Enzymatic interesterification of palm stearin and palm olein blend catalyzed by sn-1,3-specific lipase: interesterification degree, acyl migration, and physical properties

Acyl migration of fatty acid at sn-2 is often observed alongside enzymatic interesterification (EIE), causing the loss of lipase selectivity toward the acyl group at sn-1,3. In this study, an oil blend consisting of palm stearin (PST) and palm olein (POL) was interesterified via a chemical intereste...

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मुख्य लेखकों: Zhen, Zhang, Wan, Jun Lee, Xie, Xiaodong, Ye, Jing, Tan, Chin Ping, Lai, Oi Ming, Li, Aijun, Wang, Yong
स्वरूप: लेख
भाषा:English
प्रकाशित: American Chemical Society 2021
ऑनलाइन पहुंच:http://psasir.upm.edu.my/id/eprint/97123/1/ABSTRACT.pdf
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author Zhen, Zhang
Wan, Jun Lee
Xie, Xiaodong
Ye, Jing
Tan, Chin Ping
Lai, Oi Ming
Li, Aijun
Wang, Yong
author_facet Zhen, Zhang
Wan, Jun Lee
Xie, Xiaodong
Ye, Jing
Tan, Chin Ping
Lai, Oi Ming
Li, Aijun
Wang, Yong
author_sort Zhen, Zhang
collection UPM
description Acyl migration of fatty acid at sn-2 is often observed alongside enzymatic interesterification (EIE), causing the loss of lipase selectivity toward the acyl group at sn-1,3. In this study, an oil blend consisting of palm stearin (PST) and palm olein (POL) was interesterified via a chemical interesterification (CIE) and enzymatic method using a packed bed reactor. Characterization in terms of the triacylglycerol (TAG) compositions, sn-2 fatty acid distributions, and solid fat content profiles was performed. In comparison to that of CIE fats, EIE fats showed different modification effects on the solid fat content. Under similar reaction conditions, different interesterification degrees (IDs) were obtained according to the various blend ratios. Using the same mass ratio of substrates (POL/PST of 9:1), the EIE reaction time and temperature affected the ID and the change in the fatty acyl group at the sn-2 position. Under the reaction time of 46 min, an ID of 94.41% was acquired, while at 80 °C, the degree of acyl migration at sn-2 was 92.87%. EIE with high acyl migration exhibited a lower crystallization rate than that of EIE with low acyl migration. However, the effect of acyl migration on crystal polymorphism and oxidative stability was insignificant. Outcomes from this study are meaningful for the establishment of a theoretical basis for a controlled positional-specific EIE that is catalyzed by sn-1,3-specific lipase.
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spelling upm.eprints-971232022-09-13T08:45:18Z http://psasir.upm.edu.my/id/eprint/97123/ Enzymatic interesterification of palm stearin and palm olein blend catalyzed by sn-1,3-specific lipase: interesterification degree, acyl migration, and physical properties Zhen, Zhang Wan, Jun Lee Xie, Xiaodong Ye, Jing Tan, Chin Ping Lai, Oi Ming Li, Aijun Wang, Yong Acyl migration of fatty acid at sn-2 is often observed alongside enzymatic interesterification (EIE), causing the loss of lipase selectivity toward the acyl group at sn-1,3. In this study, an oil blend consisting of palm stearin (PST) and palm olein (POL) was interesterified via a chemical interesterification (CIE) and enzymatic method using a packed bed reactor. Characterization in terms of the triacylglycerol (TAG) compositions, sn-2 fatty acid distributions, and solid fat content profiles was performed. In comparison to that of CIE fats, EIE fats showed different modification effects on the solid fat content. Under similar reaction conditions, different interesterification degrees (IDs) were obtained according to the various blend ratios. Using the same mass ratio of substrates (POL/PST of 9:1), the EIE reaction time and temperature affected the ID and the change in the fatty acyl group at the sn-2 position. Under the reaction time of 46 min, an ID of 94.41% was acquired, while at 80 °C, the degree of acyl migration at sn-2 was 92.87%. EIE with high acyl migration exhibited a lower crystallization rate than that of EIE with low acyl migration. However, the effect of acyl migration on crystal polymorphism and oxidative stability was insignificant. Outcomes from this study are meaningful for the establishment of a theoretical basis for a controlled positional-specific EIE that is catalyzed by sn-1,3-specific lipase. American Chemical Society 2021 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/97123/1/ABSTRACT.pdf Zhen, Zhang and Wan, Jun Lee and Xie, Xiaodong and Ye, Jing and Tan, Chin Ping and Lai, Oi Ming and Li, Aijun and Wang, Yong (2021) Enzymatic interesterification of palm stearin and palm olein blend catalyzed by sn-1,3-specific lipase: interesterification degree, acyl migration, and physical properties. Journal of Agricultural and Food Chemistry, 69 (32). 9056 - 9066. ISSN 0021-8561; ESSN: 1520-5118 https://pubs.acs.org/doi/abs/10.1021/acs.jafc.0c06297 10.1021/acs.jafc.0c06297
spellingShingle Zhen, Zhang
Wan, Jun Lee
Xie, Xiaodong
Ye, Jing
Tan, Chin Ping
Lai, Oi Ming
Li, Aijun
Wang, Yong
Enzymatic interesterification of palm stearin and palm olein blend catalyzed by sn-1,3-specific lipase: interesterification degree, acyl migration, and physical properties
title Enzymatic interesterification of palm stearin and palm olein blend catalyzed by sn-1,3-specific lipase: interesterification degree, acyl migration, and physical properties
title_full Enzymatic interesterification of palm stearin and palm olein blend catalyzed by sn-1,3-specific lipase: interesterification degree, acyl migration, and physical properties
title_fullStr Enzymatic interesterification of palm stearin and palm olein blend catalyzed by sn-1,3-specific lipase: interesterification degree, acyl migration, and physical properties
title_full_unstemmed Enzymatic interesterification of palm stearin and palm olein blend catalyzed by sn-1,3-specific lipase: interesterification degree, acyl migration, and physical properties
title_short Enzymatic interesterification of palm stearin and palm olein blend catalyzed by sn-1,3-specific lipase: interesterification degree, acyl migration, and physical properties
title_sort enzymatic interesterification of palm stearin and palm olein blend catalyzed by sn 1 3 specific lipase interesterification degree acyl migration and physical properties
url http://psasir.upm.edu.my/id/eprint/97123/1/ABSTRACT.pdf
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