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The use of biocatalysts, including enzymes and metabolically engineered cells, has attracted a great deal of attention in chemical and bio-industry, because biocatalytic reactions can be conducted under environmentally-benign conditions and in more sustainable ways. The catalytic efficiency and chemo-, regio-, and stereo-selectivity of enzymes can be enhanced and modulated using protein engineering. Metabolic engineering seeks to enhance cellular biosynthetic productivity of target metabolites via controlling and redesigning metabolic pathways using multi-omics analysis, genome-scale modeling, metabolic flux control, and reconstruction of novel pathways. The aim of this Special Issue was to deal with the recent advances in biocatalysis and metabolic engineering for biomanufacturing of biofuels, chemicals, biomaterials, and pharmaceuticals. Reviews and original research articles on the development of new strategies to improve the catalytic efficiency of enzyme, biosynthetic capability of cell factory, and their applications in production of various bioproducts and chemicals have been published. This special issue on “Recent Advances on Biocatalysis and Metabolic Engineering for Biomanufacturing” includes 18 published articles including review and original research papers. Among the research articles presented in this issue, there is a set of studies on enzyme catalysis, which was a powerful tool to effectively synthesize various target products. In more detail, Mulay et al. investigated Candida antarctica Lipase B-catalyzed transesterification of methyl 3-mercaptopropionate with tetraethylene glycol (TEG) and poly(ethylene glycol)s (PEG)s to synthesize thiol-functionalized TEGs and TEGs without use of solvent [1]. Joo et al. reported the biosynthesis ofω-hydroxydodecanoic acid via whole-cell biotransformations using a novel monooxygenase CYP153AL.m from Limnobacter sp. 105 MED [2]. ω-Aminododecanoic acid can be used as Nylon 12 monomers. The biotransformation of dodecanoic acid toω-aminododecanoic acid has been achieved by using an artificial self-sufficient P450, ω-transaminase, and alcohol dehydrogenase, as reported by Ahsan et al. [3]. This issue also covers several studies concerning the characterization of novel enzymes that become more attractive biocatalysts to serve as an alternative platform for chemical synthesis. Senger et al. successfully analyzed the infrared characterization of [NiFe]-hydrogenase from Escherichia coli HYD-2 by in situ attenuated total reflection Fourier-transform infrared spectroscopy which proved as an efficient and powerful technique for the analysis of biological macromolecules and enzymatic small molecule catalysis [4]. Glyoxal oxidase, an extracellular oxidoreductase that oxidizes aldehydes and α-hydroxy carbonyl substrates coupled to the reduction of O2 to H2O2, from Myceliophthora thermophyla, has been characterized by Kadowaki et al. [5]. In addition, hydroxylation mechanism of soluble methane monooxygenase from Methylosinus sporium strain 5, a type II methanotrophs, was reported by Park et al., which revealed that two molar equivalents of methane monooxygenase regulatory protein B (MMOB) are necessary to achieve catalytic activities toward a broad range of substrates including alkanes, alkenes, halogens, and aromatics [6].