. The starch–iodine colorimetric assay indicated that GMα strongly inhibits α-amylase activity (~16-fold more potent than GMβ) and thus is the primary active component in PLG-007. ¹³C HSQC experiments, used to follow the α-amylase-mediated hydrolysis of starch and amylopectin, further demonstrate the α-amylase inhibitory effect of GMα via α-amylase-mediated hydrolysis of starch and amylopectin. Maltohexaose (MT6) was used to circumvent the relative kinetic complexity of starch/amylopectin degradation in Michaelis–Menten analyses. The V_max, K_M, and K_i parameters were determined using peak volume integrals from ¹³C HSQC NMR spectra. In the presence of PLG-007 with α-amylase and MT6, the increase in K_M from 7.5 ± 0.6 × 10⁻³ M (control) to 21 ± 1.4 × 10⁻³ M, with no significant change in V_max, indicates that PLG-007 is a competitive inhibitor of α-amylase. Using K_M values, K_i was estimated to be 2.1 ± 0.9 × 10⁻⁶ M; however, the microscopic K_i value of GMα is expected to be larger as the binding stoichiometry is likely to be greater than 1:1. Colorimetric assays also demonstrated that GMα is a competitive inhibitor of the enzymes maltase and lactase. Overall, this study provides insight as to how PLG-007 (GMα) is likely to function in vivo.     

响应面法优化荸荠的酶解条件

采用α-淀粉酶对荸荠进行酶解,在单因素试验基础上,以荸荠汁中可溶性固含物含量为评价指标,通过响应面法优化酶解条件。结果表明,淀粉酶用量0.17%,酶解温度52℃,酶解2.29 h,荸荠酶解液可溶性固形物达到1.88%,出汁率达到91.23%。