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采用响应面法优化喷雾干燥法包封勒姆鲁鱼蛋白水解物的工艺

Optimization of the Encapsulation of Lemuru Fish Protein Hydrolysate by Spray-Drying Using Response Surface Methodology.

作者信息

Hanifah Ayu, Kosasih Wawan, Ratnaningrum Diah, Andriani Dian, Putra Herlian Eriska, Yelliantty Yellianty, Priatni Sri

机构信息

Research Center for Applied Microbiology, National Research and Innovation Agency Republic of Indonesia, Jl. Raya Jakarta-Bogor Km, 46, Cibinong, Bogor, Jawa Barat 16911, Indonesia.

Directorate of Laboratory Management, Research Facilities and Science and Technology areas, KST Samaun Samadikun, Gd Basics Tw 1, Lt 1, Cisitu-Sangkuriang, Bandung 40135, Indonesia.

出版信息

Food Technol Biotechnol. 2025 Mar;63(1):83-93. doi: 10.17113/ftb.63.01.25.8626.

DOI:10.17113/ftb.63.01.25.8626
PMID:40322287
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12044295/
Abstract

RESEARCH BACKGROUND

Encapsulating lemuru fish protein hydrolysate is important to maintain its stability. However, optimal conditions for the encapsulation process of lemuru fish protein hydrolysate using statistical methods remain unexplored. This study aims to address this problem by optimizing the encapsulation conditions.

EXPERIMENTAL APPROACH

Maltodextrin and gum Arabic were used as carrier agents, with mass per volume ratio ranging from 10 to 30 %, and spray dryer inlet temperatures between 90 and 100 °C. In this study, we analysed the main interactions of these variables using response surface methodology (RSM).

RESULTS AND CONCLUSIONS

Our results show that mass per volume ratio of maltodextrin of 25 % and inlet temperature of 100 °C are the optimal conditions for the encapsulation of fish protein hydrolysate. The optimal conditions resulted in a high desirability index of 0.864, indicating an effective balance between yield, solubility and hygroscopicity. The actual results also fall well within the confidence interval of the predicted values, confirming the robustness of the model and the reliability of the predicted optimal encapsulation conditions. Encapsulated fish protein hydrolysate was compared with its non-encapsulated counterpart and characterised using Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM), and particle size analyser (PSA) to validate the results. The encapsulated fish protein hydrolysate showed distinct properties, such as the presence of functional groups from maltodextrin, interconnected particle and more homogeneous and narrower particle size distribution.

NOVELTY AND SCIENTIFIC CONTRIBUTION

The encapsulation of lemuru fish protein hydrolysate using maltodextrin with mass per volume ratio of 25 % and inlet temperature 100 °C was successful in improving the properties of the protein hydrolysate. Further research should explore the functional properties of fish protein hydrolysate.

摘要

研究背景

包封勒穆鲁鱼蛋白水解物对于维持其稳定性很重要。然而,使用统计方法确定勒穆鲁鱼蛋白水解物包封过程的最佳条件仍未得到探索。本研究旨在通过优化包封条件来解决这一问题。

实验方法

使用麦芽糊精和阿拉伯胶作为载体,体积质量比范围为10%至30%,喷雾干燥器入口温度为90至100°C。在本研究中,我们使用响应面法(RSM)分析了这些变量的主要相互作用。

结果与结论

我们的结果表明,麦芽糊精体积质量比为25%且入口温度为100°C是鱼蛋白水解物包封的最佳条件。最佳条件导致了0.864的高可取性指数,表明在产率、溶解度和吸湿性之间实现了有效平衡。实际结果也很好地落在预测值的置信区间内,证实了模型的稳健性和预测的最佳包封条件的可靠性。将包封的鱼蛋白水解物与其未包封的对应物进行比较,并使用傅里叶变换红外光谱(FTIR)、扫描电子显微镜(SEM)和粒度分析仪(PSA)进行表征以验证结果。包封的鱼蛋白水解物表现出不同的特性,例如存在来自麦芽糊精的官能团、相互连接的颗粒以及更均匀和更窄的粒度分布。

新颖性与科学贡献

使用体积质量比为25%的麦芽糊精和入口温度为100°C成功包封勒穆鲁鱼蛋白水解物,改善了蛋白水解物的性质。进一步的研究应探索鱼蛋白水解物的功能特性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/4bdbf29a981e/FTB-63-83-fS1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/783e15955f70/FTB-63-83-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/cb99f323b68a/FTB-63-83-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/9a85bc77ce38/FTB-63-83-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/7c168217afdb/FTB-63-83-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/07d65db92427/FTB-63-83-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/c77bf7ad4725/FTB-63-83-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/4bdbf29a981e/FTB-63-83-fS1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/783e15955f70/FTB-63-83-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/cb99f323b68a/FTB-63-83-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/9a85bc77ce38/FTB-63-83-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/7c168217afdb/FTB-63-83-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/07d65db92427/FTB-63-83-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/c77bf7ad4725/FTB-63-83-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0eaa/12044295/4bdbf29a981e/FTB-63-83-fS1.jpg

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