文献检索

查找使用阿拉丁产品的科研文献

检索与阿拉丁产品相关的同行评审论文、DOI、PubMed 编号、期刊、作者、CAS 号及研究领域。

科研影响力快照

与阿拉丁产品相关的已发表科研成果

在搜索之前,这些指标可帮助访客快速了解产品关联科研的规模与质量。

346,364+ SCI 论文 与阿拉丁产品引用相关
2,295,288.15 总影响因子 匹配文献记录中影响因子的总和
81.20 最高期刊影响因子 匹配期刊中的最高 IF
6.63 平均期刊影响因子 匹配文献的平均 IF

参考指标 指标基于阿拉丁文献引用数据库及期刊影响因子记录。文献关联仅供科研参考,请以原始文献为准。

热门产品

视图 列表 网格

4 项

设置提升方向
分支酶
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY · 2022 · IF 5.895

Effect of Starch Primers on the Fine Structure of Enzymatically Synthesized Glycogen-like Glucan

Jialin Liu,Yanli Wang,Xiaoxiao Li,Zhengyu Jin,Birte Svensson,Yuxiang Bai

Glycogen-like glucan (GnG) is a unique hyperbranched polysaccharide nanoparticle which is drawing increasing attention due to its biodegradability and abundant short branches that can be functionalized. Because starch and GnG are both composed of glucose residues and have similar glucosidic bonds, GnG could be fabricated by sucrose phosphorylase, α-glucan phosphorylase, and branching enzymes from starch primers and sucrose. In this study, high-amylose starch, normal starch, and waxy corn starch were used as primers to synthesize GnG, and their impact on the fine structure of GnG was investigated. Structural analysis indicated that with increasing content of amylopectin in the starch primer, the proportion of short chains in GnG decreased, and the degree of β-amylolysis and α-amylolysis was enhanced. Amylose in the primer contributed to a compact and homogeneous structure of GnG, while amylopectin triggered the formation of branch points with a more open distribution. These findings provide a new strategy for regulating the fine structure of GnG.

CAS / MDL: 9048-71-9 9004-54-0
研究领域: 生物化学 · 材料科学
✓ 已验证 产品关联 DOI PubMed 高影响因子
查看原文 查看 PubMed
FOOD HYDROCOLLOIDS · 2024 · IF 11

An efficient approach for the preparation of branched starch through thermophilic glycogen branching enzyme modification

Jing Zhu,Xingfei Li,Cheng Lu,Xing Zhou,Long Chen,Chao Qiu,Zhengyu Jin,Jie Long

Glycogen branching enzymes (GBEs, EC 2.4.1.18) play a crucial role in modifying the starch structure and enhancing its properties. The common approaches to starch modification by GBEs typically involve either fully gelatinization the starch at high temperatures (above 95 °C) and then cooling it before adding the enzymes or directly modifying the starch granules at medium-low temperatures (below 60 °C). However, both of these methods have their limitations. Therefore, in this study, we utilized thermally stable mutant Pyrococcus horikoshii (Ph) OT3 GBEs (The thermally stable Ph GBEs mutant were named as H415W and T508K, respectively) to directly act on an ungelatinized normal corn starch (NCS) emulsion at 70 °C, enabling simultaneous starch swelling and branching modification. The results showed that after modification at 70 °C, the crystalline structure of the starch almost completely disappeared, the short-branched chains increased, and the amylose content, rapid digestibility , and retrogradation enthalpy (ΔH) of the H415W- and T508K-modified starch were reduced by 8.2%, 20.35%, and 4.38 J/g when compared to the NCS. Furthermore, when compared to wild-type (WT)-modified starch (modification conducted at 60 °C), the amylose content, rapid digestibility , and retrogradation enthalpy (ΔH) of the H415W- and T508K-modified starch were reduced by 4%, 11.71% and 1.52 J/g, respectively. The branching efficiency of the starch was enhanced due to the achievement of simultaneous starch swelling and branching modification at 70 °C, resulting in an improved branching efficiency. These findings offer valuable insights for the industrial development of branched starch through enzymatic modification.

CAS / MDL: 8049-47-6 9005-25-8
研究领域: 食品科学 · 生物化学
✓ 已验证 产品关联 DOI 高影响因子
查看原文 查看 PubMed
FOOD CHEMISTRY · 2025 · IF 9.8

Preparation of branched starch by α-amylase and thermophilic glycogen branching enzyme modification

Jing Zhu,Yi Gao,Xingfei Li,Cheng Lu,Xing Zhou,Long Chen,Chao Qiu,Zhengyu Jin,Jie Long

Maltogenic α-amylase (MA, EC 3.2.1.133), which shows high thermal stability, can cleave long starch chains linked by α-1,4 glycosidic bonds. And glycogen branching enzyme (GBE, EC 2.4.1.18) can increase the branching degree of starch. At high temperatures, Elevated temperatures enhanced starch solubilization, improving the accessibility of both MA and GBE to glucan chains. Therefore, ungelatinized normal corn starch (NCS) emulsion (20 % w /w, dry basis) was first pretreated with α-amylase (MA) at 70 °C for 2 h, followed by enzymatic modification using the thermostable Pyrococcus horikoshii OT3 GBE mutants (H415W and T508K) for an additional 10 h modification. The physicochemical properties of the modified starch were determined by scanning electron microscopy and X-ray diffraction, etc. The results demonstrated that the dual enzyme treatment decreased rapid digestibility by 23.07 % and retrograde enthalpy by 5.51 J/g compared to NCS. This study provides guidance for the industrial enzymatic preparation of highly branched starch.

CAS / MDL: 9005-25-8 9002-07-7
研究领域: 食品科学 · 生物技术 · 碳水化合物化学 · 酶学 · 淀粉加工
✓ 已验证 产品关联 DOI PubMed 高影响因子
查看原文 查看 PubMed
CARBOHYDRATE POLYMERS · 2024 · IF 10.7

Synergistic action of novel maltohexaose-forming amylase and branching enzyme improves the enzymatic conversion of starch to specific maltooligosaccharide

Lingli Zhong,Peiwen Wang,Min Jiang,Yitong Zheng,Xiaofan Xu,Xianfeng Ye,Yan Huang,Yanling Ji,Zhongli Cui,Zhoukun Li

As attractive functional ingredients, maltooligosaccharides (MOS) are typically prepared by controlled enzymatic hydrolysis of starch. However, the random attack mode of amylase often leads to discrete product distribution, thereby reducing yields and purities. In this study, a novel glycoside hydrolase family 13 amylase AmyEs from marine myxobacteria Enhygromyxa salina was identified efficient maltohexaose (G6)-forming ability (40 %, w/w). By deciphering external chain length, we found that the high density of α-1,6-branching points benefits the G6 formation of AmyEs with high purity (71–82 %), indicating the substrate selectivity of AmyEs toward high-branched starch. Based on this, asynchronous conversion strategy was designed to enhance specific MOS yield from corn starch by exploiting branching enzymes and AmyEs, and the purity and yield of G6 respectively increased by 9.5 % and 5 % compared to single AmyEs treatment. Our results demonstrate that combinatorial catalysis of MOS-forming amylases and branching enzymes provides a favorable industrial preparation of specific MOS.

研究领域: 生物化学 · 酶学 · 食品科学 · 微生物学
✓ 已验证 DOI PubMed 高影响因子
查看原文 查看 PubMed
已复制

文献关联基于可获得的产品、CAS、DOI 及引用记录。收录不代表作者或出版方对阿拉丁产品的背书,请以原始文献为准。