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Lysosomal Hydrolases

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Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...

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Spray Dried Lysozyme Microspheres: Morphological Evolution and Enzymatic Activity Retention.

Mengyuan Li¹, Shen Yan², Shengyu Zhang¹

¹Engineering Research Centre of Advanced Powder Technology, School of Chemical and Environmental Engineering, College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou, Jiangsu Province, 215123, PR China.

Pharmaceutical Research

|July 1, 2026

Summary

This study fabricated uniform lysozyme microspheres using micro-fluidic spray drying. Excipients like trehalose and dextran T40 modulated enzyme structure and activity, enabling predictable enzyme powder design.

Keywords:

carbohydrate excipients lysozyme particle formation spray drying structure–activity relationship

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Area of Science:

Biotechnology
Materials Science
Enzymology

Background:

Conventional spray drying yields heterogeneous enzyme powders, hindering mechanistic studies.
Understanding particle formation and structure-activity relationships is crucial for enzyme applications.

Purpose of the Study:

Fabricate uniform lysozyme microspheres using micro-fluidic jet spray drying.
Investigate how formulation excipients and drying conditions impact microsphere microstructure and enzymatic activity.

Main Methods:

Employed a micro-fluidic jet spray dryer for uniform lysozyme microsphere preparation.
Systematically evaluated effects of carbohydrate excipients and drying temperature on morphology, structure, and activity.

Main Results:

Pure lysozyme microspheres exhibited uniform morphology but lost activity due to drying stress.
Carbohydrate excipients influenced structural evolution; trehalose stabilized structure, while dextran T40 hindered aggregation.
Mannitol induced phase separation and enzyme inactivation, while trehalose formed a protective glassy matrix.

Conclusions:

Established a formulation-process-microstructure-activity relationship for spray-dried enzyme powders.
Demonstrated the potential for rational design of predictable enzyme powders with controlled properties.