Purification and Biochemical Characterization of α-Amylase from Newly Isolated Bacillus Cereus Strain and its Application as an Additive in Breadmaking.

Polish journal of microbiology Pub Date : 2025-03-26 eCollection Date: 2025-03-01 DOI:10.33073/pjm-2025-004
Lina S Alhazmi, Wafa A Alshehri
{"title":"Purification and Biochemical Characterization of α-Amylase from Newly Isolated <i>Bacillus Cereus</i> Strain and its Application as an Additive in Breadmaking.","authors":"Lina S Alhazmi, Wafa A Alshehri","doi":"10.33073/pjm-2025-004","DOIUrl":null,"url":null,"abstract":"<p><p>Amylase has numerous applications in the processing food sector, including brewing, animal feed, baking, fruit juice manufacturing, starch syrups, and starch liquefaction. Practical applications have been the primary focus of recent research on novel properties of bacterial α-amylases. Many amylolytic-active bacterial isolates were obtained from samples of organic-rich, salinity-rich soil. Morphological and 16S rRNA gene sequence studies clearly revealed that the organism belongs to <i>Bacillus</i> sp. and was named <i>Bacillus cereus</i> strain GL2 (PP463909.1 (When pH 6.0, 45°C, and 12 hours of incubation were met the optimal growth conditions for the strain produced the highest amount of α-amylase activity. <i>B. cereus</i> strain GL2 α-amylase isoenzyme was purified to homogeneity using Sephacryl™ S-200 chromatography and ammonium sulfate precipitation. The electrophoretic molecular weight of <i>B. cereus</i> α-amylase was 58 kDa. The optimal pH and temperature for measuring α-amylase activity were 50°C and 6.0, respectively. α-Amylase did not change at 50°C. The purified enzyme improves bread texture by reducing stiffness while improving cohesiveness and flexibility. Purified α-amylase was added to the flour, which improved the rheological properties and overall bread quality. As a result, the α-amylase from <i>B. cereus</i> strain GL2 can be used to promote bread-making.</p>","PeriodicalId":94173,"journal":{"name":"Polish journal of microbiology","volume":"74 1","pages":"48-59"},"PeriodicalIF":0.0000,"publicationDate":"2025-03-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11949385/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Polish journal of microbiology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.33073/pjm-2025-004","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/3/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

Amylase has numerous applications in the processing food sector, including brewing, animal feed, baking, fruit juice manufacturing, starch syrups, and starch liquefaction. Practical applications have been the primary focus of recent research on novel properties of bacterial α-amylases. Many amylolytic-active bacterial isolates were obtained from samples of organic-rich, salinity-rich soil. Morphological and 16S rRNA gene sequence studies clearly revealed that the organism belongs to Bacillus sp. and was named Bacillus cereus strain GL2 (PP463909.1 (When pH 6.0, 45°C, and 12 hours of incubation were met the optimal growth conditions for the strain produced the highest amount of α-amylase activity. B. cereus strain GL2 α-amylase isoenzyme was purified to homogeneity using Sephacryl™ S-200 chromatography and ammonium sulfate precipitation. The electrophoretic molecular weight of B. cereus α-amylase was 58 kDa. The optimal pH and temperature for measuring α-amylase activity were 50°C and 6.0, respectively. α-Amylase did not change at 50°C. The purified enzyme improves bread texture by reducing stiffness while improving cohesiveness and flexibility. Purified α-amylase was added to the flour, which improved the rheological properties and overall bread quality. As a result, the α-amylase from B. cereus strain GL2 can be used to promote bread-making.

蜡样芽孢杆菌α-淀粉酶的纯化、生化特性及其在面包添加剂中的应用
淀粉酶在食品加工领域有许多应用,包括酿造、动物饲料、烘焙、果汁制造、淀粉糖浆和淀粉液化。实际应用已成为近年来研究细菌α-淀粉酶新特性的主要焦点。从富含有机物、富含盐分的土壤样品中分离出许多具有解淀粉活性的细菌。形态学和16S rRNA基因序列研究明确该菌属芽孢杆菌属,命名为蜡样芽孢杆菌菌株GL2 (PP463909.1)。当pH为6.0、45℃、培养12 h时,该菌株产生的α-淀粉酶活性最高。采用Sephacryl™S-200层析和硫酸铵沉淀法纯化蜡样芽孢杆菌GL2 α-淀粉酶同工酶。蜡样芽孢杆菌α-淀粉酶的电泳分子量为58 kDa。α-淀粉酶活性测定的最佳pH和温度分别为50℃和6.0℃。α-淀粉酶在50℃时没有变化。纯化后的酶通过降低面包的硬度来改善面包的质地,同时提高面包的粘性和柔韧性。在面粉中加入纯化的α-淀粉酶,改善了面包的流变性能和整体品质。因此,蜡样芽孢杆菌GL2菌株的α-淀粉酶可用于促进面包的制作。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信